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Strewler GJ, Stern PH, Jacobs JW, et al. Parathyroid hormonelike protein from human renal carcinoma cells. Structural and functional homology with parathyroid hormone. J Clin Invest. 1987;80(6):1803-7doi: 10.1172/JCI113275.
Strewler, G. J., Stern, P. H., Jacobs, J. W., Eveloff, J., Klein, R. F., Leung, S. C., Rosenblatt, M., & Nissenson, R. A. (1987). Parathyroid hormonelike protein from human renal carcinoma cells. Structural and functional homology with parathyroid hormone. The Journal of clinical investigation, 80(6), 1803-7. https://doi.org/10.1172/JCI113275
Strewler, G J, et al. "Parathyroid hormonelike protein from human renal carcinoma cells. Structural and functional homology with parathyroid hormone." The Journal of clinical investigation vol. 80,6 (1987): 1803-7. doi: https://doi.org/10.1172/JCI113275
Strewler GJ, Stern PH, Jacobs JW, Eveloff J, Klein RF, Leung SC, Rosenblatt M, Nissenson RA. Parathyroid hormonelike protein from human renal carcinoma cells. Structural and functional homology with parathyroid hormone. J Clin Invest. 1987 Dec;80(6):1803-7. doi: 10.1172/JCI113275. PMID: 3680530; PMCID: PMC442457.
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American Society for Clinical Investigation Free PMC Article

J Clin Invest. 1987 Dec;80(6):1803-7. doi: 10.1172/JCI113275.

Parathyroid hormonelike protein from human renal carcinoma cells. Structural and functional homology with parathyroid hormone.

The Journal of clinical investigation

G J Strewler, P H Stern, J W Jacobs, J Eveloff, R F Klein, S C Leung, M Rosenblatt, R A Nissenson

Affiliations

  1. Veterans Administration Medical Center, San Francisco, California 94121.

PMID: 3680530 PMCID: PMC442457 DOI: 10.1172/JCI113275
Free PMC Article

Abstract

A variety of solid tumors secrete proteins that are immunochemically distinct from parathyroid hormone (PTH) but activate PTH-responsive adenylate cyclase. Such PTH-like proteins have been proposed as mediators of the hypercalcemia and hypophosphatemia frequently associated with malignancies. We purified to apparent homogeneity a PTH-like protein with a molecular weight of 6,000, that is produced by human renal carcinoma cells. The amino-terminal sequence of the PTH-like protein and that of human PTH were found to display at least five identities in the first 13 positions. The purified protein bound to PTH receptors, activated adenylate cyclase in renal plasma membranes, and stimulated cAMP formation in rat osteosarcoma cells. The PTH-like protein reproduced two additional effects of PTH, stimulation of bone resorption in fetal rat limb bone cultures and inhibition of phosphate uptake in cultured opossum kidney cells. These properties are consistent with a role for PTH-like proteins as mediators of the syndrome of malignancy-associated hypercalcemia.

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