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| pubmed-article:18499669 | lifeskim:mentions | umls-concept:C0081938 | lld:lifeskim |
| pubmed-article:18499669 | lifeskim:mentions | umls-concept:C0250564 | lld:lifeskim |
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| pubmed-article:18499669 | lifeskim:mentions | umls-concept:C0331858 | lld:lifeskim |
| pubmed-article:18499669 | pubmed:issue | 30 | lld:pubmed |
| pubmed-article:18499669 | pubmed:dateCreated | 2008-7-21 | lld:pubmed |
| pubmed-article:18499669 | pubmed:abstractText | Heterotropic association of tissue transglutaminase (TG2) with extracellular matrix-associated fibronectin (FN) can restore the adhesion of fibroblasts when the integrin-mediated direct binding to FN is impaired using RGD-containing peptide. We demonstrate that the compensatory effect of the TG-FN complex in the presence of RGD-containing peptides is mediated by TG2 binding to the heparan sulfate chains of the syndecan-4 cell surface receptor. This binding mediates activation of protein kinase Calpha (PKCalpha) and its subsequent interaction with beta(1) integrin since disruption of PKCalpha binding to beta(1) integrins with a cell-permeant competitive peptide inhibits cell adhesion and the associated actin stress fiber formation. Cell signaling by this process leads to the activation of focal adhesion kinase and ERK1/2 mitogen-activated protein kinases. Fibroblasts deficient in Raf-1 do not respond fully to the TG-FN complex unless either the full-length kinase competent Raf-1 or the kinase-inactive domain of Raf-1 is reintroduced, indicating the involvement of the Raf-1 protein in the signaling mechanism. We propose a model for a novel RGD-independent cell adhesion process that could be important during tissue injury and/or remodeling whereby TG-FN binding to syndecan-4 activates PKCalpha leading to its association with beta(1) integrin, reinforcement of actin-stress fiber organization, and MAPK pathway activation. | lld:pubmed |
| pubmed-article:18499669 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18499669 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18499669 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18499669 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:18499669 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:18499669 | pubmed:author | pubmed-author:LiXiaolingX | lld:pubmed |
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| pubmed-article:18499669 | pubmed:author | pubmed-author:WangZhuoZ | lld:pubmed |
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| pubmed-article:18499669 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18499669 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:18499669 | pubmed:volume | 283 | lld:pubmed |
| pubmed-article:18499669 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18499669 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18499669 | pubmed:pagination | 20937-47 | lld:pubmed |
| pubmed-article:18499669 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:18499669 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18499669 | pubmed:articleTitle | Fibronectin-tissue transglutaminase matrix rescues RGD-impaired cell adhesion through syndecan-4 and beta1 integrin co-signaling. | lld:pubmed |
| pubmed-article:18499669 | pubmed:affiliation | School of Life and Health Sciences, Aston University, Aston Triangle, Birmingham, United Kingdom. | lld:pubmed |
| pubmed-article:18499669 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18499669 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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