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Articles in PresS, published online ahead of print February 19, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00455.2001
Submitted on October 11, 2001
Accepted on February 12, 2002
1 Metabolism and Endocrinology, Institute for Adult Disease, Asahi Life Foundation, Tokyo, Japan
2 Department of Internal Medicine, Graduate School of Medicine, University of Tokyo, Tokyo, Japan
3 Department of Internal Medicine, University of Tohoku, Sendai, Japan
4 Fourth Department of Internal Medicine, Saitama Medical School, Moroyama, Japan
* To whom correspondence should be addressed. E-mail: asano-tky{at}umin.ac.jp.
5-aminoimidazole-4-carboxyamide ribonucleoside (AICAR) reportedly activates AMP-activated protein kinase (AMPK) and stimulates glucose uptake by skeletal muscle cells. In this study, we investigated the role of AMPK in AICAR-induced glucose uptake by 3T3-L1 adipocytes and rat soleus muscle cells by overexpressing wild type and dominant negative forms of the AMPK 
2 subunit using adenovirus-mediated gene transfer. Overexpression of the dominant-negative mutant had no effect on AICAR-induced glucose transport in adipocytes, though AMPK activation was almost completely abolished. This suggests AICAR-induced glucose uptake by 3T3-L1 adipocytes is independent of AMPK activation. By contrast, overexpression of the dominant-negative AMPK 2 mutant in muscle markedly suppressed both AICAR-induced glucose uptake and AMPK activation, though insulin-induced uptake was unaffected. Overexpression of the wild-type AMPK 2 subunit significantly increased AMPK activity in muscle, but did not enhance glucose uptake. Thus, while AMPK activation may not, by itself, be sufficient to increase glucose transport, it appears essential for AICAR-induced glucose uptake in muscle.
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