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Department of Zoology, Brigham Young University, Provo, Utah 84602
AMP-activated protein
kinase (AMPK) is activated during muscle contraction in response
to the increase in AMP and decrease in phosphocreatine (PCr).
Once activated, AMPK has been proposed to phosphorylate a number of
targets, resulting in increases in glucose transport, fatty acid
oxidation, and gene transcription. Although it has been possible to
directly observe phosphorylation of one of these targets, acetyl-CoA
carboxylase (ACC) in vitro, it has been more difficult to obtain direct
evidence of ACC phosphorylation in contracting skeletal muscle. In
these experiments using a phosphoserine antibody to ACC and a
phosphothreonine antibody to AMPK, evidence was obtained for
phosphorylation and activation of ACC in vitro, in gastrocnemius muscle
electrically stimulated at different frequencies, and in muscle from
rats running on the treadmill. Significant negative linear correlations
between phospho-ACC and ACC activity were observed in all models
(P < 0.01). The decline in ACC activity was related to
the decrease in PCr and the rise in AMP. A relationship between
phospho-AMPK (threonine 172) and activity of AMPK immunoprecipitated with anti-
2 subunit antibody preparation was also
observed. These data provide the first evidence of a direct link
between extent of phosphorylation of these proteins at sites recognized
by the antibodies and activity of the enzymes in electrically
stimulated muscle and in muscle of rats running on the treadmill.
creatine; fatty acid oxidation; malonyl-CoA; palmitoyl-carnitine transferase; phosphocreatine; AMP-activated protein kinase
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