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J. Biol. Chem., Vol. 275, Issue 22, 16690-16696, June 2, 2000
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From the J. A. Haley Veterans Hospital Research Service and
Department of Internal Medicine, University of South Florida
College of Medicine Tampa, FL 33612
We evaluated effects of the thiazolidinedione,
rosiglitazone, on insulin-induced activation of protein kinase C
(PKC)-
Thiazolidinedione Treatment Enhances Insulin Effects on Protein
Kinase C-
/
Activation and Glucose Transport in Adipocytes of
Nondiabetic and Goto-Kakizaki Type II Diabetic Rats*
/
and glucose transport in adipocytes of Goto-Kakizaki
(GK)-diabetic and nondiabetic rats. Insulin effects on PKC-/ and
2-deoxyglucose uptake were diminished by approximately 50% in GK
adipocytes, as compared with control adipocytes. This defect in
insulin-induced PKC-/ activation was associated with
diminished activation of IRS-1-dependent
phosphatidylinositol (PI) 3-kinase, and was accompanied by diminished
phosphorylation of threonine 410 in the activation loop of PKC-; in
contrast, protein kinase B (PKB) activation and phosphorylation were
not significantly altered. Rosiglitazone completely reversed defects in
insulin-stimulated 2-deoxyglucose uptake, PKC/ enzyme activity
and PKC- threonine 410 phosphorylation, but had no effect on PI
3-kinase activation or PKB activation/phosphorylation in GK adipocytes.
Similarly, in adipocytes of nondiabetic rats, rosiglitazone provoked
increases in insulin-stimulated 2-deoxyglucose uptake, PKC-/
enzyme activity and phosphorylation of both threonine 410 activation
loop and threonine 560 autophosphorylation sites in PKC-, but had no
effect on PI 3-kinase activation or PKB activation/phosphorylation. Our
findings suggest that (a) decreased effects of insulin on glucose transport in adipocytes of GK-diabetic rats are due at least in
part to diminished phosphorylation/activation of PKC-/, and
(b) thiazolidinediones enhance glucose transport responses to insulin in adipocytes of both diabetic and nondiabetic rats through
increases in phosphorylation/activation of PKC-/.
*
This work was supported by funds from the Department of
Veterans Affairs Merit Review Program and National Institutes of Health Research Grant 2R01DK38079-09A1.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Research Service (VAR
151), J. A. Haley Veterans Hospital, 13000 Bruce B. Downs Blvd.,
Tampa, FL 33612. Tel.: 813-972-7662; Fax: 813-972-7623; E-mail:
rfarese@com1.med.usf.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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