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Science 11 December 1987:
Vol. 238. no. 4833, pp. 1568 - 1570
DOI: 10.1126/science.3685995
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Articles
Science, Vol 238, Issue 4833, 1568-1570
Copyright © 1987 by American Association for the Advancement of Science
Parathyroid hormone-related protein of malignancy: active synthetic fragments
BE Kemp,
JM Moseley,
CP Rodda,
PR Ebeling,
RE Wettenhall,
D Stapleton,
H Diefenbach-Jagger,
F Ure,
VP Michelangeli,
HA Simmons,
and
al. et
University of Melbourne, Department of Medicine, Repatriation General Hospital, Heidelberg, Victoria, Australia.
Peptides corresponding to the amino-terminal region of the parathyroid hormone-related protein (PTHrP) of humoral hypercalcemia of malignancy were synthesized. A 34-amino acid peptide, PTHrP(1-34), was two to four times more potent than bovine or human PTH(1-34) in bioassays promoting the formation of adenosine 3',5'-monophosphate (cAMP) and plasminogen activator activity in osteogenic sarcoma cells and adenylate cyclase activity in chick kidney membranes. Like parathyroid hormone itself, in which the activity resides in the first 34 residues, PTHrP peptides of less than 30 residues from the amino terminus showed substantially reduced activity. PTHrP(1-34) had only 6% of the potency of bovine PTH(1-34) in promoting bone resorption in vitro. PTHrP(1-34) strongly promoted the excretion of cAMP and phosphorus and reduced the excretion of calcium in the isolated, perfused rat kidney consistent with the symptoms seen in malignant hypercalcemia.
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