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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1999-3-29
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pubmed:abstractText |
Human fibrillin, a major component of the extracellular matrix, exists as two highly homologous forms (fibrillin-1 and -2). Several modules of fibrillin are homologous to TGF-beta1 binding protein. Two of these modules, D25 (the 25th module of fibrillin-1 and -2 D segment) and D12 (the 12th module of fibrillin-2 D segment) contain the cell adhesion motif arginyl-glycyl-aspartyl (RGD). The ability of RGD to mediate adhesion to D25-1 and D12-2 was investigated using bacterially expressed fusion proteins. Human skin fibroblasts and murine L-cells were used in microassays of cell attachment and cell spreading on fibrillin fusion-protein substrata. Dose-dependent experiments and competitive inhibition by soluble RGD-containing peptides demonstrated that D25-1 and D12-2 mediate RGD-dependent cell adhesion. These results provide evidence for a cell adhesion function of fibrillin-2. Inhibition with anti-integrin antibodies showed that alpha(v) and beta3 integrins mediate adhesion to D25-1, while alpha3, alpha(v) and beta1 are involved in adhesion to D12-2. Binding of different receptors may elicit distinct cell signalling supporting the hypothesis that fibrillin-1 and fibrillin-2 have distinct roles.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Latent TGF-beta Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/fibrillin
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pubmed:status |
MEDLINE
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pubmed:issn |
0300-8207
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9643645-Amino Acid Sequence,
pubmed-meshheading:9643645-Animals,
pubmed-meshheading:9643645-Carrier Proteins,
pubmed-meshheading:9643645-Cell Adhesion,
pubmed-meshheading:9643645-Collagen,
pubmed-meshheading:9643645-Cytoskeleton,
pubmed-meshheading:9643645-Fibronectins,
pubmed-meshheading:9643645-Humans,
pubmed-meshheading:9643645-Integrins,
pubmed-meshheading:9643645-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:9643645-L Cells (Cell Line),
pubmed-meshheading:9643645-Latent TGF-beta Binding Proteins,
pubmed-meshheading:9643645-Mice,
pubmed-meshheading:9643645-Microfilament Proteins,
pubmed-meshheading:9643645-Molecular Sequence Data,
pubmed-meshheading:9643645-Peptides,
pubmed-meshheading:9643645-Protein Binding,
pubmed-meshheading:9643645-Sequence Homology, Amino Acid,
pubmed-meshheading:9643645-Serum Albumin, Bovine
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pubmed:year |
1998
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pubmed:articleTitle |
TGF-beta1 binding protein-like modules of fibrillin-1 and -2 mediate integrin-dependent cell adhesion.
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pubmed:affiliation |
Department of Neuropathology, Institute of Neurology, London, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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