Full metadata record
DC Field | Value | Language |
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dc.creator | Orbe, J. (Josune) | - |
dc.creator | Rodriguez, J.A. (José Antonio) | - |
dc.creator | Calvayrac, O. (Olivier) | - |
dc.creator | Rodriguez-Calvo, R. (Ricardo) | - |
dc.creator | Rodriguez, C. (Cristina) | - |
dc.creator | Roncal, C. (Carmen) | - |
dc.creator | Martinez-de-Lizarrondo, S. (Sara) | - |
dc.creator | Barrenetxe, J. (Jaione) | - |
dc.creator | Reverter, J.C. (Juan C.) | - |
dc.creator | Martinez-Gonzalez, J. (José) | - |
dc.creator | Paramo, J.A. (José Antonio) | - |
dc.date.accessioned | 2012-05-28T15:38:25Z | - |
dc.date.available | 2012-05-28T15:38:25Z | - |
dc.date.issued | 2009 | - |
dc.identifier.citation | Orbe J, Rodriguez JA, Calvayrac O, Rodriguez-Calvo R, Rodriguez C, Roncal C, et al. Matrix metalloproteinase-10 is upregulated by thrombin in endothelial cells and increased in patients with enhanced thrombin generation. Arterioscler Thromb Vasc Biol 2009 Dec;29(12):2109-2116. | es_ES |
dc.identifier.issn | 1524-4636 | - |
dc.identifier.uri | https://hdl.handle.net/10171/22257 | - |
dc.description.abstract | OBJECTIVE: Thrombin is a multifunctional serine protease that promotes vascular proinflammatory responses whose effect on endothelial MMP-10 expression has not previously been evaluated. METHODS AND RESULTS: Thrombin induced endothelial MMP-10 mRNA and protein levels, through a protease-activated receptor-1 (PAR-1)-dependent mechanism, in a dose- and time-dependent manner. This effect was mimicked by a PAR-1 agonist peptide (TRAP-1) and antagonized by an anti-PAR-1 blocking antibody. MMP-10 induction was dependent on extracellular regulated kinase1/2 (ERK1/2) and c-jun N-terminal kinase (JNK) pathways. By serial deletion analysis, site-directed mutagenesis and electrophoretic mobility shift assay an AP-1 site in the proximal region of MMP-10 promoter was found to be critical for thrombin-induced MMP-10 transcriptional activity. Thrombin and TRAP-1 upregulated MMP-10 in murine endothelial cells in culture and in vivo in mouse aorta. This effect of thrombin was not observed in PAR-1-deficient mice. Interestingly, circulating MMP-10 levels (P<0.01) were augmented in patients with endothelial activation associated with high (disseminated intravascular coagulation) and moderate (previous acute myocardial infarction) systemic thrombin generation. CONCLUSIONS: Thrombin induces MMP-10 through a PAR-1-dependent mechanism mediated by ERK1/2, JNK, and AP-1 activation. Endothelial MMP-10 upregulation could be regarded as a new proinflammatory effect of thrombin whose pathological consequences in thrombin-related disorders and plaque stability deserve further investigation. | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | American Heart Association | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.subject | Thrombin | es_ES |
dc.subject | Endothelium | es_ES |
dc.subject | MMP-10 | es_ES |
dc.subject | Atherosclerosis | es_ES |
dc.subject | Thrombosis | es_ES |
dc.title | Matrix metalloproteinase-10 is upregulated by thrombin in endothelial cells and increased in patients with enhanced thrombin generation | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.relation.publisherversion | http://atvb.ahajournals.org/content/29/12/2109 | es_ES |
dc.type.driver | info:eu-repo/semantics/article | es_ES |
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