Effect of glucocorticoids on the turnover rate of actin and myosin heavy and light chains on different types of skeletal muscle fibres.
The catabolic action of glucocorticoids on the molecular level of the two main muscular proteins, myosin and actin, was found to depend on the type of muscle fibres. The synthesis rate of actin and myosin heavy chain was decreased in all types of muscle fibres, and in myosin light chain only in the slow-twitch red fibres. The turnover rate of actin and myosin heavy chain was also found decreased in all types of muscle fibres. The myosin light chains turned over more rapidly in dexamethasone-treated than in the control rats in all types of muscle fibres except in the case of the slow-twitch red ones as was shown by single and double isotope methods. Dexamethasone treatment enhanced the urinary 3-methylhistidine excretion in rats by 60%.
D000199:Actins / Q000378:metabolism*; D000205:Actomyosin / Q000378:metabolism; D000818:Animals; D003907:Dexamethasone / Q000494:pharmacology; D005938:Glucocorticoids / Q000494:pharmacology*; D007930:Leucine / Q000378:metabolism; D008297:Male; D008762:Methylhistidines / Q000652:urine; D009132:Muscles / Q000187:drug effects / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012519:Sarcoplasmic Reticulum / Q000378:metabolism
D000199:Actins; D005938:Glucocorticoids; D008762:Methylhistidines; D003907:Dexamethasone; D000205:Actomyosin; D009218:Myosins; D007930:Leucine; C028118:3-methylhistidine