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Biomed Res Int ; 2013: 789689, 2013.
Article in English | MEDLINE | ID: mdl-23509779

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.


Subject(s)
Bothrops , Macrophages/drug effects , Phospholipases A2/pharmacology , Snake Venoms/enzymology , Superoxides/metabolism , 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
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