Activation of AMPK is essential for AICAR-induced glucose uptake by skeletal muscle but not adipocytes

Hideyuki Sakoda, Takehide Ogihara, Motonobu Anai, Midori Fujishiro, Hiraku Ono, Yukiko Onishi, Hideki Katagiri, Miho Abe, Yasushi Fukushima, Nobuhiro Shojima, Kouichi Inukai, Masatoshi Kikuchi, Yoshitomo Oka, Tomoichiro Asano

Research output: Contribution to journalArticlepeer-review

75 Citations (Scopus)

Abstract

5-Aminoimidazole-4-carboxamide 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 AMPKα2 subunit by use of adenovirus-mediated gene transfer. Overexpression of the dominant negative mutant had no effect on AICAR-induced glucose transport in adipocytes, although AMPK activation was almost completely abolished. This suggests that AICAR-induced glucose uptake by 3T3-L1 adipocytes is independent of AMPK activation. By contrast, overexpression of the dominant negative AMPKα2 mutant in muscle markedly suppressed both AICAR-induced glucose uptake and AMPK activation, although insulin-induced uptake was unaffected. Overexpression of the wild-type AMPKα2 subunit significantly increased AMPK activity in muscle but did not enhance glucose uptake. Thus, although AMPK activation may not, by itself, be sufficient to increase glucose transport, it appears essential for AICAR-induced glucose uptake in muscle.

Original languageEnglish
Pages (from-to)E1239-E1244
JournalAmerican Journal of Physiology - Endocrinology and Metabolism
Volume282
Issue number6 45-6
DOIs
Publication statusPublished - 2002

Keywords

  • 5-aminoimidazole-4-carboxamide ribonucleoside
  • AMP-activated protein kinase
  • Exercise

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Physiology
  • Physiology (medical)

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