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BAPTA induces a decrease of intracellular free calcium and a translocation and inactivation of protein kinase C in macrophages.

Abstract

Addition of BAPTA/AM to liver macrophages lowered the level of [Ca2+]i and induced a translocation and inactivation of protein kinase C. The phorbol ester- and zymosan-induced release of arachidonic acid, prostaglandin E2 and superoxide, the formation of inositol phosphates upon addition of zymosan and the lipopolysaccharide-induced synthesis of TNF-alpha was inhibited by pretreatment of the cells with BAPTA/AM. Simultaneous addition of A23187 to elevate [Ca]i could not reverse the inhibitory effect of BAPTA. Phagocytosis of zymosan and formation of prostaglandin E2 from exogenously added arachidonic acid or upon addition of A 2187 was not altered by BAPTA/AM. No protein kinase C activity could be measured in homogenates obtained from BAPTA/AM-pretreated cells. These results indicate that the action of BAPTA in eucaryotic cells is not limited to its chelating effect on calcium but that BAPTA leads to a translocation and inactivation of protein kinase C.

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BibTeXRIS

P Dieter, E Fitzke, J Duyster. 1993. BAPTA induces a decrease of intracellular free calcium and a translocation and inactivation of protein kinase C in macrophages.. https://doi.org/10.1515/bchm3.1993.374.1-6.171

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