Amino-Terminal Form of Parathyroid Hormone (PTH) with Immunologic Similarities to hPTH(1–84) Is Overproduced in Primary and Secondary Hyperparathyroidism

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Abstract
Background: To separate non-(1–84)parathyroid hormone [non-(1–84)PTH] from PTH(1–84), we developed new HPLC gradients and observed that the peak coeluting with hPTH(1–84) could be separated into two entities recognized by a cyclase-activating PTH (CA-PTH) assay that reacts with the first four amino acids of the PTH structure. Methods: Sera from six healthy individuals and five patients with primary hyperparathyroidism, and eight pools of sera from patients in renal failure were fractionated by HPLC. A total (T)-PTH assay reacting with the (15–20) region, the CA-PTH assay, and a COOH-terminal (C)-PTH assay with a (65–84) structure requirement were used to measure basal and fractionated PTH values. Results: T-PTH was higher than CA-PTH in all healthy controls [mean (SD), 3.13 (0.37) vs 2.29 (0.33) pmol/L; P P Conclusions: This new molecular form of PTH has structural integrity of the (1–4) region but presumably is modified in the region (15–20), which is usually recognized by the T-PTH assay. Its clinical implications remain to be defined.

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