Long-term regulation of AMP-activated protein kinase and acetyl-CoA carboxylase in skeletal muscle
| Autor: | Eric B. Taylor, B.E. Paxton, D. G. Hardie, S. H. Park, D.S. Rubink, Lyle J. Greenwood, William W. Winder, Kirsty J. Mustard |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Thyroid Hormones
endocrine system medicine.medical_specialty Time Factors endocrine system diseases Protein subunit Blotting Western AMP-Activated Protein Kinases Protein Serine-Threonine Kinases Biology Biochemistry Gene Expression Regulation Enzymologic AMP-activated protein kinase Multienzyme Complexes Internal medicine medicine Animals Protein Isoforms Muscle Skeletal Protein kinase A Beta oxidation Acetyl-CoA carboxylase Skeletal muscle AMPK Rats Endocrinology medicine.anatomical_structure Liver biology.protein Propylthiouracil Acetyl-CoA Carboxylase medicine.drug |
| Zdroj: | Biochemical Society Transactions. 31:182-185 |
| ISSN: | 1470-8752 0300-5127 |
| DOI: | 10.1042/bst0310182 |
| Popis: | 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 γ3 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: | OpenAIRE |
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