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Diacylglycerol stimulates phospholipase A 2 from Swiss 3T3 fibroblasts
Author(s) -
Burch Ronald M.
Publication year - 1988
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(88)80099-1
Subject(s) - diacylglycerol kinase , phospholipase , phosphoinositide phospholipase c , phospholipase c , phospholipase d , protein kinase c , chemistry , prostaglandin , gq alpha subunit , diacylglycerol lipase , phospholipase a2 , biochemistry , diglyceride , enzyme , g protein , signal transduction
We recently demonstrated that diacylglycerol induced arachidonate release and prostaglandin E 2 synthesis in 3T3 fibroblasts, and greatly augmented prostaglandin E 2 synthesis in response to submaximal and maximal concentrations of bradykinin. We have now partially purified a phospholipase A 2 from the cells. When phosphatidyl[ 3 H]choline was used as substrate, several diacylglycerols augmented phospholipase A 2 activity. Diacylglycerol was effective at concentrations as low as 30 nM. Protein kinase C inhibition did not affect diacylglycerol's stimulation of phospholipase A 2 . Diacylglycerol did not alter the calcium requirement for phospholipase A 2 or its pH optimum. The present study demonstrates that the effect of diacylglycerol to augment arachidonate metabolism is at the level of phospholipase A 2 , itself.