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10.1093/cvr/cvu053 http://scihub22266oqcxt.onion/10.1093/cvr/cvu053 C4030512!4030512 !24639195     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24639195 &cmd=llinks): Failed to open stream: HTTP request failed! 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Integrins ?v?5 and ?v?3 promote latent TGF-?1 activation by human cardiac fibroblast contraction |pdf=|usr=}}{{24639195 }} gab.com Text Integrins v 5 and v 3 promote latent TGF- 1 activation by human cardiac fibroblast contraction JO: Cardiovasc Res http://www.kidney.de/pget.php?&tw=1&pmid=24639195 #FOAvip AIMS: Pathological tissue remodelling by myofibroblast contraction is a hallmark of cardiac fibrosis. Myofibroblasts differentiate from cardiac fibroblasts under the action of transforming growth factor-?1 (TGF-?1), which is secreted into the extracellular matrix as a large latent complex. Integrin-mediated traction forces activate TGF-?1 by inducing a conformational change in the latent complex. The mesenchymal integrins ?v?5 and ?v?3 are expressed in the heart, but their role in the activation of TGF-?1 remains elusive. Here, we test whether targeting ?v?5 and ?v?3 integrins reduces latent TGF-?1 activation by cardiac fibroblasts with the goal to prevent the formation of ?-smooth muscle actin (?-SMA)-expressing cardiac myofibroblasts and their contribution to fibrosis. METHODS AND RESULTS: Using a porcine model of induced right ventricular fibrosis and pro-fibrotic culture conditions, we show that integrins ?v?5 and ?v?3 are up-regulated in myofibroblast-enriched fibrotic lesions and differentiated cultured human cardiac myofibroblasts. Both integrins autonomously contribute to latent TGF-?1 activation and myofibroblast differentiation, as demonstrated by function-blocking peptides and antibodies. Acute blocking of both integrins leads to significantly reduced TGF-?1 activation by cardiac fibroblast contraction and loss of ?-SMA expression, which is restored by adding active TGF-?1. Manipulating integrin protein levels in overexpression and shRNA experiments reveals that both integrins can compensate for each other with respect to TGF-?1 activation and induction of ?-SMA expression. CONCLUSIONS: Integrins ?v?5 and ?v?3 both control myofibroblast differentiation by activating latent TGF-?1. Pharmacological targeting of mesenchymal integrins is a possible strategy to selectively block TGF-?1 activation by cardiac myofibroblasts and progression of fibrosis in the heart. Twit Text FOAVip Integrins v 5 and v 3 promote latent TGF- 1 activation by human cardiac fibroblast contraction ????Cardiovasc Res http://www.kidney.de/pget.php?&tw=1&pmid=24639195 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24639195 #FOAvip English Wikipedia <ref>{{Cite pmid|24639195 }}</ref> Integrins ?v?5 and ?v?3 promote latent TGF-?1 activation by human cardiac fibroblast contraction #MMPMID24639195 Sarrazy V ; Koehler A ; Chow ML ; Zimina E ; Li CX ; Kato H ; Caldarone CA ; Hinz B Cardiovasc Res 2014[Jun]; 102 (3 ): 407-17 PMID24639195 show ga AIMS: Pathological tissue remodelling by myofibroblast contraction is a hallmark of cardiac fibrosis. Myofibroblasts differentiate from cardiac fibroblasts under the action of transforming growth factor-?1 (TGF-?1), which is secreted into the extracellular matrix as a large latent complex. Integrin-mediated traction forces activate TGF-?1 by inducing a conformational change in the latent complex. The mesenchymal integrins ?v?5 and ?v?3 are expressed in the heart, but their role in the activation of TGF-?1 remains elusive. Here, we test whether targeting ?v?5 and ?v?3 integrins reduces latent TGF-?1 activation by cardiac fibroblasts with the goal to prevent the formation of ?-smooth muscle actin (?-SMA)-expressing cardiac myofibroblasts and their contribution to fibrosis. METHODS AND RESULTS: Using a porcine model of induced right ventricular fibrosis and pro-fibrotic culture conditions, we show that integrins ?v?5 and ?v?3 are up-regulated in myofibroblast-enriched fibrotic lesions and differentiated cultured human cardiac myofibroblasts. Both integrins autonomously contribute to latent TGF-?1 activation and myofibroblast differentiation, as demonstrated by function-blocking peptides and antibodies. Acute blocking of both integrins leads to significantly reduced TGF-?1 activation by cardiac fibroblast contraction and loss of ?-SMA expression, which is restored by adding active TGF-?1. Manipulating integrin protein levels in overexpression and shRNA experiments reveals that both integrins can compensate for each other with respect to TGF-?1 activation and induction of ?-SMA expression. CONCLUSIONS: Integrins ?v?5 and ?v?3 both control myofibroblast differentiation by activating latent TGF-?1. Pharmacological targeting of mesenchymal integrins is a possible strategy to selectively block TGF-?1 activation by cardiac myofibroblasts and progression of fibrosis in the heart. |Actins/analysis [MESH] |Adult [MESH] |Animals [MESH] |Cell Differentiation [MESH] |Cells, Cultured [MESH] |Fibrosis [MESH] |Humans [MESH] |Integrin alphaVbeta3/antagonists & inhibitors/*physiology [MESH] |Male [MESH] |Myocardium/pathology [MESH] |Myofibroblasts/*pathology [MESH] |Receptors, Vitronectin/antagonists & inhibitors/*physiology [MESH] |Swine [MESH]Integrins ?v?5 and ?v?3 promote latent TGF-?1 activation by human card(epmc).pdf DeepDyve Pubget Overpricing