Molecular and functional characterization of a new non-hemorrhagic metalloprotease from Bothrops jararacussu snake venom with antiplatelet activity

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorMarcussi, Silvana
dc.creatorBernardeS, Carolina P.
dc.creatorSantos-Filho, Norival A.
dc.creatorMazzi, Mauricio V.
dc.creatorOliveira, Clayton Z.
dc.creatorIzidoro, Luiz Fernando M.
dc.creatorFuly, Andre L.
dc.creatorMagro, Angelo J.
dc.creatorBraz, Antonio S. K.
dc.creatorFontes, Marcos R. M.
dc.creatorGiglio, Jose R.
dc.creatorSoares, Andreimar M.
dc.date2014-05-20T13:49:21Z
dc.date2016-10-25T17:01:51Z
dc.date2014-05-20T13:49:21Z
dc.date2016-10-25T17:01:51Z
dc.date2007-12-01
dc.date.accessioned2017-04-05T21:01:05Z
dc.date.available2017-04-05T21:01:05Z
dc.identifierPeptides. New York: Elsevier B.V., v. 28, n. 12, p. 2328-2339, 2007.
dc.identifier0196-9781
dc.identifierhttp://hdl.handle.net/11449/17585
dc.identifierhttp://acervodigital.unesp.br/handle/11449/17585
dc.identifier10.1016/j.peptides.2007.10.010
dc.identifierWOS:000251698000010
dc.identifierhttp://dx.doi.org/10.1016/j.peptides.2007.10.010
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/864033
dc.descriptionBjussuMP-II is an acidic low molecular weight metalloprotease (Mr similar to 24,000 and pI similar to 6.5), isolated from Bothrops jararacussu snake venom. The chromatographic profile in RP-HPLC and its N-terminal sequence confirmed its high purity level. Its complete cDNA was obtained by RT-PCR and the 615 bp codified for a mature protein of 205 amino acid residues. The multiple alignment of its deduced amino acid sequence and those of other snake venom metalloproteases showed a high structural similarity, mainly among class P-I proteases. The molecular modeling analysis of BjussuMP-II showed also conserved structural features with other SVMPs. BjussuMP-II did not induce hemorrhage, myotoxicity and lethality, but displayed dose-dependent proteolytic activity on fibrinogen, collagen, fibrin, casein and gelatin, keeping stable at different pHs, temperatures and presence of several divalent ions. BjussuMP-II did not show any clotting or anticoagulant activity on human citrated plasma, in contrast to its inhibitory effects on platelet aggregation. The aspects broached, in this work, provide data on the relationship between structure and function, in order to better understand the effects elicited by snake venom metalloproteases. (c) 2007 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationPeptides
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectmetalloprotease
dc.subjectfibrinogenase
dc.subjectsnake venom
dc.subjectBothrops jararacussu
dc.subjectbiological activity
dc.subjectantiplatelet activity
dc.subjectcDNA
dc.subjectmolecular model
dc.titleMolecular and functional characterization of a new non-hemorrhagic metalloprotease from Bothrops jararacussu snake venom with antiplatelet activity
dc.typeOtro


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