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(Received for publication, April 2, 1996, and in revised form, May 7, 1996)
From the Laboratory of Cell Signaling, NHLBI, National Institutes
of Health, Bethesda, Maryland 20892
Phospholipase C-
Volume 271, Number 31,
Issue of August 2, 1996
pp. 18342-18349
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
by the Concerted Action of Tau
Proteins and Arachidonic Acid
(PLC-) isozymes are
thought to be activated by receptor-induced tyrosine phosphorylation.
Proteins that activate PLC-1 have now been purified from bovine
brain and identified as members of the tau family of
microtubule-associated proteins. Activation of PLC- 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 µM tau
and 25 µM arachidonic acid (AA). The effect of tau and AA
was specific to PLC- 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- isozymes indirectly in the absence of tyrosine
phosphorylation through the hydrolysis of phosphatidylcholine to
generate AA.
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