| pubmed-article:10477272 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10477272 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10477272 | lifeskim:mentions | umls-concept:C0225369 | lld:lifeskim |
| pubmed-article:10477272 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:10477272 | lifeskim:mentions | umls-concept:C0140080 | lld:lifeskim |
| pubmed-article:10477272 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:10477272 | lifeskim:mentions | umls-concept:C0081938 | lld:lifeskim |
| pubmed-article:10477272 | lifeskim:mentions | umls-concept:C0282116 | lld:lifeskim |
| pubmed-article:10477272 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:10477272 | pubmed:dateCreated | 1999-12-8 | lld:pubmed |
| pubmed-article:10477272 | pubmed:abstractText | We have examined the mechanism by which collagen-binding integrins co-operate with insulin-like growth factor-I (IGF-I) receptors (IGF-IR) to regulate chondrocyte phenotype and differentiation. Adhesion of chondrocytes to anti-beta1 integrin antibodies or collagen type II leads to phosphorylation of cytoskeletal and signalling proteins localized at focal adhesions, including alpha-actinin, vinculin, paxillin and focal adhesion kinase (FAK). These stimulate docking proteins such as Shc (Src-homology collagen). Moreover, exposure of collagen type II-cultured chondrocytes to IGF-I leads to co-immunoprecipitation of Shc protein with the IGF-IR and with beta1, alpha1 and alpha5 integrins, but not with alpha3 integrin. Shc then associates with growth factor receptor-bound protein 2 (Grb2), an adaptor protein and extracellular signal-regulated kinase. The expression of the docking protein Shc occurs only when chondrocytes are bound to collagen type II or integrin antibodies and increases when IGF-I is added, suggesting a collaboration between integrins and growth factors in a common/shared biochemical signalling pathway. Furthermore, these results indicate that focal adhesion assembly may facilitate signalling via Shc, a potential common target for signal integration between integrin and growth-factor signalling regulatory pathways. Thus, the collagen-binding integrins and IGF-IR co-operate to regulate focal adhesion components and these signalling pathways have common targets (Shc-Grb2 complex) in subcellular compartments, thereby linking to the Ras-mitogen-activated protein kinase signalling pathway. These events may play a role during chondrocyte differentiation. | lld:pubmed |
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| pubmed-article:10477272 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10477272 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10477272 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10477272 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10477272 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10477272 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:10477272 | pubmed:author | pubmed-author:De SouzaPP | lld:pubmed |
| pubmed-article:10477272 | pubmed:author | pubmed-author:MerkerH JHJ | lld:pubmed |
| pubmed-article:10477272 | pubmed:author | pubmed-author:JohnTT | lld:pubmed |
| pubmed-article:10477272 | pubmed:author | pubmed-author:RahmanzadehRR | lld:pubmed |
| pubmed-article:10477272 | pubmed:author | pubmed-author:ShakibaeiMM | lld:pubmed |
| pubmed-article:10477272 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10477272 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10477272 | pubmed:volume | 342 Pt 3 | lld:pubmed |
| pubmed-article:10477272 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10477272 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10477272 | pubmed:pagination | 615-23 | lld:pubmed |
| pubmed-article:10477272 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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