Long-term regulation of AMP-activated protein kinase and acetyl-CoA carboxylase in skeletal muscle.

Autor: Winder WW; Department of Physiology and Developmental Biology, 545 WIDB, Brigham Young University, Provo, UT 84602, USA. William_winder@byu.edu, Hardie DG, Mustard KJ, Greenwood LJ, Paxton BE, Park SH, Rubink DS, Taylor EB
Jazyk: angličtina
Zdroj: Biochemical Society transactions [Biochem Soc Trans] 2003 Feb; Vol. 31 (Pt 1), pp. 182-5.
DOI: 10.1042/bst0310182
Abstrakt: Evidence is accumulating for roles of AMP-activated protein kinase (AMPK) in controlling glucose uptake, fatty acid oxidation and gene expression in skeletal muscle. Relatively little is known, however, about the control of expression of the AMPK subunit isoforms. Marked differences are noted in subunit expression as a function of muscle fibre type. Expression of the gamma3 subunit isoform increases in fast-twitch red fibres of the rat in response to training. All subunit isoforms are expressed to a lesser extent in rats treated with propylthiouracil (PTU; an inhibitor of thyroid hormone synthesis) for 3 weeks compared with rats given excess thyroid hormones for 3 weeks. An approx. 2-fold increase in acetyl-CoA carboxylase was observed in gastrocnemius of hyperthyroid rats compared with experimentally hypothyroid rats. Thyroid state therefore appears to be one important factor controlling expression of these proteins in skeletal muscle.
Databáze: MEDLINE