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Activation of phospholipase C-gamma by the concerted action of tau proteins and arachidonic acid.

Authors
Hwang, SC; Jhon, DY; Bae, YS; Kim, JH; Rhee, SG
Citation
The Journal of biological chemistry, 271(31):18342-18349, 1996
Journal Title
The Journal of biological chemistry
ISSN
0021-92581083-351X
Abstract
Phospholipase C-gamma (PLC-gamma) isozymes are thought to be activated by receptor-induced tyrosine phosphorylation. Proteins that activate PLC-gamma1 have now been purified from bovine brain and identified as members of the tau family of microtubule-associated proteins. Activation of PLC-gamma by tau was enhanced in the presence of unsaturated fatty acids such as arachidonic acid, saturated fatty acids being ineffective. Maximal (15-20-fold) activation was apparent in the presence of 0.15 microM tau and 25 microM arachidonic acid (AA). The effect of tau and AA was specific to PLC-gamma isozymes in the presence of submicromolar concentrations of Ca2+ and was markedly inhibited by phosphatidylcholine. These results suggest that in cells that express tau, receptors coupled to cytosolic phospholipase A2 may activate PLC-gamma isozymes indirectly in the absence of tyrosine phosphorylation through the hydrolysis of phosphatidylcholine to generate AA.
MeSH terms
Amino Acid SequenceAnimalsArachidonic Acid/metabolism/*pharmacologyBrain/metabolismCattleCytosol/metabolismEnzyme Activation/drug effectsHumansHydrolysisIsoenzymes/*metabolismKineticsMolecular Sequence DataPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol Phosphates/metabolismPhosphatidylinositols/metabolismPhospholipase C gammaPhospholipases A/metabolismPhospholipases A2PhosphorylationSubstrate SpecificityType C Phospholipases/*metabolismTyrosine/metabolismtau Proteins/genetics/metabolism/*pharmacology
PMID
8702475
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Medical Science
AJOU Authors
황, 성철
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