Hormone synthesis and secretion by rat parathyroid glands in tissue culture

William Y. W. Au; Alan P. Poland; Paula H. Stern; Lawrence G. Raisz

doi:10.1172/JCI106381

^{Department of Pharmacology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

^{Department of Toxicology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

^{Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

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^{Department of Pharmacology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

^{Department of Toxicology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

^{Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

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^{Department of Pharmacology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

^{Department of Toxicology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

^{Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

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^{Department of Pharmacology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

^{Department of Toxicology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

^{Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620}

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Published in Volume 49, Issue 9 on September 1, 1970
J Clin Invest. 1970;49(9):1639–1646. https://doi.org/10.1172/JCI106381.
© 1970 The American Society for Clinical Investigation

Published September 1, 1970 - Version history

Rat parathyroid glands maintained in organ culture secrete biologically active parathyroid hormone (PTH) and synthesize and secrete labeled proteins from ³H- or ¹⁴C-labeled amino acids added to the medium. The amounts of biological activity and labeled protein in the medium are both inversely proportional to the calcium concentration. Some of the labeled low molecular weight protein was identified as PTH which had been synthesized and secreted in culture by preliminary isolation on Sephadex G-100 columns and further purification using an antibody to bovine PTH which cross-reacted with rat PTH. The cross-reacting antibody inhibited the biological effects of rat PTH and caused hypocalcemia in intact rats. The antibody bound some of the labeled low molecular weight protein of the medium at neutral pH so that it migrated as a large molecular weight complex on Sephadex. Biologically active, labeled PTH was recovered by dissociation of this complex in acid and rechromatography.