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Diabetes 51:2412-2419, 2002
© 2002 by the American Diabetes Association, Inc.

Potentiation of Insulin Signaling in Tissues of Zucker Obese Rats After Acute and Long-Term Treatment With PPAR{gamma} Agonists

Guoqiang Jiang1, Qing Dallas-Yang1, Zhihua Li1, Deborah Szalkowski1, Franklin Liu1, Xiaolan Shen2, Margaret Wu1, Gaochao Zhou1, Thomas Doebber1, Joel Berger1, David E. Moller1, and Bei B. Zhang1

1 Department of Molecular Endocrinology-Diabetes, Merck Research Laboratories, Rahway, New Jersey
2 Department of Comparative Medicine, Merck Research Laboratories, Rahway, New Jersey

Thiazolidinediones (TZDs), agonists of peroxisome proliferator-activated receptor-{gamma} (PPAR{gamma}), improve insulin sensitivity in vivo, and the mechanism remains largely unknown. In this study, we showed that, in Zucker obese (fa/fa) rats, acute (1-day) treatment with both rosiglitazone (a TZD) and a non-TZD PPAR{gamma} agonist (nTZD) reduced plasma free fatty acid and insulin levels and, concomitantly, potentiated insulin-stimulated Akt phosphorylation at threonine 308 (Akt-pT308) in adipose and muscle tissues. A similar effect on Akt was observed in liver after a 7-day treatment. The increase in Akt-pT308 was correlated with an increase in Akt phosphorylation at serine 473 (Akt-pS473), tyrosine phosphorylation of insulin receptor ß subunit and insulin receptor substrate-1, and serine phosphorylation of glycogen synthase kinase-3{alpha}/ß. The agonists appeared to potentiate Akt1 phosphorylation in muscle and liver and both Akt1 and Akt2 in adipose. Finally, potentiation of insulin signaling was also observed in isolated adipose tissue ex vivo and differentiated 3T3 L1 adipocytes in vitro, but not in rat primary hepatocytes in vitro. These results suggest that 1) PPAR{gamma} agonists acutely potentiate insulin signaling in adipose and muscle tissues and such regulation may be physiologically relevant to insulin sensitization in vivo; 2) the agonists directly target adipose tissues; and 3) the metabolic and signaling effects of the agonists are mediated by structurally distinct PPAR{gamma} agonists.


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