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dc.creatorVoisin, Mathieu-Benoit
dc.creatorRucavado Romero, Alexandra
dc.creatorMorazán, Diego
dc.creatorMacêdo, Jéssica Kele A.
dc.creatorCalvete Chornet, Juan José
dc.creatorSanz, Libia
dc.creatorNourshargh, Sussan
dc.creatorGutiérrez, José María
dc.creatorFox, Jay W.
dc.creatorHerrera Arias, Cristina
dc.creatorEscalante Muñoz, Teresa
dc.date.accessioned2017-07-07T15:46:02Z
dc.date.available2017-07-07T15:46:02Z
dc.date.issued2015-04-24
dc.identifier.citationhttp://journals.plos.org/plosntds/article?id=10.1371/journal.pntd.0003731es_ES
dc.identifier.issn1935-2735
dc.identifier.urihttp://hdl.handle.net/10669/30337
dc.description.abstractSnake venom hemorrhagic metalloproteinases (SVMPs) of the PI, PII and PIII classes were compared in terms of tissue localization and their ability to hydrolyze basement membrane components in vivo, as well as by a proteomics analysis of exudates collected in tissue injected with these enzymes. Immunohistochemical analyses of co-localization of these SVMPs with type IV collagen revealed that PII and PIII enzymes co-localized with type IV collagen in capillaries, arterioles and post-capillary venules to a higher extent than PI SVMP, which showed a more widespread distribution in the tissue. The patterns of hydrolysis by these three SVMPs of laminin, type VI collagen and nidogen in vivo greatly differ, whereas the three enzymes showed a similar pattern of degradation of type IV collagen, supporting the concept that hydrolysis of this component is critical for the destabilization of microvessel structure leading to hemorrhage. Proteomic analysis of wound exudate revealed similarities and differences between the action of the three SVMPs. Higher extent of proteolysis was observed for the PI enzyme regarding several extracellular matrix components and fibrinogen, whereas exudates from mice injected with PII and PIII SVMPs had higher amounts of some intracellular proteins. Our results provide novel clues for understanding the mechanisms by which SVMPs induce damage to the microvasculature and generate hemorrhage.es_ES
dc.description.sponsorshipUniversidad de Costa Rica//UCR/Costa Ricaes_ES
dc.language.isoen_USes_ES
dc.rightsAtribución-CompartirIgual 3.0 Costa Rica*
dc.rights.urihttp://creativecommons.org/licenses/by-sa/3.0/cr/*
dc.sourcePLOS Neglected Tropical Diseases; Volumen 9, Número 4. 2015es_ES
dc.subjectCollageneses_ES
dc.subjectVenomses_ES
dc.subjectHydrolysises_ES
dc.subjectExtracellular Matrix Proteinses_ES
dc.subjectHemorrhagees_ES
dc.subjectBasement Membranees_ES
dc.subjectSerum proteinses_ES
dc.subjectMembrane proteinses_ES
dc.titleTissue Localization and Extracellular Matrix Degradation by PI, PII and PIII Snake Venom Metalloproteinases: Clues on the Mechanisms of Venom-Induced Hemorrhagees_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1371/journal.pntd.0003731
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid25909592
dc.identifier.pmidPMC4409213


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Atribución-CompartirIgual 3.0 Costa Rica
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