Source:http://linkedlifedata.com/resource/pubmed/id/18499669
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
30
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pubmed:dateCreated |
2008-7-21
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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.
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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/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Syndecan-4,
http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases,
http://linkedlifedata.com/resource/pubmed/chemical/transglutaminase 2
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20937-47
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:18499669-3T3 Cells,
pubmed-meshheading:18499669-Animals,
pubmed-meshheading:18499669-Antigens, CD29,
pubmed-meshheading:18499669-CHO Cells,
pubmed-meshheading:18499669-Cell Adhesion,
pubmed-meshheading:18499669-Cricetinae,
pubmed-meshheading:18499669-Cricetulus,
pubmed-meshheading:18499669-Enzyme Activation,
pubmed-meshheading:18499669-Fibronectins,
pubmed-meshheading:18499669-GTP-Binding Proteins,
pubmed-meshheading:18499669-Humans,
pubmed-meshheading:18499669-MAP Kinase Signaling System,
pubmed-meshheading:18499669-Mice,
pubmed-meshheading:18499669-Protein Kinase C-alpha,
pubmed-meshheading:18499669-Syndecan-4,
pubmed-meshheading:18499669-Transglutaminases
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pubmed:year |
2008
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pubmed:articleTitle |
Fibronectin-tissue transglutaminase matrix rescues RGD-impaired cell adhesion through syndecan-4 and beta1 integrin co-signaling.
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pubmed:affiliation |
School of Life and Health Sciences, Aston University, Aston Triangle, Birmingham, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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