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Relationship between intracellular pH changes, activation of protein kinase C and NADPH oxidase in macrophages
Author(s) -
Dieter Peter
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80012-6
Subject(s) - superoxide , nadph oxidase , protein kinase c , ionomycin , chemistry , intracellular , staurosporine , zymosan , antiporter , biochemistry , respiratory burst , intracellular ph , protein kinase a , amiloride , reactive oxygen species , microbiology and biotechnology , biology , kinase , sodium , enzyme , organic chemistry , membrane , in vitro
Activation of the superoxide‐generating NADPH oxidase by phorbol ester or zymosan induced a cytoplasmic acidification when liver macrophages were incubated in sodium free media or in the presence of amiloride. Staurosporine or desensitization of protein kinase C inhibited phorbol ester‐and zymosan‐induced pH changes and generation of superoxide. The intracellular pH remained unchanged in cells incubated in physiological sodium media. Ionomycin and arachidonic acid did not induce a change in intracellular pH or a generation of superoxide. Fluoride, which has been shown to induce a translocation of protein kinase C in these cells, did not elicit superoxide generation but induced a decrease in intracellular pH. These experiments support (1) a role of the Na + /H + antiporter in macrophages as a metabolic regulator of intracellular pH upon stimulation of the superoxide‐generating NADPH oxidase, and (2) suggest an involvement of protein kinase C in this process.