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Membrane independent activation of fibroblast proMMP-2 by snake venom: novel roles for venom proteinases
dc.creator | Saravia Otten, Patricia | |
dc.creator | Frisan, Teresa | |
dc.creator | Thelestam, Mónica | |
dc.creator | Gutiérrez, José María | |
dc.date.accessioned | 2017-02-07T21:43:35Z | |
dc.date.available | 2017-02-07T21:43:35Z | |
dc.date.issued | 2004-12-01 | |
dc.identifier.citation | http://www.sciencedirect.com/science/article/pii/S0041010104003459 | |
dc.identifier.issn | 0041-0101 | |
dc.identifier.uri | https://hdl.handle.net/10669/29515 | |
dc.description.abstract | ProMMP-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.sponsorship | Swedish Research Council/[05969]//Suecia | es_ES |
dc.description.sponsorship | Swedish International Development Agency as part of the NeTropica///Suecia | es_ES |
dc.language.iso | en_US | es_ES |
dc.source | Toxicon; Volumen 44, Número 7. 2004 | es_ES |
dc.subject | MMP-2 Activation | es_ES |
dc.subject | Human Fibroblasts | es_ES |
dc.subject | Serine Proteinases | es_ES |
dc.subject | Metalloproteinases | es_ES |
dc.subject | Bothrops Asper | es_ES |
dc.subject | Snake venom | es_ES |
dc.title | Membrane independent activation of fibroblast proMMP-2 by snake venom: novel roles for venom proteinases | es_ES |
dc.type | artículo original | |
dc.identifier.doi | 10.1016/j.toxicon.2004.08.002 | |
dc.description.procedence | UCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP) | es_ES |
dc.identifier.pmid | 15500851 |
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Microbiología [1170]