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Endocrinology, Vol 126, 325-329, Copyright © 1990 by Endocrine Society

ARTICLES

Alterations of human growth hormone binding by rat liver membranes during hypo- and hyperthyroidism

Z Hochberg, T Bick and Z Harel
Rappaport Family Institute for Research in the Medical Sciences, Haifa, Israel.

Hypothyroid rats treated with human GH (hGH) were partially refractory to the latter's effects. The present study was undertaken to investigate the role of hypo- and hyperthyroidism on the GH receptor. Seven-week-old rats were rendered either hypothyroid, by methimazole, or hyperthyroid, by a daily overdose of T4, during weeks 7-14 of life. Livers were homogenized and overlaid on sucrose discontinuous density gradient. Removal of endogenous ligand from the receptor was performed by exposing the membranes to MgCl2. hGH was used with excess ovine PRL to characterize somatogenic specific binding. Lactogenic specific binding was calculated by subtracting somatogenic specific binding from the total specific binding. Creatine kinase was also measured in homogenized livers. Liver membranes of the hypothyroid rats showed a significant decline in somatogenic and lactogenic binding of hGH. This was true for both the free unoccupied binding sites and total binding after dissociation of the endogenous ligand. Replacement of T4 for 2 weeks restored hGH binding to control values. Hyperthyroid rats had high somatogenic and lactogenic hGH binding. Creatine kinase activity decreased significantly in liver homogenates of hypothyroid rats, was restored by T4 replacement, and increased significantly in hyperthyroid rats. Thus, lactogenic and somatogenic receptors are directly related to the thyroid status in vivo.


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