Journal
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
Volume 292, Issue 1, Pages C564-C572Publisher
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpcell.00269.2006
Keywords
compound C; AMPK; insulin sensitivity; Akt; mTOR
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Funding
- NIDDK NIH HHS [K01 DK066330, K01 DK 066330] Funding Source: Medline
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [K01DK066330] Funding Source: NIH RePORTER
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Data from the use of activators and inhibitors of the AMP-activated protein kinase (AMPK) suggest that AMPK increases sensitivity of glucose transport to stimulation by insulin in muscle cells. We assayed insulin action after adenoviral (Ad) transduction of constitutively active (CA; a truncated form of AMPK alpha(1)) and dominant-negative (DN; which depletes endogenous AMPK alpha) forms of AMPK alpha (Ad-AMPK alpha-CA and Ad-AMPK alpha-DN, respectively) into C(2)C(12) myotubes. Compared with control (Ad-green fluorescent protein), Ad-AMPK-CA increased the ability of insulin to stimulate glucose transport. The increased insulin action in cells expressing AMPK-CA was suppressed by compound C (an AMPK inhibitor). Exposure of cells to 5-aminoimidazole-4-carboxamide-1 beta-D-ribofuranoside (an AMPK activator) increased insulin action in uninfected myotubes and myotubes transduced with green fluorescent protein but not in Ad-AMPK-DN-infected myotubes. In Ad-AMPK-CA-transduced cells, serine phosphorylation of insulin receptor substrate 1 was decreased at a mammalian target of rapamycin (or p70 S6 kinase) target site that has been reported to be associated with insulin resistance. These data suggest that, in myotubes, activated AMPK alpha(1) is sufficient to increase insulin action and that the presence of functional AMPK alpha is required for 5-aminoimidazole-4-carboxamide-1 beta, D-ribofuranoside-related increases in insulin action.
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