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Action of two phospholipases A2 purified from Bothrops alternatus snake venom on macrophages

The in vitro effects of BaltTX-I, a catalytically inactive Lys49 variant of phospholipase A 2 (PLA 2 ), and BaltTX-II, an Asp49 catalytically active PLA 2 isolated from Bothrops alternatus snake venom, on thioglycollate-elicited macrophages (TG-macrophages) were investigated. At non-cytotoxic concen...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2013-02, Vol.78 (2), p.194-203
Main Authors: Setúbal, S. S., Pontes, A. S., Furtado, J. L., Xavier, C. V., Silva, F. L., Kayano, A. M., Izidoro, L. F. M., Soares, A. M., Calderon, L. A., Stábeli, R. G., Zuliani, J. P.
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Language:English
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Summary:The in vitro effects of BaltTX-I, a catalytically inactive Lys49 variant of phospholipase A 2 (PLA 2 ), and BaltTX-II, an Asp49 catalytically active PLA 2 isolated from Bothrops alternatus snake venom, on thioglycollate-elicited macrophages (TG-macrophages) were investigated. At non-cytotoxic concentrations, the secretory PLA 2 BaltTX-I but not BaltTX-II stimulated complement receptor-mediated phagocytosis. Pharmacological treatment of TG-macrophages with staurosporine, a protein kinase C (PKC) inhibitor, showed that this kinase is involved in the increase of serum-opsonized zymosan phagocytosis induced by BaltTX-I but not BaltTX-II secretory PLA 2 , suggesting that PKC may be involved in the stimulatory effect of this toxin in serum-opsonized zymosan phagocytosis. Moreover, BaltTX-I and -II induced superoxide production by TG-macrophages. This superoxide production stimulated by both PLA 2 s was abolished after treatment of cells with staurosporine, indicating that PKC is an important signaling pathway for the production of this radical. Our experiments showed that, at non-cytotoxic concentrations, BaltTX-I may upregulate phagocytosis via complement receptors, and that both toxins upregulated the respiratory burst in TG-macrophages.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297913020089