BE-I-PLA2, a novel acidic phospholipase A(2) from Bothrops erythromelas venom: Isolation, cloning and characterization as potent anti-platelet and inductor of prostaglandin I-2 release by endothelial cells

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dc.contributor.authorAlbuquerque Modesto, Jeanne Claine de
dc.contributor.authorSpencer, Patrick J.
dc.contributor.authorFritzen, Marcio
dc.contributor.authorValenca, Renata C.
dc.contributor.authorOliva, Maria Luiza Vilela [UNIFESP]
dc.contributor.authorBezerra da Silva, Marcia
dc.contributor.authorChudzinski-Tavassi, Ana Marisa
dc.contributor.authorCamargo Guarnieri, Miriam
dc.contributor.institutionUniversidade Federal de Pernambuco (UFPE)
dc.contributor.institutionInst Butantan
dc.contributor.institutionIPEN
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T12:41:21Z
dc.date.available2016-01-24T12:41:21Z
dc.date.issued2006-07-28
dc.description.abstractA novel acidic Asp49 phospholipase A(2) was isolated from Bothrops erythromelas (jararaca malha-de-cascavel) snake venom by four chromatographic steps. BE-I-PLA2 present a molecular weight of 13,649.57 Da as estimated by mass spectrometry. N-terminal and four internal peptides were sequenced, covering around one-third of the complete toxin sequence. the complete BE-I-PLA2 cDNA was cloned from a B. erythromelas venom-gland cDNA library. the cDNA sequence possesses 457 bp and encodes a protein with significant sequence similarity to many other phospholipase A(2) from snake venoms. When tested in platelet rich plasma, the enzyme showed a potent inhibitory effect on aggregation induced by arachidonic acid and collagen, but not ADP. On the other hand, BE-I-PLA2 did not modify aggregation in washed platelet. Furthermore, no action of BE-I-PLA2 on the principal platelets receptors was observed. Chemical modification with p-bromophenacyl bromide abolished the enzymatic activity of BE-I-PLA2, but its anti-platelet activity was only partially inhibited. in human umbilical-cord veins endothelial cells, BE-I-PLA2 was neither apoptotic nor proliferative but stimulated endothelial cells to release prostaglandin I-2, suggesting an increase of its potential anti-platelet activity in vivo. Further studies are required in order to determine the exact mechanism of action of BE-I-PLA2 in the inhibition of platelet aggregation. (c) 2006 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniv Fed Pernambuco, Dept Zool, Lab Anim Peconhentos & Toxinas, CDU, BR-50670420 Recife, PE, Brazil
dc.description.affiliationUniv Fed Pernambuco, Dept Biofis, BR-50670420 Recife, PE, Brazil
dc.description.affiliationInst Butantan, Lab Bioquim & Biofis, São Paulo, Brazil
dc.description.affiliationIPEN, Mol Biol Lab, São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Bioquim, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Bioquim, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent377-384
dc.identifierhttp://dx.doi.org/10.1016/j.bcp.2006.04.032
dc.identifier.citationBiochemical Pharmacology. Oxford: Pergamon-Elsevier B.V., v. 72, n. 3, p. 377-384, 2006.
dc.identifier.doi10.1016/j.bcp.2006.04.032
dc.identifier.issn0006-2952
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/29052
dc.identifier.wosWOS:000239235000010
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical Pharmacology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectphospholipase A(2)en
dc.subjectsnake venomsen
dc.subjectplateleten
dc.subjectplatelet receptorsen
dc.subjectendothelial cellsen
dc.subjectprostaglandin I-2en
dc.subjectnitric oxideen
dc.titleBE-I-PLA2, a novel acidic phospholipase A(2) from Bothrops erythromelas venom: Isolation, cloning and characterization as potent anti-platelet and inductor of prostaglandin I-2 release by endothelial cellsen
dc.typeinfo:eu-repo/semantics/article
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