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as a Downstream Effector of
Phosphatidylinositol 3-Kinase during Insulin Stimulation in Rat
Adipocytes
(Received for publication, July 24, 1997, and in revised form, September 8, 1997)
and
From the J. A. Haley Veterans' Hospital Research Service and
Departments of Internal Medicine and Biochemistry/Molecular Biology,
University of South Florida College of Medicine, Tampa, Florida 33612 and Insulin provoked rapid increases in enzyme
activity of immunoprecipitable protein kinase C-
Centro de Biologia Molecular "Servero Ochoa,"
Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain
(PKC-) in rat
adipocytes. Concomitantly, insulin provoked increases in
32P labeling of PKC- both in intact adipocytes and
during in vitro assay of immunoprecipitated PKC-; the
latter probably reflected autophosphorylation, as it was inhibited by
the PKC- pseudosubstrate. Insulin-induced activation of
immunoprecipitable PKC- was inhibited by LY294002 and wortmannin;
this suggested dependence upon phosphatidylinositol (PI) 3-kinase.
Accordingly, activation of PI 3-kinase by a
pYXXM-containing peptide in vitro resulted in a
wortmannin-inhibitable increase in immunoprecipitable PKC- enzyme
activity. Also, PI-3,4-(PO4)2, PI-3,4,5-(PO4)3, and
PI-4,5-(PO4)2 directly stimulated enzyme activity and autophosphoralytion in control PKC- immunoprecipitates to levels observed in insulin-treated PKC- immunoprecipitates. In
studies of glucose transport, inhibition of immunoprecipitated PKC-
enzyme activity in vitro by both the PKC-
pseudosubstrate and RO 31-8220 correlated well with inhibition of
insulin-stimulated glucose transport in intact adipocytes. Also, in
adipocytes transiently expressing hemagglutinin antigen-tagged GLUT4,
co-transfection of wild-type or constitutive PKC- stimulated
hemagglutinin antigen-GLUT4 translocation, whereas dominant-negative
PKC- partially inhibited it. Our findings suggest that insulin
activates PKC- through PI 3-kinase, and PKC- may act as a
downstream effector of PI 3-kinase and contribute to the activation of
GLUT4 translocation.
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