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dc.creatorCamacho Umaña, Erika
dc.creatorVillalobos Chacón, Eva
dc.creatorSanz, Libia
dc.creatorPérez, Alicia
dc.creatorEscalante Muñoz, Teresa
dc.creatorLomonte, Bruno
dc.creatorCalvete Chornet, Juan José
dc.creatorGutiérrez, José María
dc.creatorRucavado Romero, Alexandra
dc.date.accessioned2017-06-12T16:14:07Z
dc.date.available2017-06-12T16:14:07Z
dc.date.issued2014-06
dc.identifier.citationhttp://www.sciencedirect.com/science/article/pii/S0300908414000121es_ES
dc.identifier.issn0300-9084
dc.identifier.urihttp://hdl.handle.net/10669/30091
dc.description.abstractA new homodimeric PII metalloproteinase, named BlatH1, was purified from the venom of the Central American arboreal viperid snake Bothriechis lateralis by a combination of anion-exchange chromatography, hydrophobic interaction chromatography, and gel filtration. BlatH1 is a glycoprotein of 84 kDa. The mature protein contains a metalloproteinase domain, with the characteristic zinc-binding motif (HEXXHXXGXXH) followed by the sequence CIM at the Met-turn. In the disintegrin domain, the tripeptide sequence TDN substitutes the characteristic RGD motif found in many disintegrins. BlatH1 hydrolyzed azocasein, gelatin and fibrinogen, and exerts a potent local and systemic hemorrhagic activity in mice. The hemorrhagic activity of BlatH1 is not inhibited by the plasma proteinase inhibitor α2-macroglobulin, although the SVMP is able to cleave this plasma inhibitor, generating a 90 kDa product. BlatH1 inhibits ADP- and collagen-induced human platelet aggregation (IC50 = 0.3 μM and 0.7 μM for ADP and collagen, respectively). This activity is abrogated when the enzyme is preincubated with the metalloproteinase inhibitor Batimastat, implying that it depends on proteolysis. In agreement, a synthetic peptide containing the sequence TDN of the disintegrin domain is unable to inhibit platelet aggregation. BlatH1 is a valuable tool to understand the structural determinants of toxicity in PII SVMPs.es_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-B0-528]/UCR/Costa Ricaes_ES
dc.description.sponsorshipUniversidad de Costa Rica/[741-B2-517]/UCR/Costa Ricaes_ES
dc.description.sponsorshipInternational Foundation for Science/[F/4096-2]/IFS/Sueciaes_ES
dc.description.sponsorshipNetwork for Research and Training in Tropical Diseases in Central America/[01N-2010]/NeTropica/es_ES
dc.description.sponsorshipMinisterio de Educación y Ciencia/[BFU2010-17373]//Españaes_ES
dc.language.isoen_USes_ES
dc.sourceBiochimie; Volumen 101. 2014es_ES
dc.subjectBothriechis lateralises_ES
dc.subjectSnake venom metalloproteinasees_ES
dc.subjectα2-Macroglobulines_ES
dc.subjectPII SVMPes_ES
dc.subjectPlatelet aggregationes_ES
dc.subjectHemorrhagic activityes_ES
dc.subjectSnake venomes_ES
dc.titleUnderstanding structural and functional aspects of PII snake venom metalloproteinases: Characterization of BlatH1, a hemorrhagic dimeric enzyme from the venom of Bothriechis lateralises_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1016/j.biochi.2014.01.008
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES
dc.identifier.pmid24457155


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