| pubmed-article:18202198 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18202198 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:18202198 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:18202198 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:18202198 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:18202198 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:18202198 | lifeskim:mentions | umls-concept:C0015520 | lld:lifeskim |
| pubmed-article:18202198 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:18202198 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:18202198 | pubmed:dateCreated | 2008-1-31 | lld:pubmed |
| pubmed-article:18202198 | pubmed:abstractText | Coagulation proteases have been suggested to play a role in the pathogenesis of tissue remodeling and fibrosis. We therefore assessed the proinflammatory and fibroproliferative effects of coagulation protease factor (F)Xa. We show that FXa elicits a signaling response in C2C12 and NIH3T3 fibroblasts. FXa-induced ERK1/2 phosphorylation was dependent on protease-activated receptor (PAR)-2 cleavage because desensitization with a PAR-2 agonist (trypsin) but not a PAR-1 agonist (thrombin) abolished FXa-induced signal transduction and PAR-2 siRNA abolished FXa-induced ERK1/2 phosphorylation. The PAR-2-dependent cellular effects of FXa led to fibroblast proliferation, migration, and differentiation into myofibroblasts, as demonstrated by the expression of alpha-smooth muscle actin and desmin, followed by the secretion of the cytokines monocyte chemotactic protein-1 and interleukin-6 as well as the expression of the fibrogenic proteins transforming growth factor-beta and fibronectin. To assess the relevance of FXa-induced proliferation and cell migration, we examined the effect of FXa in a wound scratch assay. Indeed, FXa facilitated wound healing in a PAR-2- and ERK1/2-dependent manner. Taken together, these results support the notion that, beyond its role in coagulation, FXa-dependent PAR-2 cleavage might play a role in the progression of tissue fibrosis and remodeling. | lld:pubmed |
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| pubmed-article:18202198 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18202198 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18202198 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:18202198 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18202198 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18202198 | pubmed:issn | 0002-9440 | lld:pubmed |
| pubmed-article:18202198 | pubmed:author | pubmed-author:Peppelenbosch... | lld:pubmed |
| pubmed-article:18202198 | pubmed:author | pubmed-author:ReitsmaPieter... | lld:pubmed |
| pubmed-article:18202198 | pubmed:author | pubmed-author:BorensztajnKe... | lld:pubmed |
| pubmed-article:18202198 | pubmed:author | pubmed-author:SpekC... | lld:pubmed |
| pubmed-article:18202198 | pubmed:author | pubmed-author:StiekemaJurri... | lld:pubmed |
| pubmed-article:18202198 | pubmed:author | pubmed-author:NijmeijerSeba... | lld:pubmed |
| pubmed-article:18202198 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18202198 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:18202198 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18202198 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18202198 | pubmed:pagination | 309-20 | lld:pubmed |
| pubmed-article:18202198 | pubmed:dateRevised | 2010-9-22 | lld:pubmed |
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