Premium
Distinct phospholipase C‐regulated signalling pathways in Swiss 3T3 fibroblasts induce the rapid generation of the same polyunsaturated diacylglycerols
Author(s) -
Pettitt Trevor R,
Wakelam Michael J.O
Publication year - 1998
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/s0014-5793(98)00471-2
Subject(s) - diacylglycerol kinase , protein kinase c , phosphatidate , phospholipase a2 , arachidonic acid , activator (genetics) , phospholipase c , biochemistry , phospholipase d , diglyceride , polyunsaturated fatty acid , phosphatidic acid , phospholipase , chemistry , prostaglandin , biology , signal transduction , enzyme , phospholipid , fatty acid , receptor , membrane
Prostaglandin F 2α , platelet‐derived growth factor (PDGF) and calcium ionophore A23187 stimulated the rapid (within 25 s) generation of polyunsaturated 1,2‐diacylglycerol (DAG) species, in particular 18:0/20:3n‐9, 18:0/20:4n‐6 and 18:0/20:5n‐3, in Swiss 3T3 fibroblasts. This was followed by a second sustained phase characterised by saturated, monounsaturated and diunsaturated DAG species derived, at least partially, from a phospholipase D/phosphatidate phosphohydrolase‐linked pathway. This could be directly activated by phorbol ester. Assay of rat brain protein kinase C (PKC) in lipid vesicles showed that first phase, polyunsaturated‐enriched DAG isolated from Swiss 3T3 cells was a more potent activator of kinase activity compared to that achieved with DAG from control or 5 min stimulated cells. Thus activation of distinct members of the phospholipase C family leads to the rapid and almost identical generation of polyunsaturated DAG species which are capable of preferentially activating protein kinase C (PKC).