Biochemical characterization, action on macrophages, and superoxide anion production of four basic phospholipases A2 from Panamanian Bothrops asper snake venom.

Content Provider	Europe PMC
Author	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.
Copyright Year	2013
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.
ISSN	23146133
Journal	Biomed Research International
Volume Number	2013
PubMed Central reference number	PMC3591126
PubMed reference number	23509779
e-ISSN	23146141
DOI	10.1155/2013/789689
Language	English
Publisher	Hindawi
Publisher Date	2012-12-24
Access Restriction	Open
Rights License	This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Copyright © 2013 Aristides Quintero Rueda et al.
Content Type	Text
Resource Type	Article
Subject	Immunology and Microbiology Medicine Biochemistry, Genetics and Molecular Biology