In their physiological concentrations, thyroid hormones stimulate the synthesis as well as the degradation of proteins, whereas in supraphysiological doses protein catabolism predominates. In hyperthyroidism skeletal muscle protein stores suffer depletion which is reflected by an increased urinary N- and methylhistidine -excretion. Due to the enhanced skeletal muscle amino acid release, the plasma concentration of glucoplastic amino acids are often enhanced, contributing by means of an elevated substrate supply to the increased hepatic gluconeogenesis. Thyroid hormone excess induces cardiac hypertrophy which is in direct contrast to the hypotroph skeletal muscle in hyperthyroid patients. Thyroid hormones stimulate a series of intracellular and secretory proteins in the liver, although in hyperthyroid liver alcohol dehydrogenase and the enzymes of histidine and tryptophan metabolism show reduced activities. The stimulatory effect is due to thyroid hormone-induced increase in the protein synthesis at a pretranslational level and is supported experimentally for malic enzyme, alpha 2u-globulin and albumin by the measurement of their specific messenger RNA activities. Thyroid hormone action at the cellular level is reflected by a generalized increase in total cellular RNA with a selective increase or decrease in a small population of specific mRNA. The activities of protein catabolizing lysosomal enzymes are stimulated by thyroid hormones; up to now effects of T3 on the degradation of specific enzymes have not been reported. Serum total protein concentration is slightly reduced or even unchanged in hyperthyroidism. The thyroid hormone-induced increase in the turnover of total body protein is part of the hypermetabolism observed in hyperthyroidism.