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• W160381224 abstract "Three generations of assays for parathyroid hormone (PTH) have been used to characterize circulating PTH molecular forms. In a normocalcemic individual, circulating PTH is composed of 75% C-PTH fragments missing an amino-terminal structure, 5% non-(1–84) PTH fragments with a partially preserved amino-terminal structure, 2% N-PTH, a phosphorylated form of PTH(1–84), and 18% PTH(1–84), the bioactive form of the hormone. The carboxyl-terminal structure of PTH, the last 50 amino acids, does not interact with the PTH/PTHrP type 1 receptor. This has created a paradox where PTH(1–84), a minor circulating form of PTH, is responsible for the bioactivity of the hormone while C-PTH fragments are considered biologically inactive. This paradox is beginning to be resolved, as recent studies demonstrate that C-PTH fragments do appear to exert biological activities opposite to those of PTH(1–84) via a not-yet-cloned C-PTH receptor. They can decrease calcium concentration, phosphate excretion, bone resorption, and 1,25(OH) 2 D synthesis. The clinical implications of this new concept are reviewed." @default.
• W160381224 created "2016-06-24" @default.
• W160381224 creator A5003847350 @default.
• W160381224 date "2015-01-01" @default.
• W160381224 modified "2023-09-24" @default.
• W160381224 title "Metabolism and Measurement of Parathyroid Hormone" @default.
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