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.author Albuquerque Modesto, Jeanne Claine de
dc.contributor.author Spencer, Patrick J.
dc.contributor.author Fritzen, Marcio
dc.contributor.author Valenca, Renata C.
dc.contributor.author Oliva, Maria Luiza Vilela [UNIFESP]
dc.contributor.author Bezerra da Silva, Marcia
dc.contributor.author Chudzinski-Tavassi, Ana Marisa
dc.contributor.author Camargo Guarnieri, Miriam
dc.date.accessioned 2016-01-24T12:41:21Z
dc.date.available 2016-01-24T12:41:21Z
dc.date.issued 2006-07-28
dc.identifier http://dx.doi.org/10.1016/j.bcp.2006.04.032
dc.identifier.citation Biochemical Pharmacology. Oxford: Pergamon-Elsevier B.V., v. 72, n. 3, p. 377-384, 2006.
dc.identifier.issn 0006-2952
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/29052
dc.description.abstract A 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.format.extent 377-384
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Biochemical Pharmacology
dc.rights Acesso restrito
dc.subject phospholipase A(2) en
dc.subject snake venoms en
dc.subject platelet en
dc.subject platelet receptors en
dc.subject endothelial cells en
dc.subject prostaglandin I-2 en
dc.subject nitric oxide en
dc.title 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 en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de Pernambuco (UFPE)
dc.contributor.institution Inst Butantan
dc.contributor.institution IPEN
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.description.affiliation Univ Fed Pernambuco, Dept Zool, Lab Anim Peconhentos & Toxinas, CDU, BR-50670420 Recife, PE, Brazil
dc.description.affiliation Univ Fed Pernambuco, Dept Biofis, BR-50670420 Recife, PE, Brazil
dc.description.affiliation Inst Butantan, Lab Bioquim & Biofis, São Paulo, Brazil
dc.description.affiliation IPEN, Mol Biol Lab, São Paulo, Brazil
dc.description.affiliation Universidade Federal de São Paulo, Dept Bioquim, São Paulo, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Bioquim, São Paulo, Brazil
dc.identifier.doi 10.1016/j.bcp.2006.04.032
dc.description.source Web of Science
dc.identifier.wos WOS:000239235000010



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