Source:http://linkedlifedata.com/resource/pubmed/id/12749851
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2003-5-16
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pubmed:abstractText |
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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD29,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alphaVbeta3,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin beta3,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/SDC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SDC4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-1,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-4,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecans
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-4827
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
219-32
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12749851-Antigens, CD29,
pubmed-meshheading:12749851-Breast Neoplasms,
pubmed-meshheading:12749851-Cell Adhesion,
pubmed-meshheading:12749851-Cell Movement,
pubmed-meshheading:12749851-Eukaryotic Cells,
pubmed-meshheading:12749851-Female,
pubmed-meshheading:12749851-Humans,
pubmed-meshheading:12749851-Integrin alphaVbeta3,
pubmed-meshheading:12749851-Integrin beta3,
pubmed-meshheading:12749851-Magnesium,
pubmed-meshheading:12749851-Membrane Glycoproteins,
pubmed-meshheading:12749851-Protein Structure, Tertiary,
pubmed-meshheading:12749851-Proteoglycans,
pubmed-meshheading:12749851-Signal Transduction,
pubmed-meshheading:12749851-Syndecan-1,
pubmed-meshheading:12749851-Syndecan-4,
pubmed-meshheading:12749851-Syndecans,
pubmed-meshheading:12749851-Tumor Cells, Cultured
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pubmed:year |
2003
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pubmed:articleTitle |
Syndecan-1-mediated cell spreading requires signaling by alphavbeta3 integrins in human breast carcinoma cells.
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pubmed:affiliation |
Department of Pathology and Laboratory Medicine, and Program in Molecular and Cellular Pharmacology, University of Wisconsin-Madison, Madison, WI 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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