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dc.creatorSaravia Otten, Patricia
dc.creatorFrisan, Teresa
dc.creatorThelestam, Mónica
dc.creatorGutiérrez, José María
dc.date.accessioned2017-02-07T21:43:35Z
dc.date.available2017-02-07T21:43:35Z
dc.date.issued2004-12-01
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0041010104003459es_ES
dc.identifier.issn0041-0101
dc.identifier.urihttp://hdl.handle.net/10669/29515
dc.description.abstractProMMP-2 activation by Bothrops asper venom was investigated in mouse gastrocnemius muscle, mammalian cell culture and a cell-free system. Zymography revealed an increment of latent and activated forms of MMP-2 in muscle homogenates 1–3 days after venom injection. To clarify if venom can induce expression and activation of MMP-2, independently of the inflammatory response, venom was added to cultured human fibroblasts, endothelial and skeletal muscle cells, which expressed proMMP-2 constitutively. Venom activated proMMP-2 without promoting its expression. Venom also activated and degraded proMMP-2 in supernatants collected from fibroblast cultures, indicating that cells are not required for this activation. Pretreatment with EDTA increased MMP-2 activation and reduced degradation. Venom serine proteinases activated proMMP-2, whereas BaP1, a P-I metalloproteinase, predominantly degraded the latent and active forms of MMP-2. Moreover, pretreatment of conditioned medium with serine proteinase inhibitors greatly reduced the venom-induced activation, suggesting that venom proteinases activate MMP-2 via a serine proteinase secreted by fibroblasts. Venom also directly activated and degraded purified proMMP-2, albeit requiring a high concentration. Thus, B. asper venom proteinases activate and degrade proMMP-2 without inducing its synthesis. Serine proteinases play a dominant role in the activation, whereas metalloproteinases predominantly degrade MMP-2. Activation of proMMP-2 by snake venom proteinases, independently of the MT1-MMP/TIMP-2 pathway, extracellular matrix degradation or apoptosis, represents a novel mechanism in human fibroblasts.es_ES
dc.description.sponsorshipSwedish Research Council/[05969]//Sueciaes_ES
dc.description.sponsorshipSwedish International Development Agency as part of the NeTropica///Sueciaes_ES
dc.language.isoen_USes_ES
dc.sourceToxicon; Volumen 44, Número 7. 2004es_ES
dc.subjectMMP-2 Activationes_ES
dc.subjectHuman Fibroblastses_ES
dc.subjectSerine Proteinaseses_ES
dc.subjectMetalloproteinaseses_ES
dc.subjectBothrops Asperes_ES
dc.subjectSnake venomes_ES
dc.titleMembrane independent activation of fibroblast proMMP-2 by snake venom: novel roles for venom proteinaseses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/j.toxicon.2004.08.002
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid15500851


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