Article
Biochemical characterization, action on macrophages, and superoxide anion production of four basic Phospholipases A2 from Panamanian Bothrops asper Snake Venom
Registro en:
RUEDA, Aristides Quintero et al. Biochemical Characterization, Action on Macrophages, and Superoxide Anion Production of Four Basic Phospholipases A2 from Panamanian Bothrops asper Snake Venom. BioMed Research International, v. 2013, p. 1-9, 2013.
10.1155/2013/789689
Autor
Rueda, Aristides Quintero
Rodríguez, Isela González
Arantes, Eliane C.
Setúbal, Sulamita S.
Calderon, Leonardo de A.
Zuliani, Juliana P.
Stábeli, Rodrigo G.
Soares, Andreimar M.
Resumen
Bothrops asper (Squamata: Viperidae) is the most important venomous snake in Central America, being responsible for the majority of snakebite accidents. Four basic PLA2s (pMTX-I to -IV) were purified from crude venom by a single-step chromatography using a CM-Sepharose ion-exchange column (1.5 × 15 cm). Analysis of the N-terminal sequence demonstrated that pMTX-I and III belong to the catalytically active Asp49 phospholipase A2 subclass, whereas pMTX-II and IV belong to the enzymatically inactive Lys49 PLA2s-like subclass. The PLA2s isolated from Panama Bothrops asper venom (pMTX-I, II, III, and IV) are able to induce myotoxic activity, inflammatory reaction mainly leukocyte migration to the muscle, and induce J774A.1 macrophages activation to start phagocytic activity and superoxide production.