Comparison of renal and osseous binding of parathyroid hormone and hormonal fragments

Journal Article · Fri Nov 01 00:00:00 EST 1985 · Am. J. Physiol.; (United States)

OSTI ID:6388983

Demay, M; Mitchell, J; Goltzman, D

The authors compared receptor binding and adenylate cyclase stimulation of intact bovine parathyroid hormone (bPTH)-(1-84) and the synthetic amino-terminal fragments, bPTH-(1-34) and rat PTH (rPTH)-(1-34). In both canine renal membranes and cloned rat osteosarcoma cells the amino-terminal fragments bound to a single order of sites; the affinity of rPTH-(1-34) exceeded that of bPTH-(1-34), correlating with its higher potency in stimulating adenylate cyclase. In studies with oxidized bPTH-(1--84), the middle and carboxyl regions of intact PTH were found to bind to both tissues but with higher affinity to osteosarcoma cells than to renal membranes. Our results demonstrate that rPTH-(1--34) is the most favorable probe of amino-terminal PTH binding and the most potent of the PTH peptides in stimulating renal and osseous adenylate cyclase. The results also show that midregion and carboxyl determinants within intact PTH contribute to hormone binding, which does not correlate with adenylate cyclase activation and appears more significant for skeletal than for renal binding.

• Research Organization: Royal Victoria Hospital, Montreal, Canada
• OSTI ID: 6388983
• Journal Information: Am. J. Physiol.; (United States), Journal Name: Am. J. Physiol.; (United States)
• Country of Publication: United States
• Language: English

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62 RADIOLOGY AND NUCLEAR MEDICINE
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KIDNEYS
OSTEOSARCOMAS
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SKELETON
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550601* - Medicine- Unsealed Radionuclides in Diagnostics