PMID- 14695190
OWN - NLM
STAT- in-process
DA  - 20031225
IS  - 0008-5472
VI  - 63
IP  - 24
DP  - 2003 Dec 15
TI  - High heparanase activity in multiple myeloma is associated with elevated
      microvessel density.
PG  - 8749-56
AB  - Heparanase is an enzyme that cleaves heparan sulfate chains of
      proteoglycans, and its expression has been associated with increased
      growth, metastasis, and angiogenesis of some tumors. Because myeloma tumor
      cells express high levels of the syndecan-1 heparan sulfate proteoglycan
      and because these tumors grow as highly vascularized aggregates within the
      bone marrow, we analyzed the activity, expression, and function of
      heparanase in myeloma patients. Analysis of heparanase activity in the
      plasma isolated from bone marrow biopsies of 100 patients reveals 86
      positive for heparanase activity and 14 negative. The bone marrow samples
      can be further divided into three categories of heparanase activity, high
      activity (42 patients), low activity (44 patients), and negative (14
      patients). In contrast to the bone marrow plasma, levels of heparanase
      activity in peripheral blood plasma of 29 myeloma patients were either
      negative or low, suggesting that in multiple myeloma, heparanase functions
      in the local microenvironment of the bone marrow and its activity is not
      significantly elevated systemically. Immunohistochemistry reveals that
      patients with high levels of heparanase activity often have tumor cells
      with intense staining for the enzyme. Interestingly, a marked
      heterogeneity among tumor cells was noted, with clusters of heavily
      stained cells surrounded by cells with weak or negative staining for
      heparanase. Analysis of microvessel density reveals a strikingly higher
      concentration of vessels in patients with high heparanase activity (78.96
      vessels/mm(2)) as compared with patients negative for heparanase activity
      (25.03 vessels/mm(2)). When human myeloma cells transfected with the cDNA
      for heparanase are implanted in severe combined immunodeficient (SCID)
      mice, the resulting tumors exhibited a significantly higher microvessel
      density than did tumors established with control cells. Thus, expression
      of heparanase appears to play a direct role in enhancing microvessel
      density in these myeloma tumors. Because heparanase is known to stimulate
      angiogenesis, and because high microvessel density is associated with poor
      prognosis in myeloma, we conclude that heparanase expression likely plays
      an important role in regulating the growth and progression of myeloma, and
      that therapies designed to block heparanase activity may aid in
      controlling this cancer.
AD  - Departments of Pathology, Myeloma Institute for Research and Therapy,
      Arkansas Cancer Research Center, University of Arkansas for Medical
      Sciences, Little Rock, Arkansas 72205-7199, USA. KellyThomasJ@uams.edu
FAU - Kelly, Thomas
AU  - Kelly T
FAU - Miao, Hua-Quan
AU  - Miao HQ
FAU - Yang, Yang
AU  - Yang Y
FAU - Navarro, Elizabeth
AU  - Navarro E
FAU - Kussie, Paul
AU  - Kussie P
FAU - Huang, Yan
AU  - Huang Y
FAU - MacLeod, Veronica
AU  - MacLeod V
FAU - Casciano, Jonathan
AU  - Casciano J
FAU - Joseph, Lija
AU  - Joseph L
FAU - Zhan, Fenghuang
AU  - Zhan F
FAU - Zangari, Maurizio
AU  - Zangari M
FAU - Barlogie, Bart
AU  - Barlogie B
FAU - Shaughnessy, John
AU  - Shaughnessy J
FAU - Sanderson, Ralph D
AU  - Sanderson RD
LA  - eng
GR  - CA55819/CA/NCI
GR  - CA68494/CA/NCI
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JID - 2984705R
SB  - IM
EDAT- 2003/12/26 05:00
MHDA- 2003/12/26 05:00
PST - ppublish
SO  - Cancer Res 2003 Dec 15;63(24):8749-56.

PMID- 14690462
OWN - NLM
STAT- in-data-review
DA  - 20031223
IS  - 0303-6987
VI  - 31
IP  - 2
DP  - 2004 Feb
TI  - Immunolabeling pattern of syndecan-1 expression may distinguish pagetoid
      Bowen's disease, extramammary Paget's disease, and pagetoid malignant
      melanoma in situ.
PG  - 169-73
AB  - The differential diagnosis of pagetoid cells within the epidermis rests
      primarily between pagetoid Bowen's disease (PBD), extramammary Paget's
      disease (EPD), and pagetoid malignant melanoma (MIS) in situ. Although
      morphologic clues are often helpful in differentiating these lesions, the
      use of immunohistochemistry is often necessary to arrive at the correct
      diagnosis. Syndecan-1 is a cell-surface proteoglycan that mediates
      adhesion between cells and the extracellular matrix, and between cells
      themselves. Twenty-two cases of PBD, four cases of intraepidermal EPD, and
      13 cases of MIS were examined for syndecan-1 immunoreactivity.
      Cell-membrane syndecan-1 immunoreactivity was evident in PBD, cytoplasmic
      syndecan-1 immunoreactivity was evident in EPD, whereas immunoreactivity
      for syndecan-1 was not present in MIS. The patterns of syndecan-1
      immunoreactivity in these lesions may be a useful adjunct in the
      differentiation of PBD, EPD, and MIS.
AD  - Marshfield Clinic, Marshfield, WI, and Baylor College of Medicine,
      Houston, TX, USA.
FAU - Bayer-Garner, Ilene B
AU  - Bayer-Garner IB
FAU - Reed, Jon A
AU  - Reed JA
LA  - eng
PT  - Journal Article
PL  - Denmark
TA  - J Cutan Pathol
JID - 0425124
SB  - IM
EDAT- 2003/12/24 05:00
MHDA- 2003/12/24 05:00
AID - 164 [pii]
PST - ppublish
SO  - J Cutan Pathol 2004 Feb;31(2):169-73.

PMID- 14685171
OWN - NLM
STAT- completed
DA  - 20031219
DCOM- 20040121
IS  - 1471-0072
VI  - 4
IP  - 12
DP  - 2003 Dec
TI  - Syndecans: proteoglycan regulators of cell-surface microdomains?
PG  - 926-37
AD  - Division of Biomedical Sciences, Faculty of Medicine, Imperial College
      London, Exhibition Road, London SW7 2AZ, UK. j.couchman@imperial.ac.uk
FAU - Couchman, John R
AU  - Couchman JR
LA  - eng
PT  - Journal Article
PT  - Review
PT  - Review, Tutorial
PL  - England
TA  - Nat Rev Mol Cell Biol
JID - 100962782
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Phosphatidylinositol 4,5-Diphosphate)
RN  - 0 (Proteoglycans)
RN  - 0 (Thrombospondin 1)
RN  - 0 (syndecan)
SB  - IM
MH  - Animals
MH  - Body Patterning
MH  - Cytoskeleton/metabolism
MH  - Dimerization
MH  - Focal Adhesions/metabolism
MH  - Membrane Glycoproteins/chemistry/genetics/*metabolism
MH  - Membrane Microdomains/chemistry/*metabolism
MH  - Models, Molecular
MH  - Multigene Family
MH  - Phosphatidylinositol 4,5-Diphosphate/metabolism
MH  - Proteoglycans/chemistry/genetics/*metabolism
MH  - Support, Non-U.S. Gov't
MH  - Thrombospondin 1/metabolism
RF  - 111
EDAT- 2003/12/20 05:00
MHDA- 2004/01/22 05:00
AID - 10.1038/nrm1257 [doi]
AID - nrm1257 [pii]
PST - ppublish
SO  - Nat Rev Mol Cell Biol 2003 Dec;4(12):926-37.

PMID- 14681683
OWN - NLM
STAT- completed
DA  - 20031218
DCOM- 20040121
IS  - 0950-9232
VI  - 22
IP  - 58
DP  - 2003 Dec 18
TI  - Mammary gland development requires syndecan-1 to create a
      beta-catenin/TCF-responsive mammary epithelial subpopulation.
PG  - 9243-53
AB  - Mice with a null mutation in the cell surface heparan sulfate (HS)
      proteoglycan, syndecan-1 (Sdc1), develop almost normally, but resist
      mammary tumor development in response to Wnt-1. Here, we test the
      hypothesis that Sdc1 promotes Wnt-1-induced tumor development by
      interacting with the Wnt cell surface signaling complex. Thus, the
      response of Sdc1-/- mammary epithelial cells (mecs) to the intracellular,
      activated Wnt signal transducer, DeltaNbeta-catenin, was assayed both in
      vitro and in vivo, to test whether beta-catenin/TCF transactivation was
      Sdc1-independent. Surprisingly, we found that the expression of a
      canonical Wnt pathway reporter, TOP-FLASH, was reduced by 50% in both
      unstimulated Sdc1-/- mecs and in stimulated cells responding to Wnt1 or
      DeltaNbeta-catenin. Tumor development in response to DeltaNbeta-catenin
      was also significantly delayed on a Sdc1-/- background. Furthermore, the
      average beta-catenin/TCF transactivation per cell was normal in Sdc1-/-
      mec cultures, but the number of responsive cells was reduced by 50%.
      Sdc1-/- mecs show compensatory changes that maintain the number of HS
      chains, hence these experiments cannot test the coreceptor activity of HS
      for Wnt signaling. We propose that TCF-dependent transactivational
      activity is suppressed in 50% of cells in Sdc1-/- glands, and conclude
      that the major effect of Sdc1 does not map to the activity of the Wnt
      signaling complex, but to another pathway to create or stabilize the
      beta-catenin/TCF-responsive tumor precursor cells in mouse mammary gland.
AD  - McArdle Laboratory for Cancer Research, University of Wisconsin Medical
      School, 1400 University Ave, Madison, WI, USA.
FAU - Liu, Bob Y
AU  - Liu BY
FAU - Kim, Young Chul
AU  - Kim YC
FAU - Leatherberry, Vicki
AU  - Leatherberry V
FAU - Cowin, Pam
AU  - Cowin P
FAU - Alexander, Caroline M
AU  - Alexander CM
LA  - eng
GR  - CA 90877-01/CA/NCI
GR  - P30 CA14520/CA/NCI
GR  - T32 CA09135/CA/NCI
PT  - Journal Article
PL  - England
TA  - Oncogene
JID - 8711562
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Luminescent Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Plasmids)
RN  - 0 (Proteoglycans)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Trans-Activators)
RN  - 0 (proto-oncogene protein int-1)
RN  - 0 (syndecan)
RN  - 146409-33-8 (beta catenin)
RN  - 147336-22-9 (green fluorescent protein)
RN  - EC 1.13.12.- (Luciferase)
SB  - IM
MH  - Animals
MH  - Blotting, Western
MH  - Cells, Cultured
MH  - Cytoskeletal Proteins/*metabolism
MH  - Epithelium/*metabolism
MH  - Female
MH  - Flow Cytometry
MH  - Genotype
MH  - Luciferase/metabolism
MH  - Luminescent Proteins/metabolism
MH  - Mammary Glands, Animal/cytology/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Mice, Inbred C57BL
MH  - Models, Genetic
MH  - Mutation
MH  - Plasmids/metabolism
MH  - Protein Binding
MH  - Proteoglycans/*metabolism
MH  - Proto-Oncogene Proteins/metabolism
MH  - Signal Transduction
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Time Factors
MH  - Trans-Activation (Genetics)
MH  - Trans-Activators/*metabolism
MH  - Transcription, Genetic
MH  - Transfection
EDAT- 2003/12/19 05:00
MHDA- 2004/01/22 05:00
AID - 10.1038/sj.onc.1207217 [doi]
AID - 1207217 [pii]
PST - ppublish
SO  - Oncogene 2003 Dec 18;22(58):9243-53.

PMID- 14645569
OWN - NLM
STAT- completed
DA  - 20031203
DCOM- 20040113
IS  - 0022-538X
VI  - 77
IP  - 24
DP  - 2003 Dec
TI  - Different heparan sulfate proteoglycans serve as cellular receptors for
      human papillomaviruses.
PG  - 13125-35
AB  - Papillomaviruses replicate in stratified epithelia of skin and mucosa.
      Infection with certain human papillomavirus (HPV) types is the main cause
      of anogenital neoplasia, in particular cervical cancer. Early events of
      papillomavirus infectivity are poorly understood. While heparan sulfate
      proteoglycans (HSPGs) mediate initial binding to the cell surface, the
      class of proteins carrying heparan sulfates has not been defined. Here we
      examined two processes of papillomavirus infection, attachment of
      virus-like particles (VLP) to cells and infection with authentic HPV type
      11 (HPV11) virions. Of the HSPGs, syndecan-1 is the major epithelial form
      and is strongly upregulated in wound edge keratinocytes. We employed K562
      cells, which lack HSPGs except minor amounts of endogenous betaglycan, and
      stable clones that express cDNAs of syndecan-1, syndecan-4, or glypican-1.
      Binding of VLP correlated with levels of heparan sulfate on the cell
      surface. Parental K562 bound HPV16 VLP weakly, whereas all three K562
      transfectants demonstrated enhanced binding, with the highest binding
      capacity observed for syndecan-1-transfected cells, which also expressed
      the most HSPG. For HPV11 infectivity assays, a high virion inoculum was
      required to infect K562 cells, whereas ectopic expression of syndecan-1
      increased permissiveness eightfold and expression of syndecan-4 or
      glypican-1 fourfold. Infection of keratinocytes was eliminated by
      treatment with heparitinase, but not phospholipase C, further implicating
      the syndecan family of integral membrane proteins as receptor proteins.
      Human keratinocytes with a homozygous deletion of alpha6 integrin are
      permissive for HPV11 infection. These results indicate that several HSPGs
      can serve as HPV receptors and support a putative role for syndecan-1,
      rather than alpha6 integrin, as a primary receptor protein in natural HPV
      infection of keratinocytes.
AD  - Laboratory of Viral Oncology, Department of Dermatology, Division of
      Immunology, Allergy and Infectious Diseases (DIAID), University of Vienna
      Medical School, Vienna, Austria.
FAU - Shafti-Keramat, Saeed
AU  - Shafti-Keramat S
FAU - Handisurya, Alessandra
AU  - Handisurya A
FAU - Kriehuber, Ernst
AU  - Kriehuber E
FAU - Meneguzzi, Guerrino
AU  - Meneguzzi G
FAU - Slupetzky, Katharina
AU  - Slupetzky K
FAU - Kirnbauer, Reinhard
AU  - Kirnbauer R
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Virol
JID - 0113724
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Receptors, Virus)
RN  - 0 (Recombinant Proteins)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
SB  - IM
MH  - Heparan Sulfate Proteoglycan/genetics/*metabolism
MH  - Human
MH  - K562 Cells
MH  - Keratinocytes/*virology
MH  - Membrane Glycoproteins/genetics/*metabolism
MH  - Papillomavirus, Human/metabolism/*pathogenicity
MH  - Proteoglycans/genetics/*metabolism
MH  - Receptors, Virus/metabolism
MH  - Recombinant Proteins/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Transfection
MH  - Virion/metabolism/pathogenicity
EDAT- 2003/12/03 05:00
MHDA- 2004/01/14 05:00
PST - ppublish
SO  - J Virol 2003 Dec;77(24):13125-35.

PMID- 14637022
OWN - NLM
STAT- completed
DA  - 20031125
DCOM- 20040113
IS  - 0006-3002
VI  - 1617
IP  - 1-2
DP  - 2003 Oct 31
TI  - Interaction of RANTES with syndecan-1 and syndecan-4 expressed by human
      primary macrophages.
PG  - 80-8
AB  - Interaction of RANTES with its membrane ligands or receptors transduces
      multiple intracellular signals. Whether RANTES uses proteoglycans (PGs)
      belonging to the syndecan family to attach to primary cells expressing
      RANTES G-protein-coupled receptors (GPCRs) was investigated. We
      demonstrate that RANTES specifically binds to high and low affinity
      binding sites on human monocyte-derived macrophages (MDM). We show by
      co-immunoprecipitation experiments that RANTES is associated on these
      cells with syndecan-1 and syndecan-4, but neither with syndecan-2 nor with
      betaglycan, in addition to CD44 and its GPCRs, CCR5 and CCR1.
      Glycosaminidases pre-treatment of the monocyte derived-macrophages
      strongly decreases the binding of RANTES to syndecan-1 and syndecan-4 and
      also to CCR5, and abolishes RANTES binding to CD44. This suggests that
      glycosaminoglycans (GAGs) are involved in RANTES binding to the PGs and
      that such bindings facilitate the subsequent interaction of RANTES with
      CCR5, on the MDM, characterized by low membrane expression of CCR5. The
      role of these interactions in the pathophysiology of RANTES deserves
      further study.
AD  - UPRES 3410, UFR-SMBH, Universite Paris XIII, 74 rue Marcel Cachin, Hopital
      Jean Verdier, 93017 Bondy, Bobigny, France.
FAU - Slimani, Hocine
AU  - Slimani H
FAU - Charnaux, Nathalie
AU  - Charnaux N
FAU - Mbemba, Elisabeth
AU  - Mbemba E
FAU - Saffar, Line
AU  - Saffar L
FAU - Vassy, Roger
AU  - Vassy R
FAU - Vita, Claudio
AU  - Vita C
FAU - Gattegno, Liliane
AU  - Gattegno L
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Biochim Biophys Acta
JID - 0217513
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RANTES)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
SB  - IM
MH  - Cell Membrane/*chemistry/metabolism
MH  - Comparative Study
MH  - Human
MH  - Leukocytes, Mononuclear/chemistry/metabolism
MH  - Macrophages/*chemistry/*metabolism
MH  - Membrane Glycoproteins/biosynthesis/*chemistry
MH  - Protein Binding
MH  - Proteoglycans/biosynthesis/*chemistry
MH  - RANTES/*chemistry/metabolism
MH  - Support, Non-U.S. Gov't
EDAT- 2003/11/26 05:00
MHDA- 2004/01/14 05:00
AID - S0005273603002888 [pii]
PST - ppublish
SO  - Biochim Biophys Acta 2003 Oct 31;1617(1-2):80-8.

PMID- 14630925
OWN - NLM
STAT- publisher
DA  - 20031121
IS  - 1083-351X
DP  - 2003 Nov 20
TI  - Heparanase degrades syndecan-1 and perlecan heparan sulfate: Functional
      implications for tumor cell invasion.
AB  - Heparan sulfate proteoglycans (HSPG) play critical roles in regulating
      tumor cell metastasis by mediating cell adhesion and the activities of
      growth and angiogenic factors. Heparanase (HPSE-1) is involved in the
      degradation of cell-surface and extracellular matrix (ECM) heparan sulfate
      (HS) in normal and neoplastic tissues. Degradation of HSPG in mammalian
      cells is dependent upon the enzymatic activity of HPSE-1, an
      endo--D-glucuronidase, which cleaves heparan sulfate (HS) at specific
      intrachain sites. Elevated HPSE-1 levels are known to be associated with
      metastatic cancers. The mechanism of HPSE-1 action to promote tumor
      progression may involve multiple substrates as HS is present on both
      cell-surface and ECM proteoglycans. However, the specific targets of
      HPSE-1 action are not known. Of particular interest is the relationship
      between HPSE-1 and HSPG known for their involvement in tumor progression.
      Syndecan-1 is a HSPG that is expressed at the cell-surface and its role in
      cancer progression may depend upon its degradation. Conversely, another
      HSPG, perlecan, is an important component of basement membranes and ECM,
      which can promote invasive behavior. In the present study we demonstrate
      that: 1) HPSE-1 cleaves HS present on the cell-surface of metastatic
      melanoma cells; 2) HPSE-1 specifically degrades HS chains of purified
      syndecan-1 or perlecan HS isolated from WiDr cells; 3) syndecan-1 does not
      directly inhibit HPSE-1 enzymatic activity; 4) presence of exogenous
      syndecan-1 inhibits HPSE-1 - mediated invasive behavior of melanoma cells
      by in vitro chemoinvasion assays; and 5) inhibition of HPSE-1 - induced
      invasion requires syndecan-1 HS chains. These results demonstrate that
      cell-surface syndecan-1 and ECM perlecan are degradative targets of HPSE-1
      and syndecan-1 regulates HPSE-1 biological activity. These data suggest
      that expression of syndecan-1 on the melanoma cell surface and its
      degradation by HPSE-1 are important determinants in the control of tumor
      cell invasion and metastasis.
AD  - Comparative Biomedical Sciences, LSU-Baton-Rouge, School of Veterinary
      Medicine, Baton Rouge, LA 70803.
AU  - Reiland J
AU  - Sanderson RD
AU  - Waguespack M
AU  - Barker SA
AU  - Long R
AU  - Carson DD
AU  - Marchetti D
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - J Biol Chem
JID - 2985121R
EDAT- 2003/11/25 05:00
MHDA- 2003/11/25 05:00
AID - 10.1074/jbc.M304872200 [doi]
AID - M304872200 [pii]
PST - aheadofprint
SO  - J Biol Chem 2003 Nov 20;.

PMID- 14630803
OWN - NLM
STAT- publisher
DA  - 20031121
IS  - 0006-4971
DP  - 2003 Nov 20
TI  - Characterization of clonogenic multiple myeloma cells.
AB  - The identity of the cells responsible for the initiation and maintenance
      of multiple myeloma (MM) remains unclear largely because of the difficulty
      growing MM cells in vitro and in vivo. MM cell lines and clinical
      specimens are characterized by malignant plasma cells that express the
      cell surface antigen syndecan-1 (CD138); however, CD138 expression is
      limited to terminally differentiated plasma cells during B cell
      development. Moreover, circulating B cells that are clonally related to MM
      plasma cells have been reported in some patients with MM. We found that
      human MM cell lines contained small (< 5%) subpopulations that lacked
      CD138 expression and had greater clonogenic potential in vitro than
      corresponding CD138(+) plasma cells. CD138(neg) cells from clinical MM
      samples were similarly clonogenic both in vitro and in NOD/SCID mice,
      whereas CD138(+) cells were not. Furthermore, CD138(neg) cells from both
      cell lines and clinical samples phenotypically resembled post-germinal
      center B cells, and their clonogenic growth was inhibited by the anti-CD20
      monoclonal antibody rituximab. These data suggest that MM "stem cells" are
      CD138(neg) B cells with the ability to replicate and subsequently
      differentiate into malignant CD138(+) plasma cells.
AD  - Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University School
      of Medicine, Baltimore, MD, USA.
AU  - Matsui WH
AU  - Huff CA
AU  - Wang Q
AU  - Malehorn MT
AU  - Barber J
AU  - Tanhehco Y
AU  - Smith BD
AU  - Civin CI
AU  - Jones RJ
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - Blood
JID - 7603509
EDAT- 2003/11/25 05:00
MHDA- 2003/11/25 05:00
AID - 10.1182/blood-2003-09-3064 [doi]
AID - 2003-09-3064 [pii]
PST - aheadofprint
SO  - Blood 2003 Nov 20;.

PMID- 14625378
OWN - NLM
STAT- publisher
DA  - 20031119
IS  - 1094-8341
DP  - 2003 Nov 18
TI  - Increased Syndecan Expression Following Myocardial Infarction Indicates a
      Role in Cardiac Remodeling.
AB  - The purpose of this study was to identify essential genes involved in
      myocardial growth and remodeling following myocardial infarction (MI).
      Left ventricular non-infarcted tissues from six mice subjected to MI under
      general anesthesia and from six sham operated mice were obtained one week
      after primary surgery, and analyzed by means of cDNA filter arrays. Out of
      a total of 1176 genes, 641 were consistently expressed, twenty-three were
      upregulated and thirteen downregulated. Five genes were only expressed
      following MI. Syndecan-3, a transmembranous heparan sulphate proteoglycan,
      was found to be upregulated together with a transcriptional activator of
      syndecans, Wilms tumor protein 1 (WT-1). Northern blotting demonstrated a
      significant upregulation of syndecan 1-4, WT-1, fibronectin and basic
      fibroblast growth factor (FGF) receptor 1. Furthermore, Western blot
      analysis showed statistically significant increases in protein levels for
      syndecan-3 and -4. In conclusion, we have identified a subset of genes
      with increased expression in non-infarcted left ventricular tissue
      following MI,including syndecan 1-4, WT-1, fibronectin, collagen 6A and
      FGF receptor 1. Since the syndecans link the cytoskeleton to the
      extracellular matrix and function as required coreceptors for FGF, we
      suggest a role for the syndecans in cardiac remodeling following MI.
AD  - Ullevaal University Hospital, Institute for Experimental Medical Research,
      Oslo, Norway.
AU  - Finsen AV
AU  - Woldbaek PR
AU  - Li J
AU  - Wu J
AU  - Lyberg T
AU  - Tonnessen T
AU  - Christensen G
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - Physiol Genomics
JID - 9815683
EDAT- 2003/11/20 05:00
MHDA- 2003/11/20 05:00
AID - 10.1152/physiolgenomics.00144.2002 [doi]
AID - 00144.2002 [pii]
PST - aheadofprint
SO  - Physiol Genomics 2003 Nov 18;.

PMID- 14612567
OWN - NLM
STAT- in-process
DA  - 20031203
IS  - 0027-8424
VI  - 100
IP  - 24
DP  - 2003 Nov 25
TI  - Functional identification of distinct sets of antitumor activities
      mediated by the FKBP gene family.
PG  - 14253-8
AB  - Assigning biologic function to the many sequenced but still
      uncharacterized genes remains the greatest obstacle confronting the human
      genome project. Differential gene expression profiling routinely detects
      uncharacterized genes aberrantly expressed in conditions such as cancer
      but cannot determine which genes are functionally involved in such complex
      phenotypes. Integrating gene expression profiling with specific modulation
      of gene expression in relevant disease models can identify complex
      biologic functions controlled by currently uncharacterized genes. Here, we
      used systemic gene transfer in tumor-bearing mice to identify novel
      antiinvasive and antimetastatic functions for Fkbp8, and subsequently for
      Fkbp1a. Fkbp8 is a previously uncharacterized member of the FK-506-binding
      protein (FKBP) gene family down-regulated in aggressive tumors. Antitumor
      effects produced by Fkbp1a gene expression are mediated by cellular
      pathways entirely distinct from those responsible for antitumor effects
      produced by Fkbp1a binding to its bacterially derived ligand, rapamycin.
      We then used gene expression profiling to identify syndecan 1 (Sdc1) and
      matrix metalloproteinase 9 (MMP9) as genes directly regulated by Fkbp1a
      and Fkbp8. FKBP gene expression coordinately induces the expression of the
      antiinvasive Sdc1 gene and suppresses the proinvasive MMP9 gene.
      Conversely, short interfering RNA-mediated suppression of Fkbp1a increases
      tumor cell invasion and MMP9 levels, while down-regulating Sdc1. Thus,
      syndecan 1 and MMP9 appear to mediate the antiinvasive and antimetastatic
      effects produced by FKBP gene expression. These studies show that
      uncharacterized genes differentially expressed in metastatic cancers can
      play important functional roles in the metastatic phenotype. Furthermore,
      identifying gene regulatory networks that function to control tumor
      progression may permit more accurate modeling of the complex molecular
      mechanisms of this disease.
AD  - California Pacific Medical Research Institute, San Francisco, CA 94115,
      USA.
FAU - Fong, Sylvia
AU  - Fong S
FAU - Mounkes, Leslie
AU  - Mounkes L
FAU - Liu, Yong
AU  - Liu Y
FAU - Maibaum, Michael
AU  - Maibaum M
FAU - Alonzo, Eric
AU  - Alonzo E
FAU - Desprez, Pierre-Yves
AU  - Desprez PY
FAU - Thor, Ann D
AU  - Thor AD
FAU - Kashani-Sabet, Mohammed
AU  - Kashani-Sabet M
FAU - Debs, Robert J
AU  - Debs RJ
LA  - eng
GR  - R01 CA82575/CA/NCI
PT  - Journal Article
DEP - 20031111
PL  - United States
TA  - Proc Natl Acad Sci U S A
JID - 7505876
SB  - IM
EDAT- 2003/11/13 05:00
MHDA- 2003/11/13 05:00
PHST- 2003/Nov/11 [aheadofprint]
AID - 10.1073/pnas.2332307100 [doi]
AID - 2332307100 [pii]
PST - ppublish
SO  - Proc Natl Acad Sci U S A 2003 Nov 25;100(24):14253-8.

PMID- 14612502
OWN - NLM
STAT- completed
DA  - 20031112
DCOM- 20040116
IS  - 0008-5472
VI  - 63
IP  - 21
DP  - 2003 Nov 1
TI  - Role of Id-2 in the maintenance of a differentiated and noninvasive
      phenotype in breast cancer cells.
PG  - 7098-105
AB  - Id proteins are inhibitors of basic helix-loop-helix transcription factors
      and generally stimulate cell proliferation and inhibit differentiation. We
      have shown that ectopic expression of Id-1 in murine mammary epithelial
      cells resulted in loss of differentiation and gain of invasive and
      proliferative abilities. Moreover, Id-1 was highly expressed in aggressive
      breast cancer cells in culture and in biopsies from infiltrating
      carcinomas. In contrast to Id-1, we found that, in vitro and in vivo, Id-2
      mRNA and protein were up-regulated as mammary epithelial cells lost
      proliferative capacity and initiated differentiation. We further
      determined that this up-regulation of Id-2 was a necessary step toward a
      fully differentiated phenotype in breast cells. Here we show that one of
      the components of the extracellular matrix network, laminin, is
      responsible for the increase in Id-2 expression during differentiation. We
      also show that Id-2 expression is inversely correlated with the rate of
      proliferation in murine mammary epithelial cells and that Id-2 is
      expressed at a higher level in differentiated human breast cancer cells in
      comparison with very aggressive and metastatic cells. When reintroduced in
      aggressive breast cancer cells, Id-2 is able to reduce their proliferative
      and invasive phenotypes and decrease their level of matrix
      metalloproteinase 9 secretion as well as increase syndecan-1 expression.
      Moreover, little Id-2 protein expression is detectable in human biopsies
      from aggressive and invasive carcinomas in comparison with in situ
      carcinomas. In conclusion, Id-2 expression not only follows a pattern
      opposite to that of Id-1 during mammary gland development and breast
      cancer progression but also appears to act as an important protein for the
      maintenance of a differentiated and noninvasive phenotype in normal and
      transformed breast cells.
AD  - Cancer Research Institute, California Pacific Medical Center, Stern
      Building, 2230 Clay Street, San Francisco, CA 94115, USA.
FAU - Itahana, Yoko
AU  - Itahana Y
FAU - Singh, Jarnail
AU  - Singh J
FAU - Sumida, Tomoki
AU  - Sumida T
FAU - Coppe, Jean-Philippe
AU  - Coppe JP
FAU - Parrinello, Simona
AU  - Parrinello S
FAU - Bennington, James L
AU  - Bennington JL
FAU - Desprez, Pierre-Yves
AU  - Desprez PY
LA  - eng
GR  - R01 CA 82548/CA/NCI
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JID - 2984705R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Laminin)
RN  - 0 (Transcription Factors)
RN  - 146990-20-7 (Id-2 protein)
SB  - IM
MH  - Animals
MH  - Biopsy
MH  - Breast Neoplasms/*metabolism/*pathology
MH  - Cell Differentiation/physiology
MH  - Cell Line, Tumor
MH  - DNA-Binding Proteins/biosynthesis/genetics/*physiology
MH  - Disease Progression
MH  - Gene Expression Regulation
MH  - Human
MH  - Laminin/physiology
MH  - Mammary Glands, Animal/cytology/metabolism
MH  - Mice
MH  - Prognosis
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Transcription Factors/biosynthesis/genetics/*physiology
EDAT- 2003/11/13 05:00
MHDA- 2004/01/17 05:00
PST - ppublish
SO  - Cancer Res 2003 Nov 1;63(21):7098-105.

PMID- 14580209
OWN - NLM
STAT- completed
DA  - 20031028
DCOM- 20031210
IS  - 0006-2960
VI  - 42
IP  - 43
DP  - 2003 Nov 4
TI  - Syndecan binding sites in the laminin alpha1 chain G domain.
PG  - 12625-33
AB  - The laminin alpha1 chain G domain has multiple biological activities.
      Previously, we identified cell binding sequences in the laminin alpha1
      chain G domain by screening 113 synthetic peptide-polystyrene beads for
      cell attachment activity. Here, we have used a recombinant protein of the
      laminin alpha1 G domain (rec-alpha1G) and a large set of synthetic
      peptides to further identify and characterize heparin, cell, and
      syndecan-4 binding sites in the laminin alpha1 chain G domain. The
      rec-alpha1G protein promoted both cell attachment and heparin binding
      (K(D) = 19 nM). Cell attachment to the rec-alpha1G protein was inhibited
      60% by heparin and 30% by EDTA. The heparin binding sites were identified
      by competing heparin binding to the rec-alpha1G protein with 110 synthetic
      peptides in solution. Only two peptides, AG73 (IC(50) = 147 microM) and
      AG75 (IC(50) = 206 microM), inhibited heparin binding to rec-alpha1G. When
      the peptides were compared in a solid-phase heparin binding assay, AG73
      showed more heparin binding than AG75. AG73 also inhibited fibroblast
      attachment to the rec-alpha1G protein, but AG75 did not. Cell attachment
      to the peptides was studied using peptide-coated plates and
      peptide-conjugated sepharose beads. AG73 promoted cell attachment in both
      assays, but AG75 only showed cell attachment activity in the bead assay.
      Additionally, AG73, but not AG75, inhibited branching morphogenesis of
      mouse submandibular glands in organ culture. Furthermore, the rec-alpha1G
      protein bound syndecan-4, and both AG73 and AG75 inhibited this binding.
      These results suggest that the AG73 and AG75 sites are important for
      heparin and syndecan-4 binding in the laminin alpha1 chain G domain. These
      sites may play a critical role in the diverse biological activities
      involving heparin and syndecan-4 binding.
AD  - Graduate School of Environmental Earth Science, Hokkaido University,
      Sapporo 060-0810, Japan.
FAU - Suzuki, Nobuharu
AU  - Suzuki N
FAU - Ichikawa, Naoki
AU  - Ichikawa N
FAU - Kasai, Shingo
AU  - Kasai S
FAU - Yamada, Masanori
AU  - Yamada M
FAU - Nishi, Norio
AU  - Nishi N
FAU - Morioka, Hiroshi
AU  - Morioka H
FAU - Yamashita, Hironobu
AU  - Yamashita H
FAU - Kitagawa, Yasuo
AU  - Kitagawa Y
FAU - Utani, Atsushi
AU  - Utani A
FAU - Hoffman, Matthew P
AU  - Hoffman MP
FAU - Nomizu, Motoyoshi
AU  - Nomizu M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Biochemistry
JID - 0370623
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptides)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 151186-83-3 (laminin A)
RN  - 9005-49-6 (Heparin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - CHO Cells
MH  - Cell Adhesion
MH  - Cells, Cultured
MH  - Comparative Study
MH  - Hamsters
MH  - Heparin/metabolism
MH  - Human
MH  - In Vitro
MH  - Laminin/chemistry/*metabolism
MH  - Membrane Glycoproteins/chemistry/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Peptides/pharmacology
MH  - Protein Binding
MH  - Proteoglycans/chemistry/*metabolism
MH  - Submandibular Gland/drug effects/growth & development
MH  - Support, Non-U.S. Gov't
EDAT- 2003/10/29 05:00
MHDA- 2003/12/12 05:00
AID - 10.1021/bi030014s [doi]
PST - ppublish
SO  - Biochemistry 2003 Nov 4;42(43):12625-33.

PMID- 14578401
OWN - NLM
STAT- completed
DA  - 20031027
DCOM- 20031120
IS  - 0146-0404
VI  - 44
IP  - 11
DP  - 2003 Nov
TI  - Effect of heparin II domain of fibronectin on aqueous outflow in cultured
      anterior segments of human eyes.
PG  - 4796-804
AB  - PURPOSE: To determine whether an integrin/syndecan-binding domain of
      fibronectin, called the heparin II (Hep II) domain, affects outflow
      facility in the human eye. METHODS: Anterior segments of human eyes were
      placed in perfusion organ culture. One eye of each pair received the Hep
      II domain, and the fellow eye received DMEM or a heat-denatured Hep II
      domain. The Hep II domain was produced as a recombinant glutathione
      S-transferase (GST)-fusion protein. Microscopic changes were assessed.
      RESULTS: Outflow facility in anterior segments treated with Hep II domain
      increased by 93% compared with that in anterior segments treated with
      DMEM. In contrast, facility in anterior segments treated with the
      heat-denatured Hep II domain showed very little change. Outflow facility
      remained high during Hep II domain perfusion and returned to baseline
      after removal of the protein. Electron microscopy revealed disruptions in
      the endothelial lining of Schlemm's canal in anterior segments fixed
      during maximum effect and in anterior segments after facility had returned
      to baseline. Scattered disruptions of canal cells were noted in control
      anterior segments. Trabecular cells in other regions looked normal. Major
      changes in the extracellular matrix of the juxtacanalicular tissue were
      not observed. Repeated doses of the Hep II domain administered after
      facility returned to baseline increased facility in two of three anterior
      segments. CONCLUSIONS: The Hep II domain of fibronectin increases outflow
      facility in the human anterior segment. This suggests that
      fibronectin-mediated interactions may have a role in modulating aqueous
      hydrodynamics. Such interactions may represent avenues of novel
      therapeutic interventions for glaucoma.
AD  - Department of Pathology and Laboratory Medicine, University of Wisconsin,
      Madison, Wisconsin 53706, USA.
FAU - Santas, Amy J
AU  - Santas AJ
FAU - Bahler, Cindy
AU  - Bahler C
FAU - Peterson, Jennifer A
AU  - Peterson JA
FAU - Filla, Mark S
AU  - Filla MS
FAU - Kaufman, Paul L
AU  - Kaufman PL
FAU - Tamm, Ernst R
AU  - Tamm ER
FAU - Johnson, Douglas H
AU  - Johnson DH
FAU - Peters, Donna M Pesciotta
AU  - Peters DM
LA  - eng
GR  - EY02698/EY/NEI
GR  - EY07065/EY/NEI
GR  - EY12515/EY/NEI
PT  - Journal Article
PL  - United States
TA  - Invest Ophthalmol Vis Sci
JID - 7703701
RN  - 0 (Fibronectins)
RN  - 0 (Integrin alpha4beta1)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (syndecan)
RN  - 9005-49-6 (Heparin)
SB  - IM
MH  - Aged
MH  - Aged, 80 and over
MH  - Anterior Eye Segment/*drug effects/secretion/ultrastructure
MH  - Aqueous Humor/*secretion
MH  - Fibronectins/*metabolism/*pharmacology
MH  - Heparin/*metabolism/*pharmacology
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Integrin alpha4beta1/metabolism
MH  - Membrane Glycoproteins/metabolism
MH  - Middle Aged
MH  - Organ Culture
MH  - Peptide Fragments/pharmacology
MH  - Proteoglycans/metabolism
MH  - Recombinant Fusion Proteins
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2003/10/28 05:00
MHDA- 2003/12/03 05:00
PST - ppublish
SO  - Invest Ophthalmol Vis Sci 2003 Nov;44(11):4796-804.

PMID- 14576062
OWN - NLM
STAT- publisher
DA  - 20031024
IS  - 0006-4971
DP  - 2003 Oct 23
TI  - An inhibitor of the EGF receptor family blocks myeloma cell growth factor
      activity of HB-EGF and potentiates dexamethasone or anti-IL-6
      antibody-induced apoptosis.
AB  - We previously found that some myeloma cell lines express the
      heparin-binding epidermal growth factor-like growth factor (HB-EGF) gene.
      As the proteoglycan syndecan-1 is an HB-EGF coreceptor as well as a
      hallmark of plasma cell differentiation and a marker of myeloma cells, we
      studied the role of HB-EGF on myeloma cell growth. The HB-EGF gene was
      expressed by bone marrow mononuclear cells of 8/8 patients with myeloma,
      particularly by monocytes and stromal cells, but not by purified primary
      myeloma cells. 6/9 myeloma cell lines and 9/9 purified primary myeloma
      cells expressed ErbB1 or ErbB4 genes coding for HB-EGF receptor. In the
      presence of a low IL-6 concentration, HB-EGF stimulated the proliferation
      of the six ErbB1(+) or ErbB4(+) cell lines, through the PI-3K/AKT pathway.
      A pan-ErbB inhibitor blocked the myeloma cell growth factor activity and
      the signaling induced by HB-EGF. This inhibitor induced apoptosis of
      patients' myeloma cells cultured with their tumor environment. It also
      increased patients' myeloma cell apoptosis induced by an anti-IL-6
      antibody or dexamethasone. The ErbB inhibitor had no effect on the
      interaction between MM cells and stromal cells. It was not toxic for
      non-myeloma cells present in patients' bone marrow cultures or for the
      growth of hematopoietic progenitors. Altogether, these data identify ErbB
      receptors as putative therapeutic targets in multiple myeloma.
AD  - INSERM U475 and Unit for Cellular Therapy, CHU Montpellier, Montpellier,
      France.
AU  - Mahtouk K
AU  - Jourdan M
AU  - De Vos J
AU  - Hertogh C
AU  - Fiol G
AU  - Jourdan E
AU  - Rossi JF
AU  - Klein B
LA  - ENG
PT  - JOURNAL ARTICLE
TA  - Blood
JID - 7603509
EDAT- 2003/10/25 05:00
MHDA- 2003/10/25 05:00
AID - 10.1182/blood-2003-05-1510 [doi]
AID - 2003-05-1510 [pii]
PST - aheadofprint
SO  - Blood 2003 Oct 23;.

PMID- 14573623
OWN - NLM
STAT- in-process
DA  - 20031225
IS  - 0021-9258
VI  - 279
IP  - 1
DP  - 2004 Jan 2
TI  - Activation of syndecan-1 ectodomain shedding by Staphylococcus aureus
      alpha-toxin and beta-toxin.
PG  - 251-8
AB  - Exploitation of host components by microbes to promote their survival in
      the hostile host environment has been a recurring theme in recent years.
      Available data indicate that bacterial pathogens activate ectodomain
      shedding of host cell surface molecules to enhance their virulence. We
      reported previously that several major bacterial pathogens activate
      ectodomain shedding of syndecan-1, the major heparan sulfate proteoglycan
      of epithelial cells. Here we define the molecular basis of how
      Staphylococcus aureus activates syndecan-1 shedding. We screened mutant S.
      aureus strains devoid of various toxin and protease genes and found that
      only strains lacking both alpha-toxin and beta-toxin genes do not
      stimulate shedding. Mutations in the agr global regulatory locus, which
      positively regulates expression of alpha- and beta-toxins and other
      exoproteins, also abrogated the capacity to stimulate syndecan-1 shedding.
      Furthermore, purified S. aureus alpha- and beta-toxins, but not
      enterotoxin A and toxic shock syndrome toxin-1, rapidly potentiated
      shedding in a concentration-dependent manner. These results establish that
      S. aureus activates syndecan-1 ectodomain shedding via its two virulence
      factors, alpha- and beta-toxins. Toxin-activated shedding was also
      selectively inhibited by antagonists of the host cell shedding mechanism,
      indicating that alpha- and beta-toxins shed syndecan-1 ectodomains through
      stimulation of the host cell's shedding machinery. Interestingly,
      beta-toxin, but not alpha-toxin, also enhanced ectodomain shedding of
      syndecan-4 and heparin-binding epidermal growth factor. Because shedding
      of these ectodomains has been implicated in promoting bacterial
      pathogenesis, activation of ectodomain shedding by alpha-toxin and
      beta-toxin may be a previously unknown virulence mechanism of S. aureus.
AD  - Department of Medicine, Baylor College of Medicine, Houston, TX 77030,
      USA. pwpark@bcm.tmc.edu
FAU - Park, Pyong Woo
AU  - Park PW
FAU - Foster, Timothy J
AU  - Foster TJ
FAU - Nishi, Eiichiro
AU  - Nishi E
FAU - Duncan, Sheila J
AU  - Duncan SJ
FAU - Klagsbrun, Michael
AU  - Klagsbrun M
FAU - Chen, Ye
AU  - Chen Y
LA  - eng
GR  - HL69050/HL/NHLBI
PT  - Journal Article
DEP - 20031022
PL  - United States
TA  - J Biol Chem
JID - 2985121R
SB  - IM
EDAT- 2003/10/24 05:00
MHDA- 2003/10/24 05:00
PHST- 2003/Oct/22 [aheadofprint]
AID - 10.1074/jbc.M308537200 [doi]
AID - M308537200 [pii]
PST - ppublish
SO  - J Biol Chem 2004 Jan 2;279(1):251-8.

PMID- 14562280
OWN - NLM
STAT- completed
DA  - 20031016
DCOM- 20031028
IS  - 0046-8177
VI  - 34
IP  - 9
DP  - 2003 Sep
TI  - Reduced expression of syndecan-1 correlates with histologic
      dedifferentiation, lymph node metastasis, and poor prognosis in
      intrahepatic cholangiocarcinoma.
PG  - 857-63
AB  - Syndecan-1, a cell-surface transmembrane heparan sulfate proteoglycan, has
      been reported to correlate with the biologic behavior of malignant tumors
      in various organs. We examined the correlation between the expression of
      syndecan-1 at the protein and mRNA levels and clinicopathologic features
      of 37 intrahepatic cholangiocarcinomas (ICCs). Noncancerous bile duct
      epithelial cells showed basolateral membranous expression of syndecan-1,
      whereas ICC cells showed membranous and also diffuse cytoplasmic
      expression. In situ hybridization demonstrated a distribution of
      syndecan-1 mRNA similar to that of the protein in carcinoma tissue,
      suggesting that syndecan-1 expression in ICC is regulated at the
      transcriptional level. Reduction of syndecan-1 expression in carcinoma was
      associated with poor histological differentiation (P <0.01): syndecan-1
      expression was intense and extensive in well-differentiated (10 cases) and
      largely negative or weakly positive in poorly differentiated (13 cases)
      adenocarcinoma, and its expression in moderately differentiated tumors (14
      cases) was intermediate. Patients with ICCs demonstrating negative or weak
      expression of syndecan-1 frequently had lymph node metastases and had a
      rather poor prognosis after surgical resection compared with those whose
      tumors demonstrated moderate or strong expression (P <0.05). However,
      syndecan-1 expression was not correlated with tumor size, stromal
      desmoplasia, gross classification, vascular invasion, or perineural
      invasion. We conclude that expression of syndecan-1 could correlate with
      some aspects of the biologic behaviors of ICCs and may be a useful
      prognostic marker.
AD  - Department of Human Pathology, Kanazawa University Graduate School of
      Medicine, Japan.
FAU - Harada, Kenichi
AU  - Harada K
FAU - Masuda, Shinji
AU  - Masuda S
FAU - Hirano, Makoto
AU  - Hirano M
FAU - Nakanuma, Yasuni
AU  - Nakanuma Y
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Hum Pathol
JID - 9421547
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Neoplasm)
RN  - 0 (syndecan)
SB  - IM
MH  - Aged
MH  - Bile Duct Neoplasms/genetics/*metabolism/pathology
MH  - *Bile Ducts, Intrahepatic
MH  - Cell Transformation, Neoplastic/genetics/*metabolism/pathology
MH  - Cholangiocarcinoma/genetics/*metabolism/secondary
MH  - Disease-Free Survival
MH  - Female
MH  - Human
MH  - Immunoenzyme Techniques
MH  - In Situ Hybridization
MH  - Lymph Nodes/pathology
MH  - Male
MH  - Membrane Glycoproteins/genetics/*metabolism
MH  - Proteoglycans/genetics/*metabolism
MH  - RNA, Messenger/metabolism
MH  - RNA, Neoplasm/analysis
EDAT- 2003/10/17 05:00
MHDA- 2003/10/29 05:00
AID - S0046817703003368 [pii]
PST - ppublish
SO  - Hum Pathol 2003 Sep;34(9):857-63.

PMID- 14527891
OWN - NLM
STAT- completed
DA  - 20031006
DCOM- 20031124
IS  - 0006-4971
VI  - 102
IP  - 8
DP  - 2003 Oct 15
TI  - Do human myeloma cells directly produce basic FGF?
PG  - 3071-2; author reply 3072-3
FAU - Colla, Simona
AU  - Colla S
FAU - Morandi, Francesca
AU  - Morandi F
FAU - Lazzaretti, Mirca
AU  - Lazzaretti M
FAU - Polistena, Paola
AU  - Polistena P
FAU - Svaldi, Mirija
AU  - Svaldi M
FAU - Coser, Paolo
AU  - Coser P
FAU - Bonomini, Sabrina
AU  - Bonomini S
FAU - Hojden, Magda
AU  - Hojden M
FAU - Martella, Eugenia
AU  - Martella E
FAU - Chisesi, Teodoro
AU  - Chisesi T
FAU - Rizzoli, Vittorio
AU  - Rizzoli V
FAU - Giuliani, Nicola
AU  - Giuliani N
LA  - eng
PT  - Comment
PT  - Letter
PL  - United States
TA  - Blood
JID - 7603509
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 103107-01-3 (Fibroblast Growth Factor 2)
SB  - AIM
SB  - IM
CON - Blood. 2003 Apr 1;101(7):2775-83. PMID: 12517814
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Blotting, Western
MH  - Bone Marrow Cells/metabolism
MH  - Fibroblast Growth Factor 2/*biosynthesis
MH  - Human
MH  - Membrane Glycoproteins/biosynthesis
MH  - Middle Aged
MH  - Multiple Myeloma/*metabolism
MH  - Proteoglycans/biosynthesis
MH  - Reverse Transcriptase Polymerase Chain Reaction
EDAT- 2003/10/07 05:00
MHDA- 2003/12/03 05:00
AID - 10.1182/blood-2003-06-1883 [doi]
AID - 102/8/3071 [pii]
PST - ppublish
SO  - Blood 2003 Oct 15;102(8):3071-2; author reply 3072-3.

PMID- 14522909
OWN - NLM
STAT- completed
DA  - 20031002
DCOM- 20031204
LR  - 20040120
IS  - 0008-5472
VI  - 63
IP  - 18
DP  - 2003 Sep 15
TI  - Insulin-like growth factor-1 induces adhesion and migration in human
      multiple myeloma cells via activation of beta1-integrin and
      phosphatidylinositol 3'-kinase/AKT signaling.
PG  - 5850-8
AB  - Insulin-like growth factor-1 (IGF-I) is a growth and survival factor in
      human multiple myeloma (MM) cells. Here we examine the effect of IGF-I on
      MM cell adhesion and migration, and define the role of beta1 integrin in
      these processes. IGF-I increases adhesion of MM.1S and OPM6 MM cells to
      fibronectin (FN) in a time- and dose-dependent manner, as a consequence of
      IGF-IR activation. Conversely, blocking anti-beta1 integrin monoclonal
      antibody, RGD peptide, and cytochalasin D inhibit IGF-I-induced cell
      adhesion to FN. IGF-I rapidly and transiently induces association of
      IGF-IR and beta1 integrin, with phosphorylation of IGF-IR, IRS-1, and
      p85(PI3-K). IGF-I also triggers phosphorylation of AKT and ERK
      significantly. Both IGF-IR and beta1 integrin colocalize to lipid rafts on
      the plasma membrane after IGF-I stimulation. In addition, IGF-I triggers
      polymerization of F-actin, induces phosphorylation of p125(FAK) and
      paxillin, and enhances beta1 integrin interaction with these focal
      adhesion proteins. Importantly, using pharmacological inhibitors of
      phosphatidylinositol 3'-kinase (PI3-K) (LY294002 and wortmannin) and
      extracellular signal-regulated kinase (PD98059), we demonstrate that
      IGF-I-induced MM cell adhesion to FN is achieved only when PI3-K/AKT is
      activated. IGF-I induces a 1.7-2.2 (MM.1S) and 2-2.5-fold (OPM6) increase
      in migration, whereas blocking anti-IGF-I and anti-beta1 integrin
      monoclonal antibodies, PI3-K inhibitors, as well as cytochalasin D
      abrogate IGF-I-induced MM cell transmigration. Finally, IGF-I induces
      adhesion of CD138+ patient MM cells. Therefore, these studies suggest a
      role for IGF-I in trafficking and localization of MM cells in the bone
      marrow microenvironment. Moreover, they define the functional association
      of IGF-IR and beta1 integrin in mediating MM cell homing, providing the
      preclinical rationale for novel treatment strategies targeting
      IGF-I/IGF-IR in MM.
AD  - The Jerome Lipper Multiple Myeloma Center, Department of Medical Oncology,
      Dana-Farber Cancer Institute, Boston, MA 02115, USA.
FAU - Tai, Yu-Tzu
AU  - Tai YT
FAU - Podar, Klaus
AU  - Podar K
FAU - Catley, Laurence
AU  - Catley L
FAU - Tseng, Yu-Hua
AU  - Tseng YH
FAU - Akiyama, Masaharu
AU  - Akiyama M
FAU - Shringarpure, Reshma
AU  - Shringarpure R
FAU - Burger, Renate
AU  - Burger R
FAU - Hideshima, Teru
AU  - Hideshima T
FAU - Chauhan, Dharminder
AU  - Chauhan D
FAU - Mitsiades, Nicholas
AU  - Mitsiades N
FAU - Richardson, Paul
AU  - Richardson P
FAU - Munshi, Nikhil C
AU  - Munshi NC
FAU - Kahn, C Ronald
AU  - Kahn CR
FAU - Mitsiades, Constantine
AU  - Mitsiades C
FAU - Anderson, Kenneth C
AU  - Anderson KC
LA  - eng
GR  - P01-78378/PHS
GR  - R0-1 50947/PHS
PT  - Journal Article
PL  - United States
TA  - Cancer Res
JID - 2984705R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Antigens, CD29)
RN  - 0 (Fibronectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Oligopeptides)
RN  - 0 (Proteoglycans)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (proto-oncogene protein akt)
RN  - 0 (syndecan)
RN  - 67763-96-6 (Insulin-Like Growth Factor I)
RN  - 99896-85-2 (arginyl-glycyl-aspartic acid)
RN  - EC 2.7.1.112 (Receptor, IGF Type 1)
RN  - EC 2.7.1.137 (1-Phosphatidylinositol 3-Kinase)
RN  - EC 2.7.1.37 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.1.37 (p42 MAP Kinase)
RN  - EC 2.7.10.- (extracellular signal-regulated kinase 1)
SB  - IM
EIN - Cancer Res. 2003 Nov 1;63(21):7543
MH  - 1-Phosphatidylinositol 3-Kinase/antagonists &
      inhibitors/metabolism/*physiology
MH  - Antibodies, Monoclonal/pharmacology
MH  - Antigens, CD29/metabolism/*physiology
MH  - Cell Adhesion/drug effects/physiology
MH  - Cell Line, Tumor
MH  - Cell Movement/drug effects/physiology
MH  - Enzyme Activation
MH  - Fibronectins/metabolism
MH  - Human
MH  - Insulin-Like Growth Factor I/antagonists &
      inhibitors/pharmacology/*physiology
MH  - Membrane Glycoproteins/metabolism
MH  - Membrane Microdomains/metabolism
MH  - Mitogen-Activated Protein Kinases/antagonists & inhibitors/metabolism
MH  - Multiple Myeloma/*enzymology/*pathology
MH  - Oligopeptides/pharmacology
MH  - Proteoglycans/metabolism
MH  - Proto-Oncogene Proteins/metabolism/*physiology
MH  - Receptor Cross-Talk/physiology
MH  - Receptor, IGF Type 1/metabolism/physiology
MH  - Signal Transduction/physiology
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - p42 MAP Kinase/antagonists & inhibitors/metabolism
EDAT- 2003/10/03 05:00
MHDA- 2003/12/05 05:00
PST - ppublish
SO  - Cancer Res 2003 Sep 15;63(18):5850-8.

PMID- 14521955
OWN - NLM
STAT- completed
DA  - 20031002
DCOM- 20031125
IS  - 0006-291X
VI  - 310
IP  - 2
DP  - 2003 Oct 17
TI  - Proteolytic processing of IGFBP-related protein-1 (TAF/angiomodulin/mac25)
      modulates its biological activity.
PG  - 612-8
AB  - Insulin-like growth factor (IGF) binding protein-related protein-1
      (IGFBP-rP1) was previously identified as tumor-derived adhesion factor
      (TAF) secreted from human bladder carcinoma cells. It exhibits
      growth-stimulatory activity in synergy with insulin or IGFs. In the
      present study, we found that IGFBP-rP1 was proteolytically cleaved to a
      two-chain form. The cleavage sequence suggested that a trypsin-like serine
      proteinase may be responsible for the processing. The cleavage of
      IGFBP-rP1 led to an almost complete loss of both insulin/IGF-1-binding
      activity and insulin/IGF-1-dependent growth-stimulatory activity. On the
      other hand, the cell attachment activity of IGFBP-rP1 was markedly
      increased by the proteolytic processing. Syndecan-1 was thought to be a
      cell surface receptor for both intact and cleaved IGFBP-rP1 forms.
      Although the proteolytic cleavage of IGFBP-rP1 decreased its
      heparin-binding activity, the cleaved form could bind syndecan-1
      efficiently. Thus the proteolytic processing of IGFBP-rP1 seems to
      modulate its insulin/IGF-dependent and -independent biological functions.
AD  - Division of Cell Biology, Kihara Institute for Biological Research,
      Yokohama City University, 641-12 Maioka-cho, Totsuka-ku, Yokohama
      244-0813, Japan.
FAU - Ahmed, Sanjida
AU  - Ahmed S
FAU - Yamamoto, Kazuhiro
AU  - Yamamoto K
FAU - Sato, Yuichiro
AU  - Sato Y
FAU - Ogawa, Takashi
AU  - Ogawa T
FAU - Herrmann, Andreas
AU  - Herrmann A
FAU - Higashi, Shouichi
AU  - Higashi S
FAU - Miyazaki, Kaoru
AU  - Miyazaki K
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Biochem Biophys Res Commun
JID - 0372516
RN  - 0 (Insulin-Like Growth-Factor-Binding Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (insulin like-growth factor-binding protein-7)
RN  - 0 (syndecan)
RN  - 11061-68-0 (Insulin)
RN  - 67763-96-6 (Insulin-Like Growth Factor I)
SB  - IM
MH  - Amino Acid Sequence
MH  - Cell Adhesion/drug effects
MH  - Cell Division/drug effects
MH  - Cell Line, Tumor
MH  - Human
MH  - Insulin/metabolism/pharmacology
MH  - Insulin-Like Growth Factor I/metabolism/pharmacology
MH  - Insulin-Like Growth-Factor-Binding
      Proteins/chemistry/*metabolism/*pharmacology
MH  - Membrane Glycoproteins/metabolism
MH  - Proteoglycans/metabolism
MH  - Support, Non-U.S. Gov't
EDAT- 2003/10/03 05:00
MHDA- 2003/12/03 05:00
AID - S0006291X03018436 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun 2003 Oct 17;310(2):612-8.

PMID- 14501288
OWN - NLM
STAT- completed
DA  - 20030922
DCOM- 20040114
IS  - 0193-1091
VI  - 25
IP  - 5
DP  - 2003 Oct
TI  - Dermatofibroma: upregulation of syndecan-1 expression in mesenchymal
      tissue.
PG  - 392-8
AB  - Cell surface proteoglycans play a prominent role in tissue remodeling and
      homeostasis. Syndecans, their most prominent members, act by binding to
      growth factors and interstitial matrix molecules. They, thereby, modulate
      the effect of the primary ligand-receptor interaction at the cell membrane
      by increasing the affinity of cell-ligand interactions. Additionally, they
      influence the strength of cell-cell and cell-matrix interactions.
      Syndecan-1 is the prototypical member of this family of proteins. Under
      physiological conditions, its expression is restricted to the epidermis,
      the outer root sheath of the anagen hair follicle, and the sweat gland
      epithelium. The dermal compartment-with the exception of the follicular
      papilla of the anagen hair follicle-physiologically does not express
      syndecan-1. Dermatofibromas are mesenchymal lesions, which often exhibit
      hyperplastic changes in the overlying epidermis. In analogy to the hair
      follicle, they, thereby, can be used as a model for studying
      epithelial-mesenchymal interactions. In the current study, we examined
      dermatofibromas immunohistochemically for syndecan-1 expression. We report
      immunoreactivity for syndecan-1 in dermatofibromas, which correlates
      mainly with the deposition of intercellular matrix material. Syndecan-1 is
      also noted in the stroma surrounding areas of basaloid hyperplasia
      overlying dermatofibromas and may be important in the pathogenesis of this
      inductive phenomenon. In analogy to the follicular papilla of the anagen
      hair follicle, the staining pattern for syndecan-1 in dermatofibromas
      indicates that this cell surface protein is produced by stromal cells and
      most likely serves an essential function in the growth of these common
      mesenchymal cutaneous lesions.
AD  - The Jefferson Center for Dermatopathology, Department of Pathology, Thomas
      Jefferson University, Philadelphia, PA, USA.
FAU - Sellheyer, Klaus
AU  - Sellheyer K
FAU - Smoller, Bruce R
AU  - Smoller BR
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Am J Dermatopathol
JID - 7911005
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (syndecan)
SB  - IM
MH  - Cell Count
MH  - Dermatofibroma/*metabolism/pathology
MH  - Human
MH  - Hyperplasia
MH  - Immunoenzyme Techniques
MH  - Membrane Glycoproteins/*metabolism
MH  - Mesoderm/*metabolism
MH  - Proteoglycans/*metabolism
MH  - Skin Neoplasms/*metabolism/pathology
MH  - Tumor Markers, Biological/metabolism
MH  - Up-Regulation
EDAT- 2003/09/23 05:00
MHDA- 2004/01/15 05:00
PST - ppublish
SO  - Am J Dermatopathol 2003 Oct;25(5):392-8.

PMID- 12975379
OWN - NLM
STAT- in-process
DA  - 20031117
IS  - 0021-9258
VI  - 278
IP  - 47
DP  - 2003 Nov 21
TI  - Syndecan-1 transmembrane and extracellular domains have unique and
      distinct roles in cell spreading.
PG  - 46607-15
AB  - Raji cells expressing syndecan-1 (Raji-S1) adhere and spread when plated
      on heparan sulfate-binding extracellular matrix ligands or monoclonal
      antibody 281.2, an antibody directed against the syndecan-1 extracellular
      domain. Cells plated on monoclonal antibody 281.2 initially extend a broad
      lamellipodium, a response accompanied by membrane ruffling at the cell
      margin. Membrane ruffling then becomes polarized, leading to an elongated
      cell morphology. Previous work demonstrated that the syndecan-1
      cytoplasmic domain is not required for these activities, suggesting
      important roles for the syndecan-1 transmembrane and/or extracellular
      domains in the assembly of a signaling complex necessary for spreading.
      Work described here demonstrates that truncation of the syndecan-1
      extracellular domain does not affect the initial lamellipodial extension
      in the Raji-S1 cells but does inhibit the active membrane ruffling that is
      necessary for cell polarization. Replacement of the entire syndecan-1
      transmembrane domain with leucine residues completely blocks the cell
      spreading. These data demonstrate that the syndecan-1 transmembrane and
      extracellular domains have important but distinct roles in Raji-S1 cell
      spreading; the extracellular domain mediates an interaction that is
      necessary for dynamic cytoskeletal rearrangements whereas an interaction
      of the transmembrane domain is required for the initial spreading
      response.
AD  - Department of Pathology and Laboratory Medicine and Graduate Program in
      Cellular and Molecular Biology, University of Wisconsin-Madison, 1300
      University Avenue, Madison, WI 53706, USA.
FAU - McQuade, Kyle J
AU  - McQuade KJ
FAU - Rapraeger, Alan C
AU  - Rapraeger AC
LA  - eng
GR  - R01 HD 21881/HD/NICHD
PT  - Journal Article
DEP - 20030914
PL  - United States
TA  - J Biol Chem
JID - 2985121R
SB  - IM
EDAT- 2003/09/17 05:00
MHDA- 2003/09/17 05:00
PHST- 2003/Sep/14 [aheadofprint]
AID - 10.1074/jbc.M304775200 [doi]
AID - M304775200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 Nov 21;278(47):46607-15.

PMID- 12969959
OWN - NLM
STAT- in-process
DA  - 20031219
IS  - 0006-4971
VI  - 103
IP  - 1
DP  - 2004 Jan 1
TI  - Infection of HHV-8+ primary effusion lymphoma cells with a recombinant
      Epstein-Barr virus leads to restricted EBV latency, altered phenotype, and
      increased tumorigenicity without affecting TCL1 expression.
PG  - 313-6
AB  - To investigate the role of Epstein-Barr virus (EBV) in the pathogenesis of
      primary effusion lymphoma (PEL), we infected human herpesvirus 8 (HHV-8+)
      but EBV- PEL lines BC-3, CRO-AP/6, and CRO-AP/3 cells with the recombinant
      Akata EBV strain. All EBV-infected clones expressed EBER-1, EBNA-1, and
      LMP2A. The expression of LMP1 and LMP2B was variable. None, however,
      expressed EBNA2-6. The surface markers CD30, CD74, and syndecan-1 were
      down-regulated in EBV convertants. EBV-infected BC-3 and CRO-AP/6 cells
      were highly tumorigenic in severe combined immunodeficiency (SCID) mice in
      contrast to their respective EBV- parental cells. However, neither the
      parental cells nor the virus-converted counterparts expressed TCL1. The
      results showing that PEL cells on in vitro EBV infection do not sustain
      latency III despite the absence of immune pressure indicate that the
      choice of EBV latent gene expression program is cell dependent. The data
      suggest an important role of EBV in the pathogenesis of PEL.
AD  - Department of Experimental Medicine and Pathology, University of Rome, "La
      Sapienza," Rome, Italy. pankaj.trivedi@uniroma1.it
FAU - Trivedi, Pankaj
AU  - Trivedi P
FAU - Takazawa, Kumi
AU  - Takazawa K
FAU - Zompetta, Claudia
AU  - Zompetta C
FAU - Cuomo, Laura
AU  - Cuomo L
FAU - Anastasiadou, Elena
AU  - Anastasiadou E
FAU - Carbone, Antonino
AU  - Carbone A
FAU - Uccini, Stefania
AU  - Uccini S
FAU - Belardelli, Filippo
AU  - Belardelli F
FAU - Takada, Kenzo
AU  - Takada K
FAU - Frati, Luigi
AU  - Frati L
FAU - Faggioni, Alberto
AU  - Faggioni A
LA  - eng
PT  - Journal Article
DEP - 20030911
PL  - United States
TA  - Blood
JID - 7603509
SB  - AIM
SB  - IM
EDAT- 2003/09/13 05:00
MHDA- 2003/09/13 05:00
PHST- 2003/Sep/11 [aheadofprint]
AID - 10.1182/blood-2003-05-1710 [doi]
AID - 2003-05-1710 [pii]
PST - ppublish
SO  - Blood 2004 Jan 1;103(1):313-6.

PMID- 12969225
OWN - NLM
STAT- completed
DA  - 20030912
DCOM- 20031210
IS  - 0904-2512
VI  - 32
IP  - 9
DP  - 2003 Oct
TI  - Immunohistochemical study of syndecan-1 down-regulation and the expression
      of p53 protein or Ki-67 antigen in oral leukoplakia with or without
      epithelial dysplasia.
PG  - 513-21
AB  - BACKGROUND: Leukoplakia is an oral pre-cancerous lesion that sometimes
      develops into squamous cell carcinoma. Therefore, leukoplakia with
      epithelial dysplasia is useful for studying carcinogenesis at the cellular
      level. The purpose of this study was to evaluate a potential association
      between the loss of syndecan-1 expression and the expression of p53
      protein and Ki-67 antigen, and to identify reliable markers for predicting
      malignant changes in oral leukoplakia with epithelial dysplasia. METHODS:
      Changes in the expression of syndecan-1, p53, and Ki-67 were examined
      immunohistochemically in 43 cases of oral leukoplakia with or without
      epithelial dysplasia. The subjects were categorized as: none, 13 cases;
      mild dysplasia, 5 cases; moderate dysplasia, 17 cases; and severe
      dysplasia, 8 cases. The expression of these molecules in normal oral
      epithelia (22 cases) was also investigated. RESULTS: Strong syndecan-1
      expression was observed on the surface of keratinocytes in normal
      epithelium. Immunopositivity was lost gradually as the extent of
      epithelial dysplasia increased. In normal epithelium, p53 and Ki-67
      appeared mainly in the basal cell layer, while they were more widely
      distributed in leukoplakia. Specifically, significant changes were
      observed in the labeling index of p53 and Ki-67 in leukoplakia as
      epithelial dysplasia progressed from mild to moderate or severe.
      CONCLUSION: Our results reveal that overexpression of p53 protein and
      Ki-67 antigen, and down-regulation of syndecan-1 expression in the lower
      part of the epithelium, are associated with dysplastic changes. Therefore,
      the down-regulation of syndecan-1 expression may be the most important
      reliable marker for dysplastic changes.
AD  - Second Department of Oral and Maxillofacial Surgery, Kyushu Dental
      College, Kitakyushu 803-8580, Japan. kuro@kyu-dent.ac.jp
FAU - Kurokawa, Hideo
AU  - Kurokawa H
FAU - Matsumoto, Shinobu
AU  - Matsumoto S
FAU - Murata, Tomoyuki
AU  - Murata T
FAU - Yamashita, Yoshihiro
AU  - Yamashita Y
FAU - Tomoyose, Taiki
AU  - Tomoyose T
FAU - Zhang, Min
AU  - Zhang M
FAU - Fukuyama, Hiroshi
AU  - Fukuyama H
FAU - Takahashi, Tetsu
AU  - Takahashi T
LA  - eng
PT  - Journal Article
PL  - Denmark
TA  - J Oral Pathol Med
JID - 8911934
RN  - 0 (Ki-67 Antigen)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Protein p53)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (syndecan)
SB  - D
SB  - IM
MH  - Adult
MH  - Aged
MH  - Aged, 80 and over
MH  - Cell Transformation, Neoplastic/pathology
MH  - Disease Progression
MH  - *Down-Regulation
MH  - Epithelium/pathology
MH  - Female
MH  - Gene Expression Regulation, Neoplastic
MH  - Human
MH  - Immunohistochemistry
MH  - Keratinocytes/pathology
MH  - Ki-67 Antigen/*analysis
MH  - Leukoplakia, Oral/*pathology
MH  - Male
MH  - Membrane Glycoproteins/*analysis
MH  - Middle Aged
MH  - Mouth Mucosa/pathology
MH  - Mouth Neoplasms/*pathology
MH  - Protein p53/*analysis
MH  - Proteoglycans/*analysis
MH  - Statistics, Nonparametric
MH  - Tumor Markers, Biological/analysis
EDAT- 2003/09/13 05:00
MHDA- 2003/12/12 05:00
AID - 117 [pii]
PST - ppublish
SO  - J Oral Pathol Med 2003 Oct;32(9):513-21.

PMID- 12953803
OWN - NLM
STAT- completed
DA  - 20030904
DCOM- 20031020
IS  - 0925-5710
VI  - 78
IP  - 2
DP  - 2003 Aug
TI  - Survival and proliferation factors of normal and malignant plasma cells.
PG  - 106-13
AB  - Since the first identification of interleukin (IL)-6 as a myeloma cell
      growth factor by Dr. Kawano's and Dr. Klein's groups 14 years ago,
      numerous studies have emphasized its major roles in the emergence of
      malignant plasma cells in vivo and in the generation of normal plasma
      cells. Four transcription factors control B-cell differentiation into
      plasma cells. The B-cell transcription factor pax-5 is mainly responsible
      for a B-cell phenotype, and bcl-6 represses the plasma cell transcription
      factor blimp-1 and plasma cell differentiation. bcl-6 expression is
      triggered by CD40 and IL-4 activation. A lack of CD40 and IL-4 activation
      yields a down-regulation of bcl-6 expression, and IL-6 stimulation yields
      an up-regulation of blimp-1, mainly through STAT3 activation. Blimp-1
      further down-regulates bcl-6 and pax-5 expression and makes plasma cell
      differentiation possible. IL-6 as well as IL-10 up-regulate XBP-1. XBP-1
      is another transcription factor that is involved in plasma cell
      differentiation and whose gene expression is shut down by pax-5. The
      plasma cell transcription factors blimp-1 and XBP-1 are up-regulated, and
      the B-cell transcription factors bcl-6 and pax-5 are down-regulated, in
      malignant cells compared to B-cells. Apart from the recent identification
      of these 4 transcription factors, the factors involved in normal plasma
      cell generation are mostly unknown. Regarding malignant plasma cells, 3
      categories of growth factors have been identified: (1) the IL-6 family
      cytokines, IL-10, and interferon alpha that activate the Janus
      kinase-signal transducer and activator of transcription (JAK/STAT) and
      mitogen-activated protein (MAP) kinase pathways; (2) growth factors
      activating the phosphatidylinositol (PI)-3 kinase/AKT and MAP kinase
      pathways, unlike the JAK/STAT pathway (insulin-like growth factor 1,
      hepatocyte growth factor, and members of the epidermal growth factor
      family able to bind syndecan-1 proteoglycan); and (3) B-cell-activating
      factor (BAFF) or proliferation-inducing ligand (APRIL) that activate the
      nuclear factor KB and PI-3 kinase/AKT pathways. BAFF and APRIL bind to
      BAFF receptor and TACI and are major B-cell survival factors. Recent data
      indicate that these various growth factors may cooperate to provide
      optimum signaling because they are localized together and with cytoplasmic
      transduction elements in caveolinlinked membrane caveolae. The
      identification of these myeloma cell growth factors and of the associated
      transduction pathways should provide novel therapeutic targets in multiple
      myeloma.
AD  - INSERM U475 and Unit for Cellular and Gene Therapy, CHU Montpellier,
      Montpellier, France. klein@montp.inserm.fr
FAU - Klein, Bernard
AU  - Klein B
FAU - Tarte, Karin
AU  - Tarte K
FAU - Jourdan, Michel
AU  - Jourdan M
FAU - Mathouk, Karene
AU  - Mathouk K
FAU - Moreaux, Jerome
AU  - Moreaux J
FAU - Jourdan, Eric
AU  - Jourdan E
FAU - Legouffe, Eric
AU  - Legouffe E
FAU - De Vos, John
AU  - De Vos J
FAU - Rossi, Jean Francois
AU  - Rossi JF
LA  - eng
PT  - Journal Article
PT  - Review
PT  - Review Literature
PL  - Ireland
TA  - Int J Hematol
JID - 9111627
RN  - 0 (Interleukin-6)
RN  - 0 (Membrane Proteins)
RN  - 0 (TALL-1 protein)
RN  - 0 (Tumor Necrosis Factor)
RN  - 62229-50-9 (Epidermal Growth Factor)
RN  - 67256-21-7 (Hepatocyte Growth Factor)
RN  - 67763-96-6 (Insulin-Like Growth Factor I)
SB  - IM
MH  - Cell Division/immunology
MH  - Cell Survival/immunology
MH  - Epidermal Growth Factor/metabolism
MH  - Hepatocyte Growth Factor/metabolism
MH  - Human
MH  - Insulin-Like Growth Factor I/metabolism
MH  - Interleukin-6/metabolism
MH  - Leukemia, Plasmacytic/metabolism/*pathology
MH  - Membrane Proteins/metabolism
MH  - Plasma Cells/*cytology/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Tumor Necrosis Factor/metabolism
RF  - 81
EDAT- 2003/09/05 05:00
MHDA- 2003/10/21 05:00
PST - ppublish
SO  - Int J Hematol 2003 Aug;78(2):106-13.

PMID- 12947106
OWN - NLM
STAT- completed
DA  - 20031103
DCOM- 20040105
IS  - 0021-9258
VI  - 278
IP  - 45
DP  - 2003 Nov 7
TI  - Normal human keratinocytes bind to the alpha3LG4/5 domain of unprocessed
      laminin-5 through the receptor syndecan-1.
PG  - 44168-77
AB  - Basal keratinocytes of the epidermis adhere to their underlying basement
      membrane through a specific interaction with laminin-5, which is composed
      by the association of alpha3, beta3, and gamma2 chains. Laminin-5 has the
      ability to induce either stable cell adhesion or migration depending on
      specific processing of different parts of the molecule. One event results
      in the cleavage of the carboxyl-terminal globular domains 4 and 5 (LG4/5)
      of the alpha3 chain. In this study, we recombinantly expressed the human
      alpha3LG4/5 fragment in mammalian cells, and we show that this fragment
      induces adhesion of normal human keratinocytes and fibrosarcoma-derived
      HT1080 cells in a heparan- and chondroitin sulfate-dependent manner.
      Immunoprecipitation experiments with Na2 35SO4-labeled keratinocyte and
      HT1080 cell lysates as well as immunoblotting experiments revealed that
      the major proteoglycan receptor for the alpha3LG4/5 fragment is
      syndecan-1. Syndecan-4 from keratinocytes also bound to alpha3LG4/5.
      Furthermore we could show for the first time that unprocessed laminin-5
      specifically binds syndecan-1, while processed laminin-5 does not. These
      results demonstrate that the LG4/5 modules within unprocessed laminin-5
      permit its cell binding activity through heparan and chondroitin sulfate
      chains of syndecan-1 and reinforce previous data suggesting specific
      properties for the precursor molecule.
AD  - Institut de Biologie et Chimie des Proteines, Unite Mixte de Recherche
      5086, Institut Federatif de Recherche 128 BioSciences Lyon-Gerland, 7
      passage du Vercors, 69367 Lyon, France.
FAU - Okamoto, Osamu
AU  - Okamoto O
FAU - Bachy, Sophie
AU  - Bachy S
FAU - Odenthal, Uwe
AU  - Odenthal U
FAU - Bernaud, Janine
AU  - Bernaud J
FAU - Rigal, Dominique
AU  - Rigal D
FAU - Lortat-Jacob, Hugues
AU  - Lortat-Jacob H
FAU - Smyth, Neil
AU  - Smyth N
FAU - Rousselle, Patricia
AU  - Rousselle P
LA  - eng
PT  - Journal Article
DEP - 20030828
PL  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Sulfates)
RN  - 0 (Sulfur Radioisotopes)
RN  - 0 (kalinin)
RN  - 0 (syndecan)
RN  - 170834-93-2 (laminin alpha 3)
RN  - 7757-82-6 (sodium sulfate)
RN  - 9007-28-7 (Chondroitin Sulfates)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 4.2.2. (Polysaccharide-Lyases)
RN  - EC 4.2.2.4 (Chondroitin ABC Lyase)
RN  - EC 4.2.2.8 (heparitinsulfate lyase)
SB  - IM
MH  - Animals
MH  - Binding Sites
MH  - CHO Cells
MH  - Cell Adhesion
MH  - Cell Adhesion Molecules/*chemistry/metabolism
MH  - Cell Line
MH  - Chondroitin ABC Lyase/metabolism
MH  - Chondroitin Sulfates/analysis/metabolism/pharmacology
MH  - Embryo
MH  - Fibrosarcoma
MH  - Gene Expression
MH  - Hamsters
MH  - Heparitin Sulfate/analysis/metabolism/pharmacology
MH  - Human
MH  - Immunoblotting
MH  - Immunosorbent Techniques
MH  - Keratinocytes/*metabolism
MH  - Kidney
MH  - Laminin/*chemistry/genetics/*metabolism
MH  - Membrane Glycoproteins/chemistry/*metabolism
MH  - Polysaccharide-Lyases/metabolism
MH  - Proteoglycans/chemistry/*metabolism
MH  - Recombinant Proteins
MH  - Sulfates
MH  - Sulfur Radioisotopes
MH  - Support, Non-U.S. Gov't
MH  - Transfection
MH  - Tumor Cells, Cultured
EDAT- 2003/08/30 05:00
MHDA- 2004/01/06 05:00
PHST- 2003/Aug/28 [aheadofprint]
AID - 10.1074/jbc.M300726200 [doi]
AID - M300726200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 Nov 7;278(45):44168-77.

PMID- 12935821
OWN - NLM
STAT- in-process
DA  - 20030825
IS  - 0945-053X
VI  - 22
IP  - 4
DP  - 2003 Jun
TI  - An extracellular matrix-specific microarray allowed the identification of
      target genes downstream of discoidin domain receptors.
PG  - 373-81
AB  - The two discoidin domain receptors, DDR1 and DDR2, are tyrosine kinases
      that are activated by collagen and are essential regulators of cell-matrix
      communication. However, the target genes downstream of activated DDRs and
      their physiological significance are largely unknown. Here, we describe a
      novel method to dissect signaling pathways induced by extracellular matrix
      (ECM) receptors. Using the doxycycline-inducible repression system
      (tet-off), we generated human fibrosarcoma and mouse fibroblast cell lines
      over-expressing DDR1 or DDR2. These cell lines were employed for gene
      expression analysis using microarrays specific for human and mouse genes
      coding for ECM proteins or ECM-interacting factors. We found that
      approximately 10% of the genes studied were up- or down-regulated more
      than twofold in response to signals generated by over-expressing DDRs. A
      common event downstream of DDR1 and DDR2 in human and mouse cells was the
      up-regulation of P-selectin glycoprotein ligand. Key target genes
      repressed upon DDR activation were agrin, syndecan-1 and alpha3 integrin.
      ECM-specific microarrays were found a valuable tool to dissect gene
      expression changes induced by collagen-receptor signaling pathways.
AD  - Department of Laboratory Medicine and Pathobiology, University of Toronto,
      Toronto, Ont, Canada M5S 1A8.
FAU - Faraci, Elena
AU  - Faraci E
FAU - Eck, Maresa
AU  - Eck M
FAU - Gerstmayer, Bernhard
AU  - Gerstmayer B
FAU - Bosio, Andreas
AU  - Bosio A
FAU - Vogel, Wolfgang F
AU  - Vogel WF
LA  - eng
PT  - Journal Article
PL  - Germany
TA  - Matrix Biol
JID - 9432592
SB  - IM
EDAT- 2003/08/26 05:00
MHDA- 2003/08/26 05:00
AID - S0945053X03000532 [pii]
PST - ppublish
SO  - Matrix Biol 2003 Jun;22(4):373-81.

PMID- 12933811
OWN - NLM
STAT- completed
DA  - 20031110
DCOM- 20031224
IS  - 0021-9258
VI  - 278
IP  - 46
DP  - 2003 Nov 14
TI  - Biological activities of homologous loop regions in the laminin alpha
      chain G domains.
PG  - 45697-705
AB  - Laminin alpha chains (alpha1-alpha5 chains) have diverse chain-specific
      biological functions. The LG4 modules of laminin alpha chains consist of a
      14-stranded beta-sheet (A-N) sandwich structure. Several biologically
      active sequences have been identified in the connecting loop regions.
      Here, we evaluated the biological activities of the loop regions of the E
      and F strands in the LG4 modules using five homologous peptides from each
      of the mouse alpha chains (EF-1: DYATLQLQEGRLHFMFDLG, alpha1 chain
      2747-2765; EF-2: DFGTVQLRNGFPFFSYDLG, alpha2 chain 2808-2826; EF-3:
      RDSFVALYLSEGHVIFALG, alpha3 chain 2266-2284; EF-4: DFMTLFLAHGRLVFMFNVG,
      alpha4 chain 1511-1529; EF-5: SPSLVLFLNHGHFVAQTEGP, alpha5 chain
      3304-3323). These homologous peptides showed chain-specific cell
      attachment and neurite outgrowth activities. Well organized actin stress
      fibers and focal contacts with vinculin accumulation were observed in
      fibroblasts attached on EF-1, whereas fibroblasts on EF-2 and EF-4 showed
      filopodia with ruffling. Fibroblast attachment to EF-2 and EF-4 was
      mediated by syndecan-2. In contrast, EF-1 promoted alpha2beta1
      integrin-mediated fibroblast attachment and inhibited fibroblast
      attachment to a recombinant laminin alpha1 chain LG4-5. The receptors for
      EF-3 and EF-5 are unknown. Further, when the active core sequence of EF-1
      was cyclized, utilizing two additional cysteine residues at both the N and
      C termini through a disulfide bridge, the cyclic peptide significantly
      enhanced integrin-mediated cell attachment. These results indicate that
      integrin-mediated cell attachment to the EF-1 sequence is
      conformation-dependent and that the loop structure is important for the
      activity. The homologous peptides, which promote either integrin- or
      syndecan-mediated cell attachment, may be useful for understanding the
      cell type- and chain-specific biological activities of the laminins.
AD  - Graduate School of Environmental Earth Science, Hokkaido University,
      Sapporo 060-0810, Japan.
FAU - Suzuki, Nobuharu
AU  - Suzuki N
FAU - Nakatsuka, Hiroko
AU  - Nakatsuka H
FAU - Mochizuki, Mayumi
AU  - Mochizuki M
FAU - Nishi, Norio
AU  - Nishi N
FAU - Kadoya, Yuichi
AU  - Kadoya Y
FAU - Utani, Atsushi
AU  - Utani A
FAU - Oishi, Shinya
AU  - Oishi S
FAU - Fujii, Nobutaka
AU  - Fujii N
FAU - Kleinman, Hynda K
AU  - Kleinman HK
FAU - Nomizu, Motoyoshi
AU  - Nomizu M
LA  - eng
PT  - Journal Article
DEP - 20030820
PL  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (Actins)
RN  - 0 (Disulfides)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Laminin)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptides)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (laminin alpha 2)
RN  - 0 (laminin alpha 4)
RN  - 0 (laminin alpha5)
RN  - 0 (syndecan)
RN  - 125361-02-6 (Vinculin)
RN  - 149769-25-5 (fibroglycan)
RN  - 151186-83-3 (laminin A)
RN  - 170834-93-2 (laminin alpha 3)
RN  - 60-00-4 (Edetic Acid)
RN  - 9005-49-6 (Heparin)
SB  - IM
MH  - Actins/biosynthesis/chemistry
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Cell Adhesion
MH  - Cell Line
MH  - Cell Line, Tumor
MH  - Cytoskeleton/metabolism
MH  - Disulfides
MH  - Dose-Response Relationship, Drug
MH  - Edetic Acid/pharmacology
MH  - Fibroblasts/metabolism
MH  - Heparan Sulfate Proteoglycan/biosynthesis
MH  - Heparin/pharmacology
MH  - Human
MH  - Laminin/*chemistry/*physiology
MH  - Membrane Glycoproteins/biosynthesis/chemistry
MH  - Mice
MH  - Molecular Sequence Data
MH  - Neurons/metabolism
MH  - PC12 Cells
MH  - Peptides/chemistry
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/biosynthesis/chemistry
MH  - Rats
MH  - Recombinant Proteins/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Vinculin/biosynthesis
EDAT- 2003/08/23 05:00
MHDA- 2003/12/25 05:00
PHST- 2003/Aug/20 [aheadofprint]
AID - 10.1074/jbc.M304667200 [doi]
AID - M304667200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 Nov 14;278(46):45697-705.

PMID- 12929127
OWN - NLM
STAT- completed
DA  - 20030820
DCOM- 20031014
LR  - 20031114
IS  - 0360-4012
VI  - 73
IP  - 5
DP  - 2003 Sep 1
TI  - Matrix metalloproteinase-dependent shedding of syndecan-3, a transmembrane
      heparan sulfate proteoglycan, in Schwann cells.
PG  - 593-602
AB  - Schwann cells transiently express the transmembrane heparan sulfate
      proteoglycan syndecan-3 during the late embryonic and early postnatal
      periods of peripheral nerve development. Neonatal rat Schwann cells
      released soluble syndecan-3 into the culture medium by a process that was
      blocked by inhibition of endogenous matrix metalloproteinase activity.
      When Schwann cells were plated on a substratum that binds syndecan-3, the
      released proteoglycan bound to the substratum adjacent to the cell border.
      Membrane-anchored syndecan-3 was concentrated in actin-containing
      filopodia that projected from the lateral edges of the Schwann cell
      membrane. Membrane shedding was specific for syndecan-3 and was not
      observed for the related proteoglycan syndecan-1. Analysis of Schwann
      cells transfected with wild-type and chimeric syndecan-1 and syndecan-3
      cDNAs revealed that membrane shedding was a property of the syndecan-3
      ectodomain. Inhibition of syndecan-3 release significantly enhanced
      Schwann cell adhesion and process extension on dishes coated with the
      non-collagenous N-terminal domain of alpha4(V) collagen, which binds
      syndecan-3 and mediates heparan sulfate-dependent Schwann cell adhesion.
      Matrix metalloproteinase-dependent syndecan-3 shedding was also observed
      in newborn rat peripheral nerve tissue. Syndecan-3 shedding in peripheral
      nerve tissue was age specific, and was not observed during later stages of
      postnatal nerve development. These results demonstrate that Schwann cell
      syndecan-3 is subject to matrix metalloproteinase-dependent membrane
      processing, which modulates the biological function of this proteoglycan.
CI  - Copyright 2003 Wiley-Liss, Inc.
AD  - Weis Center for Research, Geisinger Clinic, Danville, Pennsylvania
      17822-2601, USA.
FAU - Asundi, Vinod K
AU  - Asundi VK
FAU - Erdman, Robert
AU  - Erdman R
FAU - Stahl, Richard C
AU  - Stahl RC
FAU - Carey, David J
AU  - Carey DJ
LA  - eng
GR  - NS21925/NS/NINDS
PT  - Journal Article
PL  - United States
TA  - J Neurosci Res
JID - 7600111
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan 3)
RN  - EC 3.4.24.- (Matrix Metalloproteinases)
SB  - IM
MH  - Age Factors
MH  - Animals
MH  - Animals, Newborn
MH  - Blotting, Western
MH  - Cell Adhesion/physiology
MH  - Cells, Cultured
MH  - Comparative Study
MH  - Enzyme Inhibitors/pharmacology
MH  - Fluorescent Antibody Technique
MH  - Heparan Sulfate Proteoglycan/metabolism
MH  - Matrix Metalloproteinases/antagonists & inhibitors/*metabolism
MH  - Membrane Glycoproteins/analysis/drug effects/genetics/*metabolism
MH  - Peripheral Nerves/chemistry/*growth & development/metabolism
MH  - Protein Structure, Tertiary
MH  - Proteoglycans/analysis/drug effects/genetics/*metabolism
MH  - Rats
MH  - Schwann Cells/chemistry/cytology/*physiology
MH  - Support, U.S. Gov't, P.H.S.
MH  - Transfection
EDAT- 2003/08/21 05:00
MHDA- 2003/10/15 05:00
AID - 10.1002/jnr.10699 [doi]
PST - ppublish
SO  - J Neurosci Res 2003 Sep 1;73(5):593-602.

PMID- 12926067
OWN - NLM
STAT- completed
DA  - 20030820
DCOM- 20030930
IS  - 0250-7005
VI  - 23
IP  - 4
DP  - 2003 Jul-Aug
TI  - Large matrix proteoglycans, versican and perlecan, are expressed and
      secreted by human leukemic monocytes.
PG  - 3303-9
AB  - THP-1 is a monocytic cell line originally derived from a patient with
      acute monocytic leukemia. Interactions of THP-1 cells with other cells and
      their microenvironment are largely determined by proteoglycans (PGs), the
      identity of which has not been determined. Previous studies on
      glycosaminoglycan expression by THP-1 cells and peripheral blood
      mononuclear cells from healthy individuals showed that both cell types
      secrete mainly chondroitin sulfate PGs to the culture medium, whereas
      heparan sulfate PGs are mainly retarded at the cell membrane. However,
      limited data on the type of PGs synthesized by THP-1 is available. In this
      study, the identification of PG types synthesised by THP-1 cells, which
      are not differentiated to macrophages, was examined. Analysis at the mRNA
      level by RT-PCR showed the expression of six cell membrane-associated PGs:
      syndecan-1, -2 and -4, glypican-1, thrombomodulin and CD44. Cell
      extraction, ion-exchange chromatography and dot blot analysis of the
      isolated PG populations with monoclonal antibodies showed the presence of
      syndecan-1 and thrombomodulin; the other two syndecans were not detected
      in any of the isolated populations. The synthesis of matrix PGs was also
      studied. THP-1 monocytes were positive for the mRNA encoding for versican
      and perlecan, but not for those encoding for decorin, biglycan, betaglycan
      and fibromodulin. The mRNA encoding for two versican splice variants V0
      (351 bp) and V1 (386 bp), but not for V2, were identified. Biochemical
      analysis showed the presence of perlecan and of two populations of
      versican in culture medium with protein cores of average molecular sizes
      similar to those of V0 and V1. The production of these large matrix PGs by
      THP-1 monocytes is reported for the first time and may be of importance in
      monocyte malignant transformation and differentiation.
AD  - Department of Chemistry, Section of Organic Chemistry, Biochemistry &
      Natural Products, University of Patras, 26500 Patras, Greece.
FAU - Makatsori, Evdokia
AU  - Makatsori E
FAU - Lamari, Fotini N
AU  - Lamari FN
FAU - Theocharis, Achilleas D
AU  - Theocharis AD
FAU - Anagnostides, Stavros
AU  - Anagnostides S
FAU - Hjerpe, Anders
AU  - Hjerpe A
FAU - Tsegenidis, Theodore
AU  - Tsegenidis T
FAU - Karamanos, Nikos K
AU  - Karamanos NK
LA  - eng
PT  - Journal Article
PL  - Greece
TA  - Anticancer Res
JID - 8102988
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Protein Isoforms)
RN  - 0 (Proteochondroitin Sulfates)
RN  - 0 (RNA, Messenger)
RN  - 126968-45-4 (versican)
RN  - 143972-95-6 (perlecan)
SB  - IM
MH  - Gene Expression
MH  - Heparan Sulfate Proteoglycan/*biosynthesis/secretion
MH  - Human
MH  - Leukemia, Monocytic, Acute
MH  - Monocytes/*metabolism/physiology/secretion
MH  - Protein Isoforms
MH  - Proteochondroitin Sulfates/*biosynthesis/secretion
MH  - RNA, Messenger/biosynthesis/genetics
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Support, Non-U.S. Gov't
MH  - Tumor Cells, Cultured
EDAT- 2003/08/21 05:00
MHDA- 2003/10/01 05:00
PST - ppublish
SO  - Anticancer Res 2003 Jul-Aug;23(4):3303-9.

PMID- 12920224
OWN - NLM
STAT- in-process
DA  - 20030815
IS  - 0893-3952
VI  - 16
IP  - 8
DP  - 2003 Aug
TI  - Induced expression of syndecan-1 in the stroma of head and neck squamous
      cell carcinoma.
PG  - 796-801
AB  - Syndecan-1 (CD138), a cell-surface heparan sulfate proteoglycan, is
      involved in cell-cell, cell-matrix interaction and growth factor binding.
      Loss of expression of syndecan-1 in tumor cells leads to decreased
      intercellular cohesion, increased potential for tumor invasiveness, and
      metastatic spread. Furthermore, induction of syndecan-1 expression in the
      tumor stroma has been postulated to promote tumor angiogenesis via its
      binding to growth factors such as basic fibroblast growth factor. Although
      syndecan-1 expression within tumor cells has been investigated in head and
      neck squamous cell carcinoma, stromal expression has not been studied in
      detail. We analyzed 38 cases of head and neck squamous cell carcinoma by
      immunohistochemical staining for syndecan-1 expression within the stroma.
      The expression of syndecan-1 within tumor cells of various histologic
      grades of differentiation, squamous cell carcinoma in situ cells, and
      benign squamous epithelium was also determined. Variable levels of
      diminished syndecan-1 expression were noted within the dysplastic cells of
      9 of 16 (60%) squamous cell carcinoma in situ lesions and in all 38 (100%)
      invasive squamous cell carcinoma. In general, higher levels of syndecan-1
      expression were observed in the well-differentiated tumors, in contrast to
      significant reduction of expression seen in poorly differentiated tumors.
      Syndecan-1 expression was observed within the stroma (in fibroblasts)
      surrounding infiltrating carcinoma cells in 28 of 38 (74%) cases. The
      intensity of syndecan-1 staining within the stroma showed generally an
      inverse correlation with the degree of tumor cell differentiation.
      Syndecan-1 expression was not detected in the stroma beneath normal
      squamous epithelium or adjacent to areas of squamous cell carcinoma in
      situ. We conclude that induced expression of syndecan-1 in the stroma
      surrounding tumor cells of invasive head and neck squamous cell carcinoma
      is a frequent event. The increased stromal syndecan-1 expression, coupled
      with its loss from the surface of carcinoma cells, may contribute to tumor
      cell invasion and the development of metastases.
AD  - Department of Pathology, University of Arkansas for Medical Sciences and
      Central Arkansas Veterans Healthcare System, Little Rock, Arkansas 72205,
      USA. mukunyadziperkins@uams.edu
FAU - Mukunyadzi, Perkins
AU  - Mukunyadzi P
FAU - Liu, Kela
AU  - Liu K
FAU - Hanna, Ehab Y
AU  - Hanna EY
FAU - Suen, James Y
AU  - Suen JY
FAU - Fan, Chun-Yang
AU  - Fan CY
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Mod Pathol
JID - 8806605
SB  - IM
EDAT- 2003/08/16 05:00
MHDA- 2003/08/16 05:00
PST - ppublish
SO  - Mod Pathol 2003 Aug;16(8):796-801.

PMID- 12917256
OWN - NLM
STAT- in-process
DA  - 20030814
IS  - 0953-8178
VI  - 15
IP  - 9
DP  - 2003 Sep
TI  - Increased plasma cell frequency and accumulation of abnormal
      syndecan-1plus T-cells in Igmu-deficient/lpr mice.
PG  - 1045-52
AB  - The expression of muH chain is an important checkpoint in B cell
      development. In mice deficient for IgM transmembrane tail exons (muMT
      mice) B cell development is blocked at the pro-B stage. However, we showed
      that Fas-deficient muMT mice (muMT/lpr) develop a very small population of
      isotype-switched B cells and produce high titers of self-reactive serum
      antibodies. In addition, muMT/lpr mice develop severe lymphoproliferation
      and both pathologic processes occur at young ages. This may suggest that
      lack of Fas-Fas ligand signaling exacerbates murine lupus in B cell
      lymphopenic mice. To test this we analyzed antibody and plasma cell
      formation, and accumulation of abnormal T cells in muMT/lpr mice. Our
      results show that the muMT/lpr mouse is particularly permissive for the
      development and accumulation of antibody-producing cells, thereby
      explaining the high titers of serum antibodies in these mice. In addition,
      we found that accumulating cells in spleen and lymph nodes of muMT/lpr
      mice are alphabeta T cells expressing the abnormal B220+/CD3+ surface
      markers, a phenotype also described for other Fas-deficient mouse models.
      Strikingly, we found that accumulating cells in muMT/lpr mice express the
      membrane proteoglycan syndecan-1, a known plasma cell marker. Development
      of these cells is blocked in mice deficient for TCRbeta and TCRdelta. We
      also found that both antibody production and lymphoproliferation in
      muMT/lpr mice are Th1 regulated. Our results, therefore, suggest that in
      the muMT/lpr mouse model a small population of isotype-switched B cells is
      sufficient for the initiation and propagation of Th1-regulated murine
      lupus.
AD  - Department of Immunology, Bruce Rappaport Faculty of Medicine,
      Technion-Israel Institute of Technology, Haifa 31096, Israel.
FAU - Seagal, Jane
AU  - Seagal J
FAU - Leider, Nira
AU  - Leider N
FAU - Wildbaum, Gizi
AU  - Wildbaum G
FAU - Karin, Nathan
AU  - Karin N
FAU - Melamed, Doron
AU  - Melamed D
LA  - eng
PT  - Journal Article
PL  - England
TA  - Int Immunol
JID - 8916182
SB  - IM
EDAT- 2003/08/15 05:00
MHDA- 2003/08/15 05:00
PST - ppublish
SO  - Int Immunol 2003 Sep;15(9):1045-52.

PMID- 12911939
OWN - NLM
STAT- completed
DA  - 20030812
DCOM- 20040114
IS  - 1024-5332
VI  - 8
IP  - 4
DP  - 2003 Aug
TI  - Syndecan-1 in multiple myeloma: relationship to conventional prognostic
      factors.
PG  - 221-8
AB  - Syndecan-1 (CD138) mediates myeloma cell adhesion, and loss of syndecan-1
      from the cell surface may contribute to myeloma cell proliferation and
      dissemination and influence the prognosis in patients with multiple
      myeloma (MM). In order to test this hypothesis, we have evaluated
      syndecan-1 expression on the surface of malignant plasma cells and soluble
      forms of syndecan-1 in the serum of 25 newly diagnosed MM patients by flow
      cytometry and immunosorbent assay. Soluble syndecan-1 levels were
      significantly higher in MM as compared to controls (P<0.001). Cellular and
      soluble syndecan-1 was significantly inversely correlated (r=-0.89,
      P<0.001). The soluble syndecan-1 was significantly higher in non-
      responders to chemotherapy when compared to responders (P<0.01), and in
      non- survivors as compared to survivors (P<0.001). In contrast, cellular
      syndecan-1 expression was significantly lower in non- responders when
      compared to responders (P<0.01), and in non- survivors as compared to
      survivors (P<0.05). The levels of soluble syndecan-1 increased from stage
      I through stage II to stage III, whereas cellular syndecan-1 expression
      were decreased from high levels in stage III down to a low in stage I,
      with a statistically significant difference (P<0.01, P<0.05,
      respectively). There was a significant positive correlation between
      soluble syndecan-1 and plasma cell count (r=0.079, P<0.001), beta2
      microglobulin (r=0.85, P<0.001), serum creatinine (r=0.84, P<0.001),
      C-reactive protein (r=0.082, P<0.001), alkaline phosphatase (r=0.58,
      P<0.05) and serum calcium (r=0.77, P<0.01) and a negative correlation with
      hemoglobin level (r=-0.78, P<0.01), platelets count (r=-0.82, P<0.01) and
      Albumin level (r=-0.64, P<0.01). Cox regression analysis using soluble
      syndecan-1 at mean-2SD of the controls could correctly classify patient
      outcome in 84.0%. The addition of beta2 microglobulin to soluble
      syndecan-1 increased the predictability of the patients' outcome to 96.7%.
      We conclude that soluble syndecan-1 levels are negatively correlated to
      the cellular form and that high levels of soluble syndecan-1 and lower
      expression of cellular syndecan-1 at diagnosis are negative prognostic
      factors. Assessment of soluble syndecan-1 and beta2 microglobulin at
      diagnosis is an independent prognostic system for MM.
AD  - Hematology Unit, Clinical pathology Department, Mansoura Faculty of
      Medicine, Mansoura University, Mansoura, Egypt. salaharef@yahoo.com
FAU - Aref, Salah
AU  - Aref S
FAU - Goda, T
AU  - Goda T
FAU - El-Sherbiny, M
AU  - El-Sherbiny M
LA  - eng
PT  - Journal Article
PL  - England
TA  - Hematology
JID - 9708388
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Tumor Markers, Biological)
RN  - 0 (beta 2-Microglobulin)
RN  - 0 (syndecan)
SB  - IM
MH  - Case-Control Studies
MH  - Female
MH  - Human
MH  - Male
MH  - Membrane Glycoproteins/*analysis/blood/physiology
MH  - Middle Aged
MH  - Multiple Myeloma/chemistry/*diagnosis/etiology
MH  - Plasma Cells/chemistry/pathology
MH  - Prognosis
MH  - Proteoglycans/*analysis/blood/physiology
MH  - Regression Analysis
MH  - Risk Factors
MH  - Severity of Illness Index
MH  - Solubility
MH  - Survival Analysis
MH  - Treatment Outcome
MH  - Tumor Markers, Biological/analysis/blood
MH  - beta 2-Microglobulin/analysis
EDAT- 2003/08/13 05:00
MHDA- 2004/01/15 05:00
AID - 10.1080/1024533031000153630 [doi]
AID - 927ULGMVKJC190J2 [pii]
PST - ppublish
SO  - Hematology 2003 Aug;8(4):221-8.

PMID- 12904296
OWN - NLM
STAT- completed
DA  - 20031013
DCOM- 20031203
IS  - 0021-9258
VI  - 278
IP  - 42
DP  - 2003 Oct 17
TI  - Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1
      stimulates cell migration.
PG  - 40764-70
AB  - The transmembrane heparan sulfate proteoglycan syndecan-1 was identified
      from a human placenta cDNA library by the expression cloning method as a
      gene product that interacts with membrane type matrix metalloproteinase-1
      (MT1-MMP). Co-expression of MT1-MMP with syndecan-1 in HEK293T cells
      promoted syndecan-1 shedding, and concentration of cell-associated
      syndecan-1 was reduced. Treatment of cells with MMP inhibitor BB-94 or
      tissue inhibitor of MMP (TIMP)-2 but not TIMP-1 interfered with the
      syndecan-1 shedding promoted by MT1-MMP expression. In contrast,
      syndecan-1 shedding induced by 12-O-tetradecanoylphorbol-13-acetate
      treatment was inhibited by BB-94 but not by either TIMP-1 or TIMP-2.
      Shedding of syndecan-1 was also induced by MT3-MMP but not by other
      MT-MMPs. Recombinant syndecan-1 core protein was shown to be cleaved by
      recombinant MT1-MMP or MT3-MMP preferentially at the Gly245-Leu246 peptide
      bond. HT1080 fibrosarcoma cells stably transfected with the syndecan-1
      cDNA (HT1080/SDC), which express endogenous MT1-MMP, spontaneously shed
      syndecan-1. Migration of HT1080/SDC cells on collagen-coated dishes was
      significantly slower than that of control HT1080 cells. Treatment of
      HT1080/SDC cells with BB-94 or TIMP-2 induced accumulation of syndecan-1
      on the cell surface, concomitant with further retardation of cell
      migration. Substitution of Gly245 of syndecan-1 with Leu significantly
      reduced shedding from HT1080/SDC cells and cell migration. These results
      suggest that the shedding of syndecan-1 promoted by MT1-MMP through the
      preferential cleavage of Gly245-Leu246 peptide bond stimulates cell
      migration.
AD  - Department of Molecular Virology and Oncology, Cancer Research Institute,
      Graduate School of Medical Science, Kanazawa University, 13-1
      Takara-machi, Kanazawa, Ishikawa 920-0934, Japan.
FAU - Endo, Kazuhira
AU  - Endo K
FAU - Takino, Takahisa
AU  - Takino T
FAU - Miyamori, Hisashi
AU  - Miyamori H
FAU - Kinsen, Hidenori
AU  - Kinsen H
FAU - Yoshizaki, Tomokazu
AU  - Yoshizaki T
FAU - Furukawa, Mitsuru
AU  - Furukawa M
FAU - Sato, Hiroshi
AU  - Sato H
LA  - eng
PT  - Journal Article
DEP - 20030806
PL  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (Carcinogens)
RN  - 0 (DNA, Complementary)
RN  - 0 (Epitopes)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptides)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Tissue-Inhibitor of Metalloproteinase-1)
RN  - 0 (syndecan)
RN  - 127497-59-0 (Tissue Inhibitor-of Metalloproteinase-2)
RN  - 16561-29-8 (Tetradecanoylphorbol Acetate)
RN  - 56-40-6 (Glycine)
RN  - 61-90-5 (Leucine)
RN  - EC 3.4.24 (Metalloendopeptidases)
RN  - EC 3.4.24.- (membrane-type 1 matrix metalloproteinase)
SB  - IM
MH  - Binding Sites
MH  - Carcinogens
MH  - Cell Line
MH  - Cell Line, Tumor
MH  - Cell Movement
MH  - Cloning, Molecular
MH  - DNA, Complementary/metabolism
MH  - Epitopes
MH  - Gene Library
MH  - Glycine/chemistry
MH  - Human
MH  - Leucine/chemistry
MH  - Membrane Glycoproteins/*metabolism
MH  - Metalloendopeptidases/*metabolism
MH  - Peptides/chemistry
MH  - Protein Binding
MH  - Proteoglycans/*metabolism
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Tetradecanoylphorbol Acetate
MH  - Tissue Inhibitor-of Metalloproteinase-2/metabolism
MH  - Tissue-Inhibitor of Metalloproteinase-1/metabolism
MH  - Transfection
MH  - Wound Healing
EDAT- 2003/08/09 05:00
MHDA- 2003/12/04 05:00
PHST- 2003/Aug/06 [aheadofprint]
AID - 10.1074/jbc.M306736200 [doi]
AID - M306736200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 Oct 17;278(42):40764-70.

PMID- 12902511
OWN - NLM
STAT- completed
DA  - 20030806
DCOM- 20031031
IS  - 0022-1767
VI  - 171
IP  - 4
DP  - 2003 Aug 15
TI  - Plasminogen activator inhibitor-1 supports IL-8-mediated neutrophil
      transendothelial migration by inhibition of the constitutive shedding of
      endothelial IL-8/heparan sulfate/syndecan-1 complexes.
PG  - 2057-65
AB  - The endothelium is the primary barrier to leukocyte recruitment at sites
      of inflammation. Neutrophil recruitment is directed by transendothelial
      gradients of IL-8 that, in vivo, are bound to the endothelial cell
      surface. We have investigated the identity and function of the binding
      site(s) in an in vitro model of neutrophil transendothelial migration. In
      endothelial culture supernatants, IL-8 was detected in a trimolecular
      complex with heparan sulfate and syndecan-1. Constitutive shedding of IL-8
      in this form was increased in the presence of a neutralizing Ab to
      plasminogen activator inhibitor-1 (PAI-1), indicating a role for
      endothelial plasminogen activator in the shedding of IL-8. Increased
      shedding of IL-8/heparan sulfate/syndecan-1 complexes was accompanied by
      inhibition of neutrophil transendothelial migration, and aprotinin, a
      potent plasmin inhibitor, reversed this inhibition. Platelets, added as an
      exogenous source of PAI-1, had no effect on shedding of the complexes or
      neutrophil migration. Our results indicate that IL-8 is immobilized on the
      endothelial cell surface through binding to syndecan-1 ectodomains, and
      that plasmin, generated by endothelial plasminogen activator, induces the
      shedding of this form of IL-8. PAI-1 appears to stabilize the
      chemoattractant form of IL-8 at the cell surface and may represent a
      therapeutic target for novel anti-inflammatory strategies.
AD  - School of Pharmacy and Biomedical Sciences, University of Portsmouth,
      Portsmouth, Hampshire, United Kingdom.
FAU - Marshall, Lindsay J
AU  - Marshall LJ
FAU - Ramdin, Lara S P
AU  - Ramdin LS
FAU - Brooks, Teresa
AU  - Brooks T
FAU - DPhil, Peter Charlton
AU  - DPhil PC
FAU - Shute, Janis K
AU  - Shute JK
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Immunol
JID - 2985117R
RN  - 0 (Antibodies, Monoclonal)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Interleukin-8)
RN  - 0 (Macromolecular Systems)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Plasminogen Activator Inhibitor 1)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (syndecan)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 3.4.21.7 (Plasmin)
SB  - AIM
SB  - IM
MH  - Antibodies, Monoclonal/pharmacology
MH  - Blood Platelets/physiology
MH  - Cell Line
MH  - Cell Migration Inhibition
MH  - Cell-Free System/chemistry
MH  - Chemotaxis, Leukocyte/*immunology
MH  - Coculture
MH  - Endothelium, Vascular/cytology/immunology/*metabolism
MH  - Heparan Sulfate Proteoglycan/analysis/metabolism
MH  - Heparitin Sulfate/*antagonists & inhibitors/metabolism
MH  - Human
MH  - Interleukin-8/*antagonists & inhibitors/metabolism/*physiology
MH  - Macromolecular Systems
MH  - Membrane Glycoproteins/*antagonists & inhibitors/metabolism
MH  - Neutrophils/*cytology/immunology/metabolism
MH  - Plasmin/physiology
MH  - Plasminogen Activator Inhibitor 1/immunology/*physiology
MH  - Proteoglycans/*antagonists & inhibitors/metabolism
MH  - Recombinant Proteins/pharmacology
MH  - Solubility
MH  - Support, Non-U.S. Gov't
EDAT- 2003/08/07 05:00
MHDA- 2003/11/01 05:00
PST - ppublish
SO  - J Immunol 2003 Aug 15;171(4):2057-65.

PMID- 12901703
OWN - NLM
STAT- completed
DA  - 20030806
DCOM- 20030822
LR  - 20031114
IS  - 0022-3069
VI  - 62
IP  - 7
DP  - 2003 Jul
TI  - Heparan sulfate proteoglycans modulate monocyte migration across cerebral
      endothelium.
PG  - 780-90
AB  - Heparan sulfate proteoglycans (HSPGs) are known to participate in a wide
      range of biological events, including cellular trafficking. In this study
      we report that in situ cerebral blood vessels highly express HSPGs. Of the
      syndecan family, syndecan-2 is highly expressed on virtually all brain
      vessels and syndecan-1 and -3 are only present on larger blood vessels.
      These endothelial HSPGs have a functional role in monocyte diapedesis
      across brain endothelium, as assessed in our in vitro adhesion and
      migration assays. Our data indicate that heparin prevents monocyte
      adhesion to brain endothelium by interacting solely with the monocyte.
      Transendothelial migration of monocytes can be prevented by preincubation
      of brain endothelium with heparin by enzymatic removal of heparan sulphate
      side chains or by inhibition of cellular sulfation. Blocking of
      G-protein-dependent signaling in the monocytes prevented monocyte adhesion
      and migration to similar extent, suggesting that G-dependent signaling may
      be involved in HSPG-mediated monocyte adhesion and transendothelial
      migration. Our data demonstrate that brain endothelial HSPGs have a
      modulatory role in the transendothelial migration of monocytes in a direct
      and indirect fashion and may therefore contribute to the formation of
      neuroinflammatory lesions.
AD  - Department of Molecular Cell Biology , Vrije Universiteit Medical Center,
      Amsterdam, The Netherlands.
FAU - Floris, Sarah
AU  - Floris S
FAU - van den Born, Jacob
AU  - van den Born J
FAU - van der Pol, Susanne M A
AU  - van der Pol SM
FAU - Dijkstra, Christine D
AU  - Dijkstra CD
FAU - De Vries, Helga E
AU  - De Vries HE
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Neuropathol Exp Neurol
JID - 2985192R
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Sulfates)
RN  - 149769-25-5 (fibroglycan)
RN  - 9005-49-6 (Heparin)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
SB  - IM
MH  - Animals
MH  - Cell Adhesion/drug effects/physiology
MH  - Cerebral Cortex/blood supply/*metabolism/physiopathology
MH  - Chemotaxis, Leukocyte/drug effects/*physiology
MH  - Disease Models, Animal
MH  - Encephalitis/drug therapy/*metabolism/physiopathology
MH  - Encephalomyelitis, Experimental Autoimmune
MH  - Endothelium, Vascular/drug effects/*metabolism
MH  - Extracellular Matrix/drug effects/metabolism
MH  - GTP-Binding Proteins/antagonists & inhibitors/metabolism
MH  - Heparan Sulfate Proteoglycan/*metabolism
MH  - Heparin/pharmacology
MH  - Male
MH  - Membrane Glycoproteins/*metabolism
MH  - Monocytes/drug effects/*metabolism
MH  - Protein Structure, Secondary/drug effects/physiology
MH  - Proteoglycans/*metabolism
MH  - Rats
MH  - Rats, Inbred Lew
MH  - Rats, Wistar
MH  - Signal Transduction/drug effects/physiology
MH  - Sulfates/antagonists & inhibitors
MH  - Support, Non-U.S. Gov't
EDAT- 2003/08/07 05:00
MHDA- 2003/08/23 05:00
PST - ppublish
SO  - J Neuropathol Exp Neurol 2003 Jul;62(7):780-90.

PMID- 12883204
OWN - NLM
STAT- completed
DA  - 20030728
DCOM- 20030904
LR  - 20031114
IS  - 0041-1337
VI  - 76
IP  - 2
DP  - 2003 Jul 27
TI  - Increased levels of syndecan-1 in serum during acute graft-versus-host
      disease.
PG  - 423-6
AB  - Acute graft-versus-host disease (GVHD) may affect several organs.
      Syndecan-1 is a heparan sulfate proteoglycan that can be shed from the
      surface of most epithelial cells (skin, liver, and gut among others),
      which are target organs for GVHD. Syndecan-1 was measured in serum samples
      from 60 patients after allogeneic stem-cell transplantation and was
      related to the degree of GVHD. Syndecan-1 levels increased in patients who
      developed acute GVHD but not in patients without GVHD. The difference
      between groups was significant 3 to 10 weeks after transplantation. The
      peak level of syndecan-1 in serum correlated with the degree of acute GVHD
      (r=0.46, P<0.001). Combined, the peak levels of syndecan-1 and soluble
      interleukin-2 receptor detected patients with acute GVHD (sensitivity 82%,
      specificity 89%). This study shows that syndecan-1 levels are increased
      during acute GVHD. Syndecan-1 may be a marker for acute GVHD, especially
      if combined with determination of soluble interleukin-2 receptor.
AD  - Division of Pathology, Department of Laboratory Medicine, Karolinska
      Institute, Huddinge University Hospital, Stockholm, Sweden.
      carina.seidel@labmed.ki.se.
FAU - Seidel, Carina
AU  - Seidel C
FAU - Ringden, Olle
AU  - Ringden O
FAU - Remberger, Mats
AU  - Remberger M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Transplantation
JID - 0132144
RN  - 0 (Biological Markers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Acute Disease
MH  - Adolescent
MH  - Adult
MH  - Biological Markers
MH  - Child
MH  - Child, Preschool
MH  - Epithelial Cells/metabolism
MH  - Female
MH  - Graft vs Host Disease/*blood/*diagnosis
MH  - Human
MH  - Leukemia, Lymphocytic, Acute/blood/therapy
MH  - Leukemia, Myelocytic, Acute/blood/therapy
MH  - Leukemia, Myeloid, Chronic/blood/therapy
MH  - Male
MH  - Membrane Glycoproteins/*blood
MH  - Middle Aged
MH  - Proteoglycans/*blood
MH  - Sensitivity and Specificity
MH  - *Stem Cell Transplantation
MH  - Support, Non-U.S. Gov't
EDAT- 2003/07/29 05:00
MHDA- 2003/09/05 05:00
AID - 10.1097/01.TP.0000074316.76104.A5 [doi]
PST - ppublish
SO  - Transplantation 2003 Jul 27;76(2):423-6.

PMID- 12881311
OWN - NLM
STAT- completed
DA  - 20031118
DCOM- 20040114
IS  - 0006-4971
VI  - 102
IP  - 12
DP  - 2003 Dec 1
TI  - Complexity within the plasma cell compartment of mice deficient in both E-
      and P-selectin: implications for plasma cell differentiation.
PG  - 4076-83
AB  - Antibody-secreting plasma cells represent the critical end-stage effector
      cells of the humoral immune response. Here, we show that several distinct
      plasma cell subsets are concurrently present in the lymph nodes, spleen,
      and bone marrow of mice deficient in both E- and P-selectin. One of these
      subsets was a B220-negative immunoglobulin g (IgG) plasma cell population
      expressing low to negative surface levels of syndecan-1. Examination of
      the chemotactic responsiveness of IgG plasma cell subsets revealed that
      migration toward stromal cell-derived factor 1/CXC ligand 12
      (SDF-1/CXCL12) was primarily limited to the B220-lo subset regardless of
      tissue source. Although B220-negative plasma cells did not migrate
      efficiently in response to CXCL12 or to other chemokines for which
      receptor mRNA was expressed, these cells expressed substantial surface CXC
      chemokine receptor-4 (CXCR4), and CXCL12 stimulation rapidly induced
      extracellular signal regulated kinase 1 (ERK1)/ERK2 phosphorylation,
      demonstrating that CXCR4 retained signaling capacity. Therefore,
      B220-negative plasma cells exhibit a selective uncoupling of chemokine
      receptor expression and signaling from migration. Taken together, our
      findings document the presence of significant heterogeneity within the
      plasma cell compartment, which suggests a complex step-wise scheme of
      plasma cell differentiation in which the degree of differentiation and
      tissue location can influence the chemotactic responsiveness of IgG plasma
      cells.
AD  - Department of Microbiology-Immunology, Northwestern Medical School, 303 E
      Chicago Ave, Chicago, IL 60611, USA.
FAU - Underhill, Gregory H
AU  - Underhill GH
FAU - Kolli, K Pallav
AU  - Kolli KP
FAU - Kansas, Geoffrey S
AU  - Kansas GS
LA  - eng
GR  - HL58710/HL/NHLBI
PT  - Journal Article
DEP - 20030724
PL  - United States
TA  - Blood
JID - 7603509
RN  - 0 (Antigens, CD45)
RN  - 0 (Chemokines, CXC)
RN  - 0 (E-Selectin)
RN  - 0 (P-Selectin)
RN  - 0 (stromal cell-derived factor-1alpha)
SB  - AIM
SB  - IM
MH  - Animals
MH  - Antigens, CD45/analysis
MH  - Bone Marrow Cells
MH  - Cell Differentiation/*physiology
MH  - Chemokines, CXC/physiology
MH  - Chemotaxis
MH  - E-Selectin/*genetics
MH  - Lymph Nodes/cytology
MH  - Mice
MH  - Mice, Knockout
MH  - P-Selectin/*genetics
MH  - Plasma Cells/*cytology
MH  - Spleen/cytology
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tissue Distribution
EDAT- 2003/07/26 05:00
MHDA- 2004/01/15 05:00
PHST- 2003/Jul/24 [aheadofprint]
AID - 10.1182/blood-2003-03-0947 [doi]
AID - 2003-03-0947 [pii]
PST - ppublish
SO  - Blood 2003 Dec 1;102(12):4076-83.

PMID- 12879463
OWN - NLM
STAT- completed
DA  - 20030724
DCOM- 20030814
LR  - 20031114
IS  - 0008-543X
VI  - 98
IP  - 3
DP  - 2003 Aug 1
TI  - High syndecan-1 expression in breast carcinoma is related to an aggressive
      phenotype and to poorer prognosis.
PG  - 474-83
AB  - BACKGROUND: Syndecan-1 is a transmembrane heparan sulphate proteoglycan
      that is involved in cell-cell adhesion, organization of cell-matrix
      adhesion, and regulation of growth factor signaling. METHODS: Specimens
      from 254 consecutive breast carcinoma (BC) cases (110 N0, 144 N1/2) with
      long-term follow-up (median, 95 months) were immunostained for syndecan-1,
      estrogen receptor (ER), progesterone receptor (PgR), and p53; in 154
      cases, c-erbB-2 status was known. Syndecan-1 mRNA and protein expression
      also were evaluated in 20 breast tissue samples (10 normal and tumor
      pairs). RESULTS: Syndecan-1 was expressed at high levels in 106 (42%) BCs;
      syndecan-1 up-regulation was confirmed by reverse transcriptase-polymerase
      chain reaction (RT-PCR) studies. High syndecan-1 expression was associated
      with high histologic grade, large tumor size, high mitotic count, c-erbB-2
      overexpression, and ER and PgR negative status. At univariate survival
      analysis syndecan overexpression was related to poor prognosis (P < 0.01
      for both overall survival (OS) and disease-free survival). Bivariate
      survival analysis showed an additive adverse effect for syndecan-1 and
      c-erbB-2 overexpression. At multivariate analysis, syndecan-1
      overexpression was independently associated with poor OS (hazard ratio
      [HR], 1.71; 95% confidence interval [CI], 1.08-2.69). High syndecan-1
      expression also was of independent prognostic value for OS in the group of
      102 ER-negative patients (HR, 2.42; 95% CI, 1.21-4.82). Stratifying
      patients on the basis of the type of adjuvant therapy given, high
      syndecan-1 expression was associated with a higher risk of death only in
      patients treated with the cyclophosphamide-methotrexate-fluorouracil
      regimen (HR, 1.9; P = 0.09); at multivariate analysis for OS, this
      association proved to be of independent statistical significance (P =
      0.03; HR, 2.15). CONCLUSIONS: Syndecan-1 is expressed at high levels in a
      significant percentage of breast carcinomas and is related to an
      aggressive phenotype and poor clinical behavior.
CI  - Copyright 2003 American Cancer Society.DOI 10.1002/cncr.11515
AD  - Department of Pathology, Santa Chiara Hospital, Trento, Italy.
FAU - Barbareschi, Mattia
AU  - Barbareschi M
FAU - Maisonneuve, Patrick
AU  - Maisonneuve P
FAU - Aldovini, Daniela
AU  - Aldovini D
FAU - Cangi, Maria Giulia
AU  - Cangi MG
FAU - Pecciarini, Lorenza
AU  - Pecciarini L
FAU - Angelo Mauri, Francesco
AU  - Angelo Mauri F
FAU - Veronese, Silvio
AU  - Veronese S
FAU - Caffo, Orazio
AU  - Caffo O
FAU - Lucenti, Antonio
AU  - Lucenti A
FAU - Palma, Paolo Dalla
AU  - Palma PD
FAU - Galligioni, Enzo
AU  - Galligioni E
FAU - Doglioni, Claudio
AU  - Doglioni C
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cancer
JID - 0374236
RN  - 0 (Antineoplastic Agents)
RN  - 0 (DNA Primers)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA, Neoplasm)
RN  - 0 (Receptors, Estrogen)
RN  - 0 (Receptors, Progesterone)
RN  - 0 (syndecan)
RN  - EC 2.7.1.112 (Receptor, erbB-2)
SB  - AIM
SB  - IM
MH  - Adenocarcinoma/*metabolism/pathology/therapy
MH  - Antineoplastic Agents/therapeutic use
MH  - Breast Neoplasms/*metabolism/pathology/therapy
MH  - Chemotherapy, Adjuvant
MH  - DNA Primers/chemistry
MH  - Female
MH  - Follow-Up Studies
MH  - Human
MH  - Immunoenzyme Techniques
MH  - Lymphatic Metastasis
MH  - Membrane Glycoproteins/genetics/*metabolism
MH  - Middle Aged
MH  - Prognosis
MH  - Proteoglycans/genetics/*metabolism
MH  - RNA, Messenger/genetics/metabolism
MH  - RNA, Neoplasm/metabolism
MH  - Receptor, erbB-2/genetics/metabolism
MH  - Receptors, Estrogen/genetics/metabolism
MH  - Receptors, Progesterone/genetics/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Stromal Cells/pathology
MH  - Support, Non-U.S. Gov't
MH  - Survival Rate
EDAT- 2003/07/25 05:00
MHDA- 2003/08/15 05:00
AID - 10.1002/cncr.11515 [doi]
PST - ppublish
SO  - Cancer 2003 Aug 1;98(3):474-83.

PMID- 12877731
OWN - NLM
STAT- in-process
DA  - 20030724
IS  - 0309-0167
VI  - 43
IP  - 2
DP  - 2003 Aug
TI  - Syndecan-1 expression in thyroid carcinoma: stromal expression followed by
      epithelial expression is significantly correlated with dedifferentiation.
PG  - 157-64
AB  - AIM: To investigate the expression of syndecan-1 in thyroid neoplasia.
      Syndecan-1 is a proteoglycan regulating cell adhesion. Previous studies
      have demonstrated that decreased expression of syndecan-1 is linked to
      malignant progression. METHODS AND RESULTS: Syndecan-1 expression in
      thyroid neoplasia was studied immunohistochemically. Syndecan-1 was
      expressed in stromal cells as well as neoplastic epithelial cells. Stromal
      syndecan-1 expression was observed more frequently in papillary carcinomas
      larger than 10 mm in size than in microcarcinomas and in widely invasive
      than in minimally invasive follicular carcinomas. Furthermore, poorly
      differentiated carcinomas showed this phenomenon more than
      well-differentiated carcinomas, but the expression in undifferentiated
      carcinomas was similar to that of poorly differentiated carcinomas.
      Epithelial syndecan-1 expression was more frequently observed in
      anaplastic (undifferentiated) carcinomas than in papillary and follicular
      carcinomas. No significant difference in epithelial expression was found
      between well and poorly differentiated carcinomas, but undifferentiated
      carcinomas expressed epithelial syndecan-1 more frequently than did poorly
      differentiated carcinomas. CONCLUSIONS: These results are in contrast to
      those previously reported for carcinomas at other sites. It is suggested
      that the role of syndecan-1 in thyroid carcinomas might be unique. Stromal
      syndecan-1 expression followed by its epithelial expression is
      significantly related to progression, including dedifferentiation of
      thyroid carcinoma.
AD  - Kuma Hospital, Kobe, Japan. ito01@kuma-h.or.jp
FAU - Ito, Y
AU  - Ito Y
FAU - Yoshida, H
AU  - Yoshida H
FAU - Nakano, K
AU  - Nakano K
FAU - Takamura, Y
AU  - Takamura Y
FAU - Miya, A
AU  - Miya A
FAU - Kobayashi, K
AU  - Kobayashi K
FAU - Yokozawa, T
AU  - Yokozawa T
FAU - Matsuzuka, F
AU  - Matsuzuka F
FAU - Matsuura, N
AU  - Matsuura N
FAU - Kuma, K
AU  - Kuma K
FAU - Miyauchi, A
AU  - Miyauchi A
LA  - eng
PT  - Journal Article
PL  - England
TA  - Histopathology
JID - 7704136
SB  - IM
EDAT- 2003/07/25 05:00
MHDA- 2003/07/25 05:00
AID - 1656 [pii]
PST - ppublish
SO  - Histopathology 2003 Aug;43(2):157-64.

PMID- 12871780
OWN - NLM
STAT- completed
DA  - 20030721
DCOM- 20031208
IS  - 0169-5002
VI  - 41
IP  - 2
DP  - 2003 Aug
TI  - Pretreatment serum syndecan-1 levels and outcome in small cell lung cancer
      patients treated with platinum-based chemotherapy.
PG  - 171-7
AB  - Syndecan-1 is a multifunctional transmembrane heparan sulphate
      proteoglycan (HSPG) that is present on a variety of cell types. The
      extracellular syndecan domains can be shed from the cell surface in a
      highly regulated process called ectodomain shedding. We studied the
      influence of soluble syndecan-1 on outcome in 88 small cell lung cancer
      (SCLC) patients treated within the context of two randomised clinical
      trials with platinum-based therapy. Serum syndecan-1 concentrations were
      determined using enzyme-linked immunosorbent assay (ELISA) from sera taken
      prior to initiation of chemotherapy. Patients with the serum syndecan-1
      level within the highest tertile (>212 microg/l) had only 38% 1-year and
      3% 2-year survival, whereas 58% of those with a lower serum level survived
      for 1 year and 25% for 2 years following the diagnosis (P=0.0034). A high
      serum syndecan-1 level (>212 microg/l) was associated with a high
      pretreatment lactate dehydrogenase (LDH) level (P=0.0024) and a poor
      Karnofsky's performance status (P=0.021), but not with the clinical stage
      or the presence of distant metastases at diagnosis. A high serum
      syndecan-1 level had independent influence on survival also in a
      multivariate analysis (the relative risk, RR, 1.68; 95% CI, 1.02-2.77;
      P=0.044) together with the clinical stage (RR, 1.72; 95% CI, 1.05-2.82;
      P=0.032). We conclude that high pretreatment serum syndecan-1 level is
      associated with poor prognosis in SCLC treated with platinum-based
      chemotherapy.
AD  - Department of Oncology, Helsinki University Central Hospital, P.O. Box
      180, FIN-00029, Helsinki, Finland. anu.anttonen@hus.fi
FAU - Anttonen, Anu
AU  - Anttonen A
FAU - Leppa, Sirpa
AU  - Leppa S
FAU - Ruotsalainen, Tarja
AU  - Ruotsalainen T
FAU - Alfthan, Henrik
AU  - Alfthan H
FAU - Mattson, Karin
AU  - Mattson K
FAU - Joensuu, Heikki
AU  - Joensuu H
LA  - eng
PT  - Journal Article
PL  - Ireland
TA  - Lung Cancer
JID - 8800805
RN  - 0 (Antineoplastic Combined Chemotherapy Protocols)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
SB  - IM
MH  - Adult
MH  - Aged
MH  - Antineoplastic Combined Chemotherapy Protocols/*therapeutic use
MH  - Carcinoma, Non-Small-Cell Lung/*blood/drug therapy/mortality
MH  - Female
MH  - Human
MH  - Lung Neoplasms/*blood/*drug therapy/mortality
MH  - Male
MH  - Membrane Glycoproteins/*blood
MH  - Middle Aged
MH  - Prognosis
MH  - Proteoglycans/*blood
MH  - Randomized Controlled Trials
MH  - Survival Analysis
MH  - Treatment Outcome
EDAT- 2003/07/23 05:00
MHDA- 2003/12/10 05:00
AID - S016950020300196X [pii]
PST - ppublish
SO  - Lung Cancer 2003 Aug;41(2):171-7.

PMID- 12859973
OWN - NLM
STAT- completed
DA  - 20030715
DCOM- 20030916
LR  - 20031114
IS  - 0006-291X
VI  - 307
IP  - 2
DP  - 2003 Jul 25
TI  - Changes in gene expression induced by H(2)O(2) in cardiac myocytes.
PG  - 416-21
AB  - Oxidative stress induces cardiac myocyte apoptosis. At least some effects
      are probably mediated through changes in gene expression. Using Affymetrix
      arrays, we examined the changes in gene expression induced by H(2)O(2)
      (0.04, 0.1, and 0.2mM; 2 and 4h) in rat neonatal ventricular myocytes.
      Changes in selected upregulated genes were confirmed by ratiometric
      RT-PCR. p21(Cip1/Waf1) was one of the only two genes upregulated in all
      conditions studied. Of the heat shock proteins, only Hsp70/70.1 was
      induced by H(2)O(2) with no change in the expression of Hsp25, Hsp60 or
      Hsp90. Heme oxygenase 1 was also potently upregulated, but not heme
      oxygenases 2 or 3. Of the intercellular adhesion proteins, syndecan-1 was
      significantly upregulated in response to H(2)O(2), with little change in
      the expression of other syndecans and no change in expression of any of
      the integrins studied. Thus, oxidative stress, exemplified by H(2)O(2),
      selectively promotes the expression of specific gene family members.
AD  - NHLI Division (Cardiac Medicine), Faculty of Medicine, Imperial College
      London, London, UK.
FAU - Kemp, Timothy J
AU  - Kemp TJ
FAU - Causton, Helen C
AU  - Causton HC
FAU - Clerk, Angela
AU  - Clerk A
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Biochem Biophys Res Commun
JID - 0372516
RN  - 0 (Cip1 protein)
RN  - 0 (Cyclins)
RN  - 0 (Heat-Shock Proteins 70)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Oxidants)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 7722-84-1 (Hydrogen Peroxide)
RN  - EC 1.14.99.- (heme oxygenase-1)
RN  - EC 1.14.99.3 (Heme Oxygenase (Decyclizing))
SB  - IM
MH  - Animals
MH  - Animals, Newborn
MH  - Cyclins/genetics/metabolism
MH  - *Gene Expression Profiling
MH  - Gene Expression Regulation/*drug effects
MH  - Heat-Shock Proteins 70/genetics/metabolism
MH  - Heme Oxygenase (Decyclizing)/genetics/metabolism
MH  - Hydrogen Peroxide/*pharmacology
MH  - Membrane Glycoproteins/genetics/metabolism
MH  - Molecular Sequence Data
MH  - Myocytes, Cardiac/*drug effects/physiology
MH  - Oligonucleotide Array Sequence Analysis
MH  - Oxidants/*pharmacology
MH  - Oxidative Stress
MH  - Proteoglycans/genetics/metabolism
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Support, Non-U.S. Gov't
EDAT- 2003/07/16 05:00
MHDA- 2003/09/17 05:00
AID - S0006291X03012154 [pii]
PST - ppublish
SO  - Biochem Biophys Res Commun 2003 Jul 25;307(2):416-21.

PMID- 12826666
OWN - NLM
STAT- completed
DA  - 20030901
DCOM- 20031007
LR  - 20031114
IS  - 0021-9258
VI  - 278
IP  - 36
DP  - 2003 Sep 5
TI  - Laminin alpha 3 LG4 module induces matrix metalloproteinase-1 through
      mitogen-activated protein kinase signaling.
PG  - 34483-90
AB  - The LG4 module of the laminin alpha 3 chain (alpha 3 LG4), a component of
      epithelial-specific laminin-5, has cell attachment activity and binds
      syndecan (Utani, A., Nomizu, M., Matsuura, H., Kato, K., Kobayashi, T.,
      Takeda, U., Aota, S., Nielsen, P. K., and Shinkai, H. (2001) J. Biol.
      Chem. 276, 28779-28788). Here, we show that recombinant alpha 3 LG4 and a
      19-mer synthetic peptide (A3G756) within alpha 3 LG4 active for syndecan
      binding increased the expression of matrix metalloproteinase-1 (MMP-1) in
      keratinocytes and fibroblasts. This induction was inhibited by heparin and
      required de novo synthesis of proteins. In keratinocytes, A3G756
      up-regulated interleukin (IL)-1 beta and MMP-1 expression and an IL-1
      receptor antagonist thoroughly inhibited A3G756-mediated induction of
      MMP-1. A3G756 also activated p38 mitogen-activated protein kinase (p38
      MAPK) and extracellular signal-related kinase (Erk). Studies with specific
      inhibitors of MAPKs showed that p38 MAPK activation was necessary for both
      IL-1 beta and MMP-1 induction, but Erk activation was required only for
      MMP-1 induction. In fibroblasts, IL-1 receptor antagonist did not block
      A3G756-mediated induction of MMP-1. These results indicated that induction
      of MMP-1 by alpha 3 LG4 is mediated through the IL-1 beta autocrine loop
      in keratinocytes but the mechanism of the induction in fibroblasts is
      different. Our study suggests that the laminin alpha 3 LG4 module may play
      an important role in tissue remodeling by inducing MMP-1 expression during
      wound healing.
AD  - Department of Dermatology, Graduate School of Medicine, Chiba University,
      Chiba 260-8670, Japan. utani@derma01.m.chiba-u.ac.jp
FAU - Utani, Atsushi
AU  - Utani A
FAU - Momota, Yutaka
AU  - Momota Y
FAU - Endo, Hideharu
AU  - Endo H
FAU - Kasuya, Yoshitoshi
AU  - Kasuya Y
FAU - Beck, Konrad
AU  - Beck K
FAU - Suzuki, Nobuharu
AU  - Suzuki N
FAU - Nomizu, Motoyoshi
AU  - Nomizu M
FAU - Shinkai, Hiroshi
AU  - Shinkai H
LA  - eng
PT  - Journal Article
DEP - 20030624
PL  - United States
TA  - J Biol Chem
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Interleukin-1)
RN  - 0 (Laminin)
RN  - 0 (MAP Kinase Signaling System)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptides)
RN  - 0 (Proteoglycans)
RN  - 0 (Recombinant Proteins)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 149769-25-5 (fibroglycan)
RN  - 170834-93-2 (laminin alpha 3)
RN  - 9007-34-5 (Collagen)
RN  - EC 2.7.1.37 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.10.- (mitogen-activated protein kinase p38)
RN  - EC 3.4.24.7 (Interstitial Collagenase)
SB  - IM
MH  - Animals
MH  - Blotting, Western
MH  - Cell Adhesion
MH  - Cell Line
MH  - Cells, Cultured
MH  - Collagen/metabolism
MH  - DNA, Complementary/metabolism
MH  - Dose-Response Relationship, Drug
MH  - Enzyme Activation
MH  - Enzyme-Linked Immunosorbent Assay
MH  - Fibroblasts/metabolism
MH  - Human
MH  - Immunohistochemistry
MH  - Interleukin-1/metabolism
MH  - Interstitial Collagenase/*chemistry/*metabolism
MH  - Keratinocytes/metabolism
MH  - Laminin/*chemistry
MH  - *MAP Kinase Signaling System
MH  - Membrane Glycoproteins/chemistry/metabolism
MH  - Microscopy, Fluorescence
MH  - Mitogen-Activated Protein Kinases/metabolism
MH  - Models, Molecular
MH  - Peptides/chemistry
MH  - Proteoglycans/chemistry/metabolism
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Signal Transduction
MH  - Support, Non-U.S. Gov't
MH  - Time Factors
MH  - Up-Regulation
MH  - Wound Healing
EDAT- 2003/06/27 05:00
MHDA- 2003/10/08 05:00
PHST- 2003/Jun/24 [aheadofprint]
AID - 10.1074/jbc.M304827200 [doi]
AID - M304827200 [pii]
PST - ppublish
SO  - J Biol Chem 2003 Sep 5;278(36):34483-90.

PMID- 12823344
OWN - NLM
STAT- completed
DA  - 20030625
DCOM- 20030916
LR  - 20031114
IS  - 0007-1048
VI  - 122
IP  - 1
DP  - 2003 Jul
TI  - Upregulation of osteoblast apoptosis by malignant plasma cells: a role in
      myeloma bone disease.
PG  - 39-52
AB  - Typical features of multiple myeloma (MM) are osteolytic lesions and
      severely affected bone regeneration. This study of 53 MM patients
      demonstrates an enhancement of osteoblast cytotoxicity by malignant
      myeloma cells via the upregulation of apoptogenic receptors, including Fas
      ligand (Fas-L) and tumour-necrosis-factor-related apoptosis inducing
      ligand (TRAIL). Both were significantly increased in the marrow myeloma
      cells of patients with extensive osteolytic lesions in a fashion similar
      to the highly malignant human myeloma cell line MCC-2. Osteoblasts from
      these subjects over-expressed Fas and death receptor (DR) 4/5 and
      underwent dramatic apoptosis when co-cultured with either MCC-2 or
      autologous myeloma cells. In osteoblast and myeloma cell co-cultures,
      monocyte chemoattractant protein 1 (MCP-1) mRNA was upregulated in
      osteoblasts from patients with severe bone disease in parallel with
      increased CC-chemokine receptor R2 (CCR2) expression, the ligand of MCP-1,
      in the myeloma cells. This chemokine was shown to activate malignant cell
      migration in vitro. An upregulation of ICAM-1 expression occurred in
      osteoblasts from patients with active skeleton disease. This upregulation
      appeared to be an effect of malignant plasma cell contact, as MCC-2
      co-culture greatly enhanced ICAM-1 production by resting osteoblasts from
      patients without skeleton involvement. Our results suggest that
      osteoblasts in active myeloma are functionally exhausted and promptly
      undergo apoptosis in the presence of myeloma cells from patients with
      severe bone disease. It is suggested that this cytotoxic effect plays a
      pivotal role in the pathogenesis of defective bone repair.
AD  - Department of Internal Medicine and Oncology (DIMO), University of Bari,
      Bari, Italy. f.silvestris@dio.uniba.it
FAU - Silvestris, Franco
AU  - Silvestris F
FAU - Cafforio, Paola
AU  - Cafforio P
FAU - Tucci, Marco
AU  - Tucci M
FAU - Grinello, Daniela
AU  - Grinello D
FAU - Dammacco, Franco
AU  - Dammacco F
LA  - eng
PT  - Journal Article
PL  - England
TA  - Br J Haematol
JID - 0372544
RN  - 0 (FasL protein)
RN  - 0 (Ligands)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Monocyte Chemoattractant Protein-1)
RN  - 0 (Proteoglycans)
RN  - 0 (TNF-related apoptosis-inducing ligand)
RN  - 0 (Tumor Necrosis Factor)
RN  - 0 (syndecan)
RN  - 126547-89-5 (Intercellular Adhesion Molecule-1)
SB  - IM
MH  - Aged
MH  - *Apoptosis
MH  - Coculture
MH  - Human
MH  - Intercellular Adhesion Molecule-1/metabolism
MH  - Ligands
MH  - Membrane Glycoproteins/metabolism
MH  - Middle Aged
MH  - Monocyte Chemoattractant Protein-1/metabolism
MH  - Multiple Myeloma/*pathology
MH  - Osteoblasts/metabolism/*pathology
MH  - Phenotype
MH  - Plasma Cells/*physiology
MH  - Proteoglycans/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Tumor Necrosis Factor/metabolism
MH  - Up-Regulation
EDAT- 2003/06/26 05:00
MHDA- 2003/09/17 05:00
AID - 4374 [pii]
PST - ppublish
SO  - Br J Haematol 2003 Jul;122(1):39-52.

PMID- 12811819
OWN - NLM
STAT- completed
DA  - 20030617
DCOM- 20030811
LR  - 20031114
IS  - 0021-9541
VI  - 196
IP  - 2
DP  - 2003 Aug
TI  - CTGF/Hcs24, hypertrophic chondrocyte-specific gene product, interacts with
      perlecan in regulating the proliferation and differentiation of
      chondrocytes.
PG  - 265-75
AB  - Connective tissue growth factor/hypertrophic chondrocyte-specific gene
      product 24 (CTGF/Hcs24) plays important roles in the control of the
      proliferation and differentiation of chondrocytes in vitro. To clarify the
      mechanisms of regulation by CTGF/Hcs24 with respect to cartilage
      metabolism, we investigated the interaction between CTGF/Hcs24 and heparan
      sulfate proteoglycan perlecan. An immunofluorescence study showed that
      CTGF/Hcs24 was colocalized with heparan sulfate and perlecan in human
      chondrosarcoma-derived chondrocytic cell line HCS-2/8 in vitro. Northern
      blot analysis showed that perlecan, syndecan-1, -2, and -4 transcripts
      were detected in HCS-2/8 cells. Particularly, expression of the perlecan
      gene increased markedly in HCS-2/8 cells by recombinant CTGF/Hcs24
      (rCTGF/Hcs24) treatment. We also found that CTGF/Hcs24 interacted with
      perlecan from HCS-2/8 cells in vitro. Furthermore, CTGF/Hcs24-stimulated
      gene expression of the aggrecan gene, as well as DNA/proteoglycan
      synthesis, was diminished when HCS-2/8 cells were pretreated with
      heparinase, indicating that the effects of CTGF/Hcs24 on chondrocytes
      occurred through the interaction between CTGF/Hcs24 and heparan sulfate on
      the cells. An in vivo study using mouse growth plate revealed that
      CTGF/Hcs24 produced by hypertrophic chondrocytes was localized from the
      proliferative to the hypertrophic zone, whereas perlecan was predominantly
      localized in the prehyphertrophic zone. Consistent with such findings in
      vivo, the binding of (125)I-rCTGF/Hcs24 to maturing chondrocytes was at
      higher levels than that to chondrocytes in hypertrophic stages. These
      findings suggest that CTGF/Hcs24 produced in the hypertrophic region may
      act on chondrocytes in the proliferative and maturative zone via some
      heparan sulfate proteoglycan, such as perlecan.
CI  - Copyright 2003 Wiley-Liss, Inc.
AD  - Department of Biochemistry and Molecular Dentistry, Okayama University
      Graduate School of Medicine and Dentistry, Okayama, Japan.
FAU - Nishida, Takashi
AU  - Nishida T
FAU - Kubota, Satoshi
AU  - Kubota S
FAU - Fukunaga, Tomohiro
AU  - Fukunaga T
FAU - Kondo, Seiji
AU  - Kondo S
FAU - Yosimichi, Gen
AU  - Yosimichi G
FAU - Nakanishi, Tohru
AU  - Nakanishi T
FAU - Takano-Yamamoto, Teruko
AU  - Takano-Yamamoto T
FAU - Takigawa, Masaharu
AU  - Takigawa M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Cell Physiol
JID - 0050222
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Immediate-Early Proteins)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 0 (Ligands)
RN  - 0 (Recombinant Proteins)
RN  - 139568-91-5 (connective tissue growth factor)
RN  - 143972-95-6 (perlecan)
RN  - EC 4.2.2.7 (Heparin Lyase)
SB  - IM
MH  - Aged
MH  - Animals
MH  - Blotting, Northern
MH  - Cell Differentiation/physiology
MH  - Cell Division/physiology
MH  - Chondrocytes/*cytology
MH  - Heparan Sulfate Proteoglycan/*physiology
MH  - Heparin Lyase/pharmacology
MH  - Human
MH  - Immediate-Early Proteins/*physiology
MH  - Immunologic Techniques
MH  - Intercellular Signaling Peptides and Proteins/*physiology
MH  - Ligands
MH  - Male
MH  - Mice
MH  - Mice, Inbred Strains
MH  - Recombinant Proteins/metabolism
MH  - Support, Non-U.S. Gov't
MH  - Tumor Cells, Cultured
EDAT- 2003/06/18 05:00
MHDA- 2003/08/12 05:00
AID - 10.1002/jcp.10277 [doi]
PST - ppublish
SO  - J Cell Physiol 2003 Aug;196(2):265-75.

PMID- 12782806
OWN - NLM
STAT- completed
DA  - 20030603
DCOM- 20030723
LR  - 20031114
IS  - 0023-852X
VI  - 113
IP  - 6
DP  - 2003 Jun
TI  - Fibronectin and adhesion molecules on canine scarred vocal folds.
PG  - 966-72
AB  - OBJECTIVE: To examine the expressions of fibronectin and other adhesion
      molecules on the scarred vocal folds in a short- and long-term animal
      model. STUDY DESIGN: Animal model. METHODS: Six beagles' vocal folds were
      stripped unilaterally and left untreated. After wounding the vocal folds
      were harvested from three dogs at 2 months and three dogs at 6 months. The
      untouched vocal fold was used as a control, and the stripped vocal fold as
      scarred. Subsequently, the expressions of fibronectin, cadherin,
      syndecan-1 and syndecan-4 on both vocal folds were examined by
      immunohistochemical and image analysis. RESULTS: Compared with the control
      vocal folds, fibronectin significantly increased in the superficial layer
      of the lamina propria on the scarred vocal folds at both 2 and 6 months.
      Co-deposition of collagen was observed only at 6 months. Syndecan-4 was
      significantly overexpressed at the basal layer cells of the epithelium at
      both 2 and 6 months. No significant expression of either cadherin or
      syndecan-1 was detected. CONCLUSIONS: Scar characteristics at 2 and 6
      months are not identical, suggesting that a 2-month period may not be a
      sufficient to study vocal fold scarring. Adhesion molecules are important
      in reorganization of extracellular matrix during wound healing because of
      their binding and adhesion characteristics. The results indicate that
      fibronectin might be important in providing a scaffold for the deposition
      of other proteins such as collagen, and the binding characteristics might
      affect the stiffness of the scarred vocal fold. Prolonged expression of
      syndecan-4 may reflect the role of focal adhesion during the assembly of
      scar structure. Ultimately, better understanding of the histological
      features of the scarred vocal fold might lead to new approaches to
      treatment.
AD  - Department of Surgery, University of Wisconsin-Madison, 53792, USA.
      hirano@surgery.wisc.edu
FAU - Hirano, Shigeru
AU  - Hirano S
FAU - Bless, Diane M
AU  - Bless DM
FAU - Rousseau, Bernard
AU  - Rousseau B
FAU - Welham, Nathan
AU  - Welham N
FAU - Scheidt, Troy
AU  - Scheidt T
FAU - Ford, Charles N
AU  - Ford CN
LA  - eng
GR  - R01DC4428/DC/NIDCD
PT  - Journal Article
PL  - United States
TA  - Laryngoscope
JID - 8607378
RN  - 0 (Cadherins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Fibronectins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 9007-34-5 (Collagen)
SB  - IM
MH  - Animals
MH  - Cadherins/analysis
MH  - Cell Adhesion Molecules/*analysis
MH  - Cicatrix/*pathology
MH  - Collagen/analysis
MH  - Disease Models, Animal
MH  - Dogs
MH  - Fibronectins/*analysis
MH  - Immunoenzyme Techniques
MH  - Membrane Glycoproteins/analysis
MH  - Proteoglycans/analysis
MH  - Respiratory Mucosa/pathology
MH  - Support, U.S. Gov't, P.H.S.
MH  - Vocal Cords/*pathology
MH  - Wound Healing/physiology
EDAT- 2003/06/05 05:00
MHDA- 2003/07/24 05:00
PST - ppublish
SO  - Laryngoscope 2003 Jun;113(6):966-72.

PMID- 12773479
OWN - NLM
STAT- in-process
DA  - 20030822
IS  - 0959-6658
VI  - 13
IP  - 9
DP  - 2003 Sep
TI  - Binding of the CC-chemokine RANTES to syndecan-1 and syndecan-4 expressed
      on HeLa cells.
PG  - 623-34
AB  - It is believed that proteoglycans influence biological properties of
      chemokines. We show that the CC chemokine RANTES binds not only to
      high-affinity binding sites on CCR5-positive HeLa cells but also to
      low-affinity binding sites on HeLa cells expressing or lacking RANTES G
      protein-coupled receptors. Coimmunoprecipitation studies demonstrate that
      RANTES forms complexes with glycanated syndecan (SD)-1 and -4, in addition
      to CCR5 on the CCR5-positive HeLa cells. Moreover, confocal microscopy
      analysis shows the colocalization of RANTES with SD-1 and -4.
      Glycosaminoglycans removal from the cells by glycosaminidases treatment
      prevented RANTES binding to SD-1 and -4 and decreased RANTES binding to
      CCR5 on the CCR5-positive HeLa cells. Removal of glycosaminoglycans by
      glycosaminidases treatment of the complexes, RANTES/SD-1/SD-4/+/-CCR5,
      immobilized on beads, reversed SD-1 and -4 bindings. Therefore, RANTES
      bindings to SD-1 and -4 depend on glycosaminoglycans and facilitate RANTES
      interaction with CCR5. Extracting plasma membrane cholesterol abolished
      the coimmunoprecipitation of SD-1 with RANTES, suggesting that rafts are
      involved in RANTES association to SD-1. Confocal microscopy analysis as
      well as coimmunoprecipitation experiments show a RANTES-independent
      heteromeric complex on the CCR5-positive HeLa cells, SD-1, SD-4, and CCR5.
      This complex is likely a functional unit in which proteoglycans may
      modulate RANTES binding to CCR5.
AD  - Laboratoire de Biologie Cellulaire, Biotherapies Benefices et Risques,
      UPRES 3410, UFR-SMBH, Universite Paris XIII, 74, rue Marcel Cachin, 93017,
      Bobigny, France.
FAU - Slimani, Hocine
AU  - Slimani H
FAU - Charnaux, Nathalie
AU  - Charnaux N
FAU - Mbemba, Elisabeth
AU  - Mbemba E
FAU - Saffar, Line
AU  - Saffar L
FAU - Vassy, Roger
AU  - Vassy R
FAU - Vita, Claudio
AU  - Vita C
FAU - Gattegno, Liliane
AU  - Gattegno L
LA  - eng
PT  - Journal Article
DEP - 20030528
PL  - England
TA  - Glycobiology
JID - 9104124
SB  - IM
EDAT- 2003/05/30 05:00
MHDA- 2003/05/30 05:00
PHST- 2003/May/28 [aheadofprint]
AID - 10.1093/glycob/cwg083 [doi]
AID - cwg083 [pii]
PST - ppublish
SO  - Glycobiology 2003 Sep;13(9):623-34.

PMID- 12761845
OWN - NLM
STAT- completed
DA  - 20030522
DCOM- 20040122
IS  - 1058-8388
VI  - 227
IP  - 2
DP  - 2003 Jun
TI  - Localisation of specific heparan sulfate proteoglycans during the
      proliferative phase of brain development.
PG  - 170-84
AB  - Early brain development is characterised by the proliferation of neural
      precursor cells. Several families of signalling molecules such as the
      fibroblast growth factors (FGFs) and Wnts are known to play important
      roles in this early phase of brain development. Accumulating evidence
      demonstrates that signalling of these molecules requires the presence of
      heparan sulfate chains attached to a proteoglycan core protein (HSPG).
      However, the specific identity of the HSPG components in the developing
      brain is unknown. To determine which HSPGs might be involved at this early
      phase, we analysed the expression of the major cell surface HSPG families
      in the developing brain at a time of most active proliferation. Syndecan-1
      and glypican-4 were the most highly expressed in the developing brain
      during the time of peak proliferation and localise to ventricular regions
      of the brain, where the precursor cells are proliferating. Syndecan-4,
      although less abundant, also localises to cells in the ventricular zone.
      We have also examined HSPG involvement in brain development using cultures
      of embryonic neural precursor cells. We find that FGF2 stimulation of
      proliferation is inhibited in the presence of sodium chlorate, an
      inhibitor of heparan sulfate synthesis, and is rescued by addition of
      exogenous heparan sulfate. These data support a requirement for heparan
      sulfate in FGF signalling for proliferation of brain precursor cells. The
      expression of these specific HSPGs within the proliferative zone of the
      brain suggests that they may be involved in regulation of early brain
      development, such as FGF-stimulated proliferation.
CI  - Copyright 2003 Wiley-Liss, Inc.
AD  - Department of Anatomy and Cell Biology, University of Melbourne,
      Parkville, Victoria, Australia. mdfp@unimelb.edu.au
FAU - Ford-Perriss, Miriam
AU  - Ford-Perriss M
FAU - Turner, Kirsty
AU  - Turner K
FAU - Guimond, Scott
AU  - Guimond S
FAU - Apedaile, Anwyn
AU  - Apedaile A
FAU - Haubeck, Hans-Dieter
AU  - Haubeck HD
FAU - Turnbull, Jeremy
AU  - Turnbull J
FAU - Murphy, Mark
AU  - Murphy M
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Dev Dyn
JID - 9201927
RN  - 0 (Chlorates)
RN  - 0 (Heparan Sulfate Proteoglycan)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (glypican 4)
RN  - 0 (syndecan)
RN  - 0 (syndecan 3)
RN  - 0 (syndecan-4)
RN  - 143972-95-6 (perlecan)
RN  - 149769-25-5 (fibroglycan)
RN  - 62031-54-3 (Fibroblast Growth Factors)
SB  - IM
MH  - Animals
MH  - Antibody Specificity
MH  - Brain/*cytology/*embryology/metabolism
MH  - Cell Division/drug effects/physiology
MH  - Cells, Cultured
MH  - Chlorates/pharmacology
MH  - Fibroblast Growth Factors/pharmacology
MH  - Gene Expression Regulation, Developmental
MH  - Heparan Sulfate Proteoglycan/genetics/immunology/*metabolism/pharmacology
MH  - Membrane Glycoproteins/genetics/metabolism
MH  - Membrane Proteins/metabolism
MH  - Mice
MH  - Neurons/cytology/*metabolism
MH  - Proteoglycans/genetics/metabolism
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Stem Cells/cytology/*metabolism
MH  - Support, Non-U.S. Gov't
EDAT- 2003/05/23 05:00
MHDA- 2004/01/24 05:00
AID - 10.1002/dvdy.10298 [doi]
PST - ppublish
SO  - Dev Dyn 2003 Jun;227(2):170-84.

PMID- 12754183
OWN - NLM
STAT- completed
DA  - 20031010
DCOM- 20031121
IS  - 1040-0605
VI  - 285
IP  - 5
DP  - 2003 Nov
TI  - Lung endothelial heparan sulfates mediate cationic peptide-induced barrier
      dysfunction: a new role for the glycocalyx.
PG  - L986-95
AB  - The endothelial glycocalyx is believed to play a major role in
      microvascular permeability. We tested the hypothesis that specific
      components of the glycocalyx, via cytoskeletal-mediated signaling,
      actively participate in barrier regulation. With the use of polymers of
      arginine and lysine as a model of neutrophil-derived inflammatory cationic
      proteins, we determined size- and dose-dependent responses of cultured
      bovine lung microvascular endothelial cell permeability as assessed by
      transendothelial electrical resistance (TER). Polymers of arginine and
      lysine >11 kDa produced maximal barrier dysfunction as demonstrated by a
      70% decrease in TER. Monomers of l-arginine and l-lysine did not alter
      barrier function, suggesting a cross-linking requirement of cell surface
      "receptors". To test the hypothesis that glycosaminoglycans (GAGs) are
      candidate receptors for this response, we used highly selective enzymes to
      remove specific GAGs before polyarginine (PA) treatment and examined the
      effect on TER. Heparinase III attenuated PA-induced barrier dysfunction by
      50%, whereas heparinase I had no effect. To link changes in barrier
      function with structural alterations, we examined actin organization and
      syndecan localization after PA. PA induced actin stress fiber formation
      and clustering of syndecan-1 and syndecan-4, which were significantly
      attenuated by heparinase III. PA-induced cytoskeletal rearrangement and
      barrier function did not involve myosin light chain kinase (MLCK) or p38
      MAPK, as ML-7, a specific MLCK inhibitor, or SB-20358, a p38 MAPK
      inhibitor, did not alter PA-induced barrier dysfunction. In summary, lung
      endothelial cell heparan sulfate proteoglycans are key participants in
      inflammatory cationic peptide-induced signaling that links cytoskeletal
      reorganization with subsequent barrier dysfunction.
AD  - Anesthesiology and Critical Care Medicine, Department of Medicine, Johns
      Hopkins School of Medicine, Baltimore, Maryland 21287, USA.
      Randal.Dull@hsc.utah.edu
FAU - Dull, Randal O
AU  - Dull RO
FAU - Dinavahi, Ramani
AU  - Dinavahi R
FAU - Schwartz, Lawrence
AU  - Schwartz L
FAU - Humphries, Donald E
AU  - Humphries DE
FAU - Berry, David
AU  - Berry D
FAU - Sasisekharan, Ram
AU  - Sasisekharan R
FAU - Garcia, Joe G N
AU  - Garcia JG
LA  - eng
GR  - KO8 HL-68063/HL/NHLBI
PT  - Journal Article
DEP - 20030516
PL  - United States
TA  - Am J Physiol Lung Cell Mol Physiol
JID - 100901229
RN  - 0 (Cations)
RN  - 0 (Disaccharides)
RN  - 0 (Glycosaminoglycans)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Peptides)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan-4)
RN  - 25104-18-1 (Polylysine)
RN  - 25212-18-4 (polyarginine)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 4.2.2.- (Chondroitinases and Chondroitin Lyases)
RN  - EC 4.2.2.7 (Heparin Lyase)
SB  - IM
CIN - Am J Physiol Lung Cell Mol Physiol. 2003 Nov;285(5):L984-5. PMID: 14551039
MH  - Animals
MH  - Cations
MH  - Cattle
MH  - Cell Membrane Permeability/drug effects
MH  - Cells, Cultured
MH  - Chondroitinases and Chondroitin Lyases/metabolism
MH  - Disaccharides/chemistry/pharmacology
MH  - Electrophysiology/methods
MH  - Endothelium, Vascular/drug effects/*physiology/*physiopathology
MH  - Glycocalyx/drug effects/*physiology
MH  - Glycosaminoglycans/physiology
MH  - Heparin Lyase/metabolism
MH  - Heparitin Sulfate/*physiology
MH  - Membrane Glycoproteins/metabolism
MH  - Microcirculation/physiology
MH  - Peptides/*pharmacology
MH  - Polylysine/*pharmacology
MH  - Proteoglycans/metabolism
MH  - Pulmonary Circulation/*physiology
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
EDAT- 2003/05/20 05:00
MHDA- 2003/12/03 05:00
PHST- 2003/May/16 [aheadofprint]
AID - 10.1152/ajplung.00022.2003 [doi]
AID - 00022.2003 [pii]
PST - ppublish
SO  - Am J Physiol Lung Cell Mol Physiol 2003 Nov;285(5):L986-95.

PMID- 12749851
OWN - NLM
STAT- completed
DA  - 20030516
DCOM- 20030711
IS  - 0014-4827
VI  - 286
IP  - 2
DP  - 2003 Jun 10
TI  - Syndecan-1-mediated cell spreading requires signaling by alphavbeta3
      integrins in human breast carcinoma cells.
PG  - 219-32
AB  - Syndecans are cell surface heparan sulfate proteoglycans with regulatory
      roles in cell adhesion, proliferation, and differentiation [Annu. Rev.
      Biochem. 68 (1999) 729]. While the syndecan heparan sulfate chains are
      essential for matrix binding, less is known about the signaling role of
      their core proteins. To mimic syndecan-specific adhesion, MDA-MB-231
      mammary carcinoma cells were plated on antibodies against syndecan-4 or
      syndecan-1. While cells adherent via syndecan-4 spread, cells adherent via
      syndecan-1 do not. However, cells adherent via syndecan-1 can be induced
      to spread by Mn(2+), suggesting that activation of a beta(1) or beta(3)
      integrin partner is required. Surprisingly, pretreatment of cells with a
      function-activating beta(1) antibody does not induce spreading, whereas
      function-blocking beta(1) integrin antibodies do, suggesting involvement
      of a beta(1)-to-beta(3) integrin cross-talk. Indeed, blockade of beta(1)
      integrin activation induces alpha(v)beta(3) integrin activation detectable
      by soluble fibrinogen binding. Spreading in response to syndecan-1 is
      independent of integrin-ligand binding. Furthermore, competition with
      soluble murine syndecan-1 ectodomain, which does not disrupt cell
      adhesion, nonetheless blocks the spreading mechanism. These data suggest
      that the ectodomain of the syndecan-1 core protein directly participates
      in the formation of a signaling complex that signals in cooperation with
      alpha(v)beta(3) integrins; signaling via this complex is negatively
      regulated by beta(1) integrins.
AD  - Department of Pathology and Laboratory Medicine, and Program in Molecular
      and Cellular Pharmacology, University of Wisconsin-Madison, Madison, WI
      53706, USA.
FAU - Beauvais, DeannaLee M
AU  - Beauvais DM
FAU - Rapraeger, Alan C
AU  - Rapraeger AC
LA  - eng
GR  - R01-HD21881/HD/NICHD
GR  - T32-GM08688/GM/NIGMS
PT  - Journal Article
PL  - United States
TA  - Exp Cell Res
JID - 0373226
RN  - 0 (Antigens, CD29)
RN  - 0 (Integrin alphaVbeta3)
RN  - 0 (Integrin beta3)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (syndecan)
RN  - 0 (syndecan-4)
RN  - 7439-95-4 (Magnesium)
SB  - IM
MH  - Antigens, CD29/drug effects/metabolism
MH  - Breast Neoplasms/*metabolism
MH  - Cell Adhesion/drug effects/*physiology
MH  - Cell Movement/drug effects/*physiology
MH  - Eukaryotic Cells/cytology/drug effects/*metabolism
MH  - Female
MH  - Human
MH  - Integrin alphaVbeta3/*metabolism
MH  - Integrin beta3/drug effects/metabolism
MH  - Magnesium/pharmacology
MH  - Membrane Glycoproteins/antagonists & inhibitors/*metabolism
MH  - Protein Structure, Tertiary/drug effects/physiology
MH  - Proteoglycans/antagonists & inhibitors/*metabolism
MH  - Signal Transduction/drug effects/physiology
MH  - Support, U.S. Gov't, P.H.S.
MH  - Tumor Cells, Cultured
EDAT- 2003/05/17 05:00
MHDA- 2003/07/12 05:00
AID - S0014482703001265 [pii]
PST - ppublish
SO  - Exp Cell Res 2003 Jun 10;286(2):219-32.

PMID- 12714503
OWN - NLM
STAT- completed
DA  - 20030805
DCOM- 20030911
IS  - 0006-4971
VI  - 102
IP  - 4
DP  - 2003 Aug 15
TI  - RANTES (CCL5) uses the proteoglycan CD44 as an auxiliary receptor to
      mediate cellular activation signals and HIV-1 enhancement.
PG  - 1169-77
AB  - The CC-chemokine RANTES (regulated on activation normal T-cell expressed
      and secreted; CCL5) transduces multiple intracellular signals. Like all
      chemokines, it stimulates G protein-coupled receptor (GPCR) activity
      through interaction with its cognate chemokine receptor(s), but in
      addition also activates a GPCR-independent signaling pathway. Here, we
      show that the latter pathway is mediated by an interaction between RANTES
      and glycosaminoglycan chains of CD44. We provide evidence that this
      association, at both low, physiologically relevant, and higher, probably
      supraphysiologic concentrations of RANTES, induces the formation of a
      signaling complex composed of CD44, src kinases, and adapter molecules.
      This triggers the activation of the p44/42 mitogen-activated protein
      kinase (MAPK) pathway. By specifically reducing CD44 expression using RNA
      interference we were able to demonstrate that the p44/p42 MAPK activation
      by RANTES requires a high level of CD44 expression. As well as potently
      inhibiting the entry of CCR5 using HIV-1 strains, RANTES can enhance HIV-1
      infectivity under certain experimental conditions. This enhancement
      process depends in part on the activation of p44/p42 MAPK. Here we show
      that silencing of CD44 in HeLa-CD4 cells prevents the activation of
      p44/p42 MAPK and leads to a substantial reduction in HIV-1 infectivity
      enhancement by RANTES.
AD  - Division of Infectious Diseases, Department of Medicine, University
      Hospital, Zurich, Switzerland.
FAU - Roscic-Mrkic, Branka
AU  - Roscic-Mrkic B
FAU - Fischer, Marek
AU  - Fischer M
FAU - Leemann, Christine
AU  - Leemann C
FAU - Manrique, Amapola
AU  - Manrique A
FAU - Gordon, Cynthia J
AU  - Gordon CJ
FAU - Moore, John P
AU  - Moore JP
FAU - Proudfoot, Amanda E I
AU  - Proudfoot AE
FAU - Trkola, Alexandra
AU  - Trkola A
LA  - eng
GR  - R01 AI41420/AI/NIAID
PT  - Journal Article
DEP - 20030424
PL  - United States
TA  - Blood
JID - 7603509
RN  - 0 (Antigens, CD44)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteoglycans)
RN  - 0 (RANTES)
RN  - 0 (Receptors, Chemokine)
RN  - 0 (syndecan)
RN  - EC 2.7.1.112 (src-Family Kinases)
RN  - EC 2.7.1.37 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.1.37 (p42 MAP Kinase)
RN  - EC 2.7.10.- (extracellular signal-regulated kinase 1)
SB  - AIM
SB  - IM
MH  - Antigens, CD44/genetics/*immunology/metabolism
MH  - Down-Regulation
MH  - Enzyme Activation
MH  - HIV-1/*pathogenicity
MH  - Hela Cells
MH  - Human
MH  - Membrane Glycoproteins/immunology/metabolism
MH  - Mitogen-Activated Protein Kinases/metabolism
MH  - Phosphorylation
MH  - Proteoglycans/immunology/metabolism
MH  - RANTES/*immunology/metabolism
MH  - RNA Interference
MH  - Receptors, Chemokine/*immunology/metabolism
MH  - Signal Transduction/physiology
MH  - Support, Non-U.S. Gov't
MH  - Support, U.S. Gov't, P.H.S.
MH  - Transfection
MH  - p42 MAP Kinase/metabolism
MH  - src-Family Kinases/metabolism
EDAT- 2003/04/26 05:00
MHDA- 2003/09/13 05:00
PHST- 2003/Apr/24 [aheadofprint]
AID - 10.1182/blood-2003-02-0488 [doi]
AID - 2003-02-0488 [pii]
PST - ppublish
SO  - Blood 2003 Aug 15;102(4):1169-77.

PMID- 12702549
OWN - NLM
STAT- completed
DA  - 20030709
DCOM- 20030821
LR  - 20031114
IS  - 1073-449X
VI  - 168
IP  - 2
DP  - 2003 Jul 15
TI  - Sputum sol neutrophil elastase activity in bronchiectasis: differential
      modulation by syndecan-1.
PG  - 192-8
AB  - The persistently dominant activity of neutrophil elastase in bronchial
      secretions replete with antielastases is crucial to the pathogenesis of
      bronchiectasis. We hypothesize that components in the bronchial secretions
      bind neutrophil elastase and compromise the inhibitory efficiency of
      prevailing antielastases. Zymographic analysis of sputum sols from
      patients with bronchiectasis found elastase activity in a polydisperse,
      alcian blue-stained zone of high molecular mass. This suggested that
      neutrophil elastase was complexed with polyanionic partners. Western blot
      analysis found not only the polyanionic partner, heparan
      sulfate/syndecan-1, but also the physiological antielastases, secretory
      leukoproteinase inhibitor and alpha1-antitrypsin, in the complex. Both
      dissociative density gradient ultracentrifugation and heparin displacement
      revealed that elastase dissociated from heparan sulfate/syndecan-1 was
      fully inhibited by the endogenous antielastases. This contrasts with the
      effects of exogenous antielastases on sputum neutrophil elastase
      activity-that of alpha1-antitrypsin was limited, but that of secretory
      leukoproteinase inhibitor was facilitated. Similarly, complexed elastase
      on blots of sputum sol zymographs was bound and inhibited by exogenous
      secretory leukoproteinase inhibitor but not by exogenous
      alpha1-antitrypsin. Taken together, the results bring a new focus to
      heparan sulfate/syndecan-1 complexed with neutrophil elastase in inflamed
      bronchial secretions as a target for modulating elastase susceptibility to
      physiological antielastases.
AD  - Department of Biochemistry, University of Hong Kong, 21 Sassoon Road, Hong
      Kong, China. shumdkhk@hkucc.hku.hk
FAU - Chan, Stanley C H
AU  - Chan SC
FAU - Shum, Daisy K Y
AU  - Shum DK
FAU - Ip, Mary S M
AU  - Ip MS
LA  - eng
PT  - Journal Article
DEP - 20030417
PL  - United States
TA  - Am J Respir Crit Care Med
JID - 9421642
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proteins)
RN  - 0 (Proteoglycans)
RN  - 0 (Serine Proteinase Inhibitors)
RN  - 0 (alpha 1-Antitrypsin)
RN  - 0 (antileukoprotease)
RN  - 0 (syndecan)
RN  - 9050-30-0 (Heparitin Sulfate)
RN  - EC 3.4.21.37 (Leukocyte Elastase)
SB  - AIM
SB  - IM
CIN - Am J Respir Crit Care Med. 2003 Jul 15;168(2):144-5. PMID: 12851241
MH  - Blotting, Western
MH  - Bronchiectasis/*enzymology
MH  - Female
MH  - Heparitin Sulfate/metabolism
MH  - Human
MH  - Leukocyte Elastase/*metabolism
MH  - Male
MH  - Membrane Glycoproteins/metabolism
MH  - Middle Aged
MH  - Proteins/metabolism
MH  - Proteoglycans/metabolism
MH  - Serine Proteinase Inhibitors/metabolism
MH  - Sputum/*enzymology
MH  - Support, Non-U.S. Gov't
MH  - alpha 1-Antitrypsin/metabolism
EDAT- 2003/04/19 05:00
MHDA- 2003/08/22 05:00
PHST- 2003/Apr/17 [aheadofprint]
AID - 10.1164/rccm.200208-829OC [doi]
AID - 200208-829OC [pii]
PST - ppublish
SO  - Am J Respir Crit Care Med 2003 Jul 15;168(2):192-8.

