| pubmed-article:10594689 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C0016055 | lld:lifeskim |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C1366894 | lld:lifeskim |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C0059239 | lld:lifeskim |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C1424689 | lld:lifeskim |
| pubmed-article:10594689 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:10594689 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10594689 | pubmed:dateCreated | 2000-2-3 | lld:pubmed |
| pubmed-article:10594689 | pubmed:abstractText | The beta1 integrins are a family of heterodimeric adhesion receptors involved in cell-to-cell contacts and cell-to-extracellular matrix interactions. Through their adhesive role, integrins participate in transduction of outside/inside signals and contribute to trigger a multitude of cellular events such as differentiation, cell activation, and motility. The fibronectin integrin receptors, alpha4beta1 and alpha5beta1, can function as costimulatory molecules in T-cell receptor (TCR)-dependent T-cell activation. In the current study the Jurkat T-cell line was used as a model system to investigate the TCR-independent role of cell adhesion to fibronectin in the activation of Zap-70, a central molecule in the signalling events in T cells. Upon adhesion to plastic immobilized fibronectin but not to bovine serum albumin (BSA) the phosphorylation of p125FAK, a protein kinase that localizes to focal adhesion sites, was induced. Moreover, clustering of fibronectin receptors led to the detection of a p125FAK/Zap-70 complex. Finally, while the complex between fak-B, another protein kinase localized to focal adhesion sites, and Zap-70 was detected in cells plated either on BSA or on fibronectin, the formation of the p125FAK/Zap-70 complex appeared specifically induced following fibronectin-mediated integrin clustering. These data suggest the existence of a high degree of specificity when the members of the beta1 integrin family mediate signalling pathways in T cells. | lld:pubmed |
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| pubmed-article:10594689 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10594689 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10594689 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10594689 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10594689 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:10594689 | pubmed:issn | 0019-2805 | lld:pubmed |
| pubmed-article:10594689 | pubmed:author | pubmed-author:ColombattiAA | lld:pubmed |
| pubmed-article:10594689 | pubmed:author | pubmed-author:FormisanoSS | lld:pubmed |
| pubmed-article:10594689 | pubmed:author | pubmed-author:PállGG | lld:pubmed |
| pubmed-article:10594689 | pubmed:author | pubmed-author:PucilloCC | lld:pubmed |
| pubmed-article:10594689 | pubmed:author | pubmed-author:BearzAA | lld:pubmed |
| pubmed-article:10594689 | pubmed:author | pubmed-author:MerluzziSS | lld:pubmed |
| pubmed-article:10594689 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10594689 | pubmed:volume | 98 | lld:pubmed |
| pubmed-article:10594689 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10594689 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10594689 | pubmed:pagination | 564-8 | lld:pubmed |
| pubmed-article:10594689 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10594689 | pubmed:meshHeading | pubmed-meshheading:10594689... | lld:pubmed |
| pubmed-article:10594689 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10594689 | pubmed:articleTitle | Adhesion to fibronectin promotes the activation of the p125(FAK)/Zap-70complex in human T cells. | lld:pubmed |
| pubmed-article:10594689 | pubmed:affiliation | Immunologie, Dipartimento di Scienze e Tecnologie Biomediche, Universitá degli Studi di Udine, Udine, Italy. | lld:pubmed |
| pubmed-article:10594689 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10594689 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10594689 | lld:pubmed |
