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. 1974 Mar;71(3):723–726. doi: 10.1073/pnas.71.3.723

Parathyroid Hormone Receptors of Renal Cortex: Specific Binding of Biologically Active, 125I-Labeled Hormone and Relationship to Adenylate Cyclase Activation

Francis P Di Bella 1,2, Thomas P Douša 1,2, Sam S Miller 1,2, Claude D Arnaud 1,2
PMCID: PMC388085  PMID: 4362630

Abstract

Biologically active 125I-labeled bovine parathyroid hormone (prepared by electrolytic iodination) and its synthetic NH2-terminal (1-34) biologically active fragment bound rapidly and specifically to a purified plasma membrane preparation from bovine renal cortex. Binding of labeled intact hormone or labeled NH2-terminal (1-34) peptide was inhibited competitively by unlabeled (1-34) peptide in the same range of concentrations that activated renal cortical 3′:5′-adenylate cyclase (EC 4.6.1.1) in these membranes. The concentrations of synthetic (1-34) peptide for half-maximal inhibition of binding of labeled hormone as well as half-maximal activation of the enzyme were about 0.6 μM (2.5 μg/ml). Therefore it is likely that the binding activity studied represents a physiologically important renal receptor for parathyroid hormone.

Biologically inactive (oxidized) forms of parathyroid hormone and (1-34) NH2-terminal peptide as well as calcitonin, glucagon, insulin, and epinephrine failed to competitively inhibit the binding of labeled (1-34) parathyroid hormone or activate adenylate cyclase in the renal cortical membrane preparation.

Observations with the NH2-terminal (1-34) biologically active fragment of parathyroid hormone suggest that the COOH-terminal region of the molecule is not required for receptor binding.

Keywords: calcium metabolism, cyclic AMP, electrolytic iodination of peptides, synthetic bovine parathyroid hormone(1-34)

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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