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Am J Physiol Endocrinol Metab 283: E338-E345, 2002. First published March 12, 2002; doi:10.1152/ajpendo.00457.2001
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Vol. 283, Issue 2, E338-E345, August 2002

Role of PKC isoforms in glucose transport in 3T3-L1 adipocytes: insignificance of atypical PKC

Masatoshi Tsuru1, Hideki Katagiri2, Tomoichiro Asano3, Tetsuya Yamada1,2, Shigeo Ohno4, Takehide Ogihara3, and Yoshitomo Oka1,2

1 Third Department of Internal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi 755-8505; 2 Division of Molecular Metabolism and Diabetes, Department of Internal Medicine, Tohoku University Graduate School of Medicine, Sendai 980-8574; 3 Faculty of Medicine, Department of Internal Medicine, University of Tokyo, Tokyo 113-8566; and 4 Department of Molecular Biology, Yokohama City University School of Medicine 3 - 9, Yokohama 236, Japan

To elucidate the involvement of protein kinase C (PKC) isoforms in insulin-induced and phorbol ester-induced glucose transport, we expressed several PKC isoforms, conventional PKC-alpha , novel PKC-delta , and atypical PKC isoforms of PKC-lambda and PKC-zeta , and their mutants in 3T3-L1 adipocytes using an adenovirus-mediated gene transduction system. Endogenous expression and the activities of PKC-alpha and PKC-lambda /zeta , but not of PKC-delta , were detected in 3T3-L1 adipocytes. Overexpression of each wild-type PKC isoform induced a large amount of PKC activity in 3T3-L1 adipocytes. Phorbol 12-myristrate 13-acetate (PMA) activated PKC-alpha and exogenous PKC-delta but not atypical PKC-lambda /zeta . Insulin also activated the overexpressed PKC-delta but not PKC-alpha . Expression of the wild-type PKC-alpha or PKC-delta resulted in significant increases in glucose transport activity in the basal and PMA-stimulated states. Dominant-negative PKC-alpha expression, which inhibited the PMA activation of PKC-alpha , decreased in PMA-stimulated glucose transport. Glucose transport activity in the insulin-stimulated state was increased by the expression of PKC-delta but not of PKC-alpha . These findings demonstrate that both conventional and novel PKC isoforms are involved in PMA-stimulated glucose transport and that other novel PKC isoforms could participate in PMA-stimulated and insulin-stimulated glucose transport. Atypical PKC-lambda /zeta was not significantly activated by insulin, and expression of the wild-type, constitutively active, and dominant-negative mutants of atypical PKC did not affect either basal or insulin-stimulated glucose transport. Thus atypical PKC enzymes do not play a major role in insulin-stimulated glucose transport in 3T3-L1 adipocytes.

protein kinase C; glucose transport; insulin; phorbol 12-myristate 13-acetate


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