Abstract
Parathyroid hormone (PTH) is an 84 amino acid peptide (mol. wt.: 9500) secreted by the parathyroid gland. Except for possible ectopic production in certain neoplastic syndromes, the parathyroid is the only known source of circulating PTH. In common with most secretory proteins, PTH is initially synthesized as a large precursor which then undergoes a series of enzymatic cleavages to yield the final secretory product, (1–84) PTH.1,2 The initial ribosomal product is a 115 amino acid peptide, known as pre-proPTH, containing the 84 amino acid PTH sequence and a 31 amino acid NH2 terminal extension.3 The first 25 amino acids of this chain, the signal or pre sequence, is a hydrophobic molecule similar to that of other (perhaps all) secreted proteins and is believed to direct the nascent peptide from the ribosome, where it is being assembled, into the cisternal space of the endoplasmic reticulum.4,5 Either during, or shortly after this directed transport, the 25 amino acid NH2 pre sequence is removed leaving the 90 amino acid proPTH inside the cisternal space.6,7
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References
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Agus, Z.S., Attie, M., Goldfarb, S., Wasserstein, A. (1983). Mineral Metabolism in Health and Disease. In: Klahr, S., Massry, S.G. (eds) Contemporary Nephrology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6722-6_6
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