Protein kinase C involved in zymosan-induced release of arachidonic acid and superoxide but not in calcium ionophore-elicited arachidonic acid release or formation of prostaglandin E2 from added arachidonate
✍ Scribed by Justus Duyster; Agnes Schulze-Specking; Edith Fitzke; Dr. Peter Dieter
- Publisher
- John Wiley and Sons
- Year
- 1992
- Tongue
- English
- Weight
- 719 KB
- Volume
- 48
- Category
- Article
- ISSN
- 0730-2312
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✦ Synopsis
Abstract
Zymosan and phorbol ester induced in liver macrophages the release of arachidonic acid, prostaglandin E~2~, and superoxide; the calcium ionophore A 23187 elicited a release of arachidonic acid and prostaglandin E~2~ but not of superoxide, and exogenously added arachidonic acid led to the formation of prostaglandin E~2~ only. The zymosan‐ and phorbol‐ester‐induced release of arachidonic acid, prostaglandin E~2~, and superoxide was dose‐dependently inhibited by staurosporine and K252a, two inhibitors of protein kinase C, and by pretreatment of the cells with phorbol ester which desensitized protein kinase C. The release of arachidonic acid or prostaglandin E~2~ following the addition of A 23187 or arachidonic acid was not affected by these treatments. Zymosan and phorbol ester but not A 23187 or arachidonic acid induced a translocation of protein kinase C from the cytosol to membranes in intact cells. These results demonstrate an involvement of protein kinase C in the zymosan‐ and phorbol‐ester‐induced release of arachidonic acid, prostaglandin E~2~, and superoxide; the release of arachidonic acid and prostaglandin E~2~ elicited by A 23187 and the formation of prostaglandin E~2~ from exogenously added arachidonic acid, however, is independent of an activation of protein kinase C.