PMID: 2491791Jan 17, 1989Paper

A role for protein kinase C-mediated phosphorylation in the mobilization of arachidonic acid in mouse macrophages

Biochimica Et Biophysica Acta
J Wijkander, R Sundler

Abstract

Mouse peritoneal macrophages respond to activators of protein kinase C and to zymosan particles and calcium ionophore by rapid enhancement of a phospholipase A pathway and mobilization of arachidonic acid. The pattern of protein phosphorylation induced in these cells by 4 beta-phorbol 12-myristate 13-acetate (PMA), 1,2-dioctanoyl-sn-glycerol, exogenous phospholipase C and by zymosan and ionophore A23187 was found to be virtually identical. The time course of phosphorylation differed among the phosphoprotein bands and in only some of those identified (i.e., those of 45 and 65 kDa) was the phosphorylation sufficiently rapid to be involved in the activation of the phospholipase A pathway. Phosphorylation of lipocortin I or II could not be detected. Down-regulation of kinase C by a 24-h pretreatment with PMA resulted in extensive inhibition of both protein phosphorylation and the mobilization of arachidonic acid in response to PMA or dioctanoylglycerol. The phosphorylation of the 45 kDa protein in response to zymosan and A23187 was also inhibited by pretreatment with PMA, while only arachidonic acid release induced by zymosan was inhibited by this pretreatment. Depletion of intracellular calcium had little effect on kinase C-depend...Continue Reading

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Citations

Sep 11, 1990·European Journal of Biochemistry·K Decker
Apr 1, 1993·European Journal of Biochemistry·M MachidaT Tanaka
Nov 14, 1994·Annals of the New York Academy of Sciences·W YoungS Constantini
Jan 1, 1993·The Journal of Pharmacy and Pharmacology·E Beubler, A Schirgi-Degen
Nov 1, 1989·Biochemical Pharmacology·F F Davidson, E A Dennis
Jan 3, 1994·Biochimica Et Biophysica Acta·J BalsindeJ A Solís-Herruzo
Jun 16, 2001·American Journal of Physiology. Renal Physiology·L R JamesJ W Scholey

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