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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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Published in: | Biochemistry (Moscow) 2013-02, Vol.78 (2), p.194-203 |
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Main Authors: | , , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0006-2979 1608-3040 |
DOI: | 10.1134/S0006297913020089 |