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Hormone metabolism and response of adenylate cyclase to parathyroid hormone in kidney
Author(s) -
Moseley Jane M.,
Martin T. J.,
Robinson C. J.,
Reit B. W.,
Tregear G. W.
Publication year - 1975
Publication title -
clinical and experimental pharmacology and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.752
H-Index - 103
eISSN - 1440-1681
pISSN - 0305-1870
DOI - 10.1111/j.1440-1681.1975.tb01860.x
Subject(s) - parathyroid hormone , kidney , cyclase , adenylate kinase , medicine , hormone , endocrinology , chemistry , incubation , hormone receptor , renal cortex , biology , biochemistry , receptor , calcium , stimulation , cancer , breast cancer
SUMMARY 1. Incubation of parathyroid hormone with plasma membranes from rat kidney cortex resulted in rapid loss of all hormonal activity. 2. Chick kidney membranes showed no ability to inactivate parathyroid hormone even with prolonged incubation. 3. Biologically active, labelled parathyroid hormone was degraded to fragments by rat kidney membranes, but not by chick kidney. 4. Hormone‐responsive adenylate cyclase activity in a mixture of rat and chick kidney membranes was additive. 5. Parathyroid hormone bound specifically to chick kidney plasma membranes. 6. It is concluded that hormone inactivation during incubation has little relevance to the effectiveness of parathyroid hormone in stimulating adenylate cyclase activity in kidney, and furthermore that failure of chick kidney to metabolize the hormone is not the explanation for the greater sensitivity of this species to the hormone.