Action of two phospholipases A(2) purified from Bothrops alternatus snake venom on macrophages

作者：Setubal 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; Stabeli R G; Zuliani J P^*

来源：Biochemistry-Moscow, 2013, 78(2): 194-203.

DOI：10.1134/S0006297913020089

• snake venom PLA(2)
• macrophages
• phagocytosis
• PKC
• superoxide
• inflammation

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.

• 出版日期2013-2