Abstract
In the present work we have studied the disappearance of the mitochondrial enzyme alpha-glycerophosphate dehydrogenase (αGPD) after thyroidectomy, as well as the induction by the continuous infusion of physiological doses of thyroxine to hypothyroid male rats in three different tissues, the liver, kidney and heart. Rats were previously rendered hypothyroid by surgical thyroidectomy and enzyme activity was determined at different time intervals following the ablation of the gland. Levels of αGPD are specifically regulated in each tissue, as both its rate of disappearance after thyroidectomy and the rate of appearance during T4 treatment are different in the liver, the kidney and the heart. Such results suggest the existence of local factors which can modify the response generated by the thyroid hormone in individual tissues.
Similar content being viewed by others
References
Lee Y.P., Takemori A.E., Lardy H. Enhanced oxidation of α-glycerophosphate by mitochondria of thyroid-fed rats. J. Biol. Chem. 234: 3041, 1959.
Lee Y.P., Lardy H. Influence of thyroid hormones on L-α-glycerophosphate dehydrogenases and other dehydrogenases in various organs of the rat. J. Biol. Chem. 240: 1427, 1965.
Oppenheimer J.H., Silva J.E., Schwartz H.L., Surk M.I. Stimulation of hepatic mitochondrial α-glycerophosphate dehydrogenase and malic enzyme by L-triiodothyronine. J. Clin. Invest. 59: 517, 1977.
Wilson E.J., McMurray W.C. Regulation of malic enzyme and mitochondrial α-glycerophosphate dehydrogenase by thyroid hormones, insulin and glucocorticoids in cultured hepatocytes. J. Biol. Chem. 256: 11657, 1981.
Tarentino A.L., Richert D.A., Westerfeld W.W. The current induction of hepatic α-glycerophosphate dehydrogenase and malate dehydrogenase by thyroid hormone. Biochim. Biophys. Acta 124: 295, 1966.
Sellinger O.Z., Lee K.L. The induction of mitochondrial α-glycerophosphate dehydrogenase by thyroid hormone: evidence for enzyme synthesis. Biochim. Biophys. Acta 91: 183, 1964.
Larsen R.P., Frumess R.D. Comparison of the biological effects of thyroxine and triiodothyronine in the rat. Endocrinology 100: 980, 1977.
Obregon M.J., Pascual A., Morreale G., Escobar F. Pituitary and plasma thyrotropin, thyroxine and triiodothyronine after hyperthyroidism. Endocrinology 104: 1467, 1979.
Benotti J., Benotti N. Protein bound iodine, total iodine and butanol extractable iodine by partial automation. Clin. Chem. 9: 408, 1963.
Snedecor G.W. Statistical methods, ed. 5. Iowa State University Press, Ames, 1956.
Goswami A., Rosenberg I.N. Iodothyronine 5′-deiodinase in rat kidney microsomes. Kinetic behavior at low substrate concentration. J. Clin. Invest. 74: 2097, 1984.
Silva E., Matthews P. Thyroid hormone metabolism and the source of plasma triiodothyronine in 2-weeks-old rats: effects of thyroid status. Endocrinology 114: 2394, 1984.
Kaplan M.M. Thyroxine 5′-monodeiodination in rat anterior pituitary homogenate. Endocrinology 106: 567, 1980.
Pascual A., Obregon M.J., Morreale de Escobar G. Tyrosine hydroxylase and the conversion of L-thyroxine into 3′,3,5-triiodo-L-thyronine in the rat. Endocrinology 104: 1574, 1979.
Oppenheimer J.H., Schwartz H.L. Factors determining the level of activity of 3,5,3′-triiodothyronine-responsive hepatic enzymes in the starved rat. Endocrinology 107: 1460, 1980.
Tibaldi J.M., Sahnoun N., Surks M.I. Response of hepatic mitochondrial α-glycerophosphate dehydrogenase and malic enzyme to constant infusions of L-triiodothyronine in rats bearing the Walker 256 carcinoma. Evidence for divergent postreceptor regulation of the thyroid hormone response. J. Clin. Invest. 74: 705, 1984.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Pascual, A. αGPD response to the continuous infusion of thyroxine into the hypothyroid rat. J Endocrinol Invest 10, 55–58 (1987). https://doi.org/10.1007/BF03347154
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF03347154