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1 Department of Physiology and Developmental Biology, Brigham Young University, Provo, Utah 84602; and 2 Division of Molecular Physiology, Dundee University, Wellcome Trust Biocentre, Dundee DD1 5EH, Scotland, United Kingdom
AMP-activated protein kinase
(AMPK) consists of three subunits:
,
, and
. Two isoforms
exist for the
-subunit (
1 and
2), two
for the
-subunit (
1 and
2), and three
for the
-subunit (
1,
2, and
3). Although the specific roles of the
- and
-subunits are not well understood, the
-subunit isoforms contain
the catalytic site and also the phosphorylation/activation site for the
upstream kinase. This study was designed to determine the role of
thyroid hormones in controlling expression levels of these AMPK
subunits and of one downstream target, acetyl-CoA carboxylase (ACC), in muscle. AMPK subunit and ACC levels were determined by Western blots in
control rats, in rats given 0.01% propylthiouracil (PTU) in drinking
water for 3 wk, and in rats given 3 mg of thyroxine and 1 mg of
triiodothyronine per kilogram chow for 1 or 3 wk. In gastrocnemius
muscle, all isoforms of AMPK subunits were significantly increased in
rats given thyroid hormones for 3 wk vs. those treated with PTU.
Similar patterns were seen in individual muscle types. Expression of
muscle ACC was also significantly increased in response to 3 wk of
treatment with excess thyroid hormones. Muscle content of malonyl-CoA
was elevated in PTU-treated rats and depressed in thyroid
hormone-treated rats. These data provide evidence that skeletal muscle
AMPK subunit and ACC expression is partially under the control of
thyroid hormones.
malonyl-CoA; propylthiouracil; thyroxine; triiodothyronine
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