Artículos de revistas
Isolation and functional characterization of proinflammatory acidic phospholipase A(2) from Bothrops leucurus snake venom
Fecha
2011Registro en:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-TOXICOLOGY & PHARMACOLOGY, v.154, n.3, p.226-233, 2011
1532-0456
10.1016/j.cbpc.2011.06.003
Autor
NUNES, Debora C. O.
RODRIGUES, Renata S.
LUCENA, Malson N.
COLOGNA, Camila T.
OLIVEIRA, Ana Carolina S.
HAMAGUCHI, Amelia
HOMSI-BRANDEBURGO, Maria I.
ARANTES, Eliane C.
TEIXEIRA, David N. S.
UEIRA-VIEIRA, Carlos
RODRIGUES, Veridiana M.
Institución
Resumen
In the present study, an acidic PLA(2), designated BI-PLA(2), was isolated from Bothrops leucurus snake venom through two chromatographic steps: ion-exchange on CM-Sepharose and hydrophobic chromatography on Phenyl-Sepharose. Bl-PLA(2) was homogeneous on SDS-PAGE and when submitted to 2D electrophoresis the molecular mass was 15,000 Da and pl was 5.4. Its N-terminal sequence revealed a high homology with other Asp49 acidic PLA(2)s from snake venoms. Its specific activity was 159.9 U/mg and the indirect hemolytic activity was also higher than that of the crude venom. Bl-PLA(2) induced low myotoxic and edema activities as compared to those of the crude venom. Moreover, the enzyme was able to induce increments in IL-12p40, TNF-alpha, IL-1 beta and IL-6 levels and no variation of IL-8 and IL-10 in human PBMC stimulated in vitro, suggesting that Bl-PLA2 induces proinflammatory cytokine production by human mononuclear cells. Bothrops leucurus venom is still not extensively explored and knowledge of its components will contribute for a better understanding of its action mechanism. (C) 2011 Elsevier Inc. All rights reserved.