1. Biochemical characterization, action on macrophages, and superoxide anion production of four basic phospholipases A2 from Panamanian Bothrops asper snake venom.
- Author
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Rueda AQ, Rodríguez IG, Arantes EC, Setúbal SS, Calderon Lde A, Zuliani JP, Stábeli RG, and Soares AM
- Subjects
- Animals, Cell Line, Cell Movement, Chromatography, Ion Exchange, Coagulants metabolism, Edema pathology, Hemorrhage metabolism, Inflammation, Leukocytes cytology, Macrophages cytology, Macrophages metabolism, Male, Mice, Microscopy, Phase-Contrast, Panama, Phagocytosis, Phospholipases A2 chemistry, Bothrops, Macrophages drug effects, Phospholipases A2 pharmacology, Snake Venoms enzymology, Superoxides metabolism
- Abstract
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.
- Published
- 2013
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