Activation of Renal Cortical Adenylate Cyclase by Circulating Immunoreactive Parathyroid Hormone Fragments

Janet M. Canterbury; Gerald S. Levey; Eric Reiss

doi:10.1172/JCI107211

^{Division of Endocrinology and Metabolism, Department of Medicine, University of Miami School of Medicine, Miami, Florida, 33152}

^{Department of Biology, Illinois Institute of Technology, Chicago, Illinois 60616}

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^{Division of Endocrinology and Metabolism, Department of Medicine, University of Miami School of Medicine, Miami, Florida, 33152}

^{Department of Biology, Illinois Institute of Technology, Chicago, Illinois 60616}

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^{Division of Endocrinology and Metabolism, Department of Medicine, University of Miami School of Medicine, Miami, Florida, 33152}

^{Department of Biology, Illinois Institute of Technology, Chicago, Illinois 60616}

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Published in Volume 52, Issue 2 on February 1, 1973
J Clin Invest. 1973;52(2):524–527. https://doi.org/10.1172/JCI107211.
© 1973 The American Society for Clinical Investigation

Published February 1, 1973 - Version history

Three distinct immunoreactive species of parathyroid hormone (PTH) are present in human serum. One has an estimated mol wt of 9,500 and probably represents glandular hormone, the second 7,000-7,500 mol wt, and the third 4,500-5,000 mol wt. In order to assess the biological activity of these circulating forms of PTH, we determined their ability to activate renal cortical adenylate cyclase. The 9,500 mol wt and 4,500-5,000 mol wt fractions produced four- to sixfold increases in cyclic 3′,5′-AMP accumulation above control; the 7,000-7,500 mol wt fraction was inactive. None of the fragments had any effects on phosphodiesterase activity. Antiserum to bovine PTH did not block the activation of adenylate cyclase by either the gragments or bovine PTH. The data suggest that a large proportion of circulating immunoreactive human PTH is biologically active and that the biologically and immunologically active sites of the hormone are distinct.

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