Activation of renal cortical adenylate cyclase by circulating immunoreactive parathyroid hormone fragments.
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.
D000262:Adenylyl Cyclases / Q000096:biosynthesis*; D000818:Animals; D004789:Enzyme Activation; D007106:Immune Sera; D007456:Iodine Isotopes; D007668:Kidney / Q000201:enzymology*; D007672:Kidney Cortex / Q000201:enzymology; D008970:Molecular Weight; D010281:Parathyroid Hormone / Q000494:pharmacology* / Q000502:physiology; D010455:Peptides / Q000494:pharmacology; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D051381:Rats
D007106:Immune Sera; D007456:Iodine Isotopes; D010281:Parathyroid Hormone; D010455:Peptides; D010727:Phosphoric Diester Hydrolases; D000262:Adenylyl Cyclases