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Partial nucleotide sequence of human calcitonin precursor mRNA identifies flanking cryptic peptides

Nature volume 295, pages 345–347 (1982)Cite this article

Abstract

Calcitonin is a small peptide hormone (molecular weight (MW) 3,500) synthesized and secreted in mammals by the C-cells of the thyroid1,2. In man a major role of calcitonin is to protect the skeleton during periods of calcium stress such as growth, pregnancy and lactation3. Excessive calcitonin levels are associated with familial and sporadic medullary carcinoma of the thyroid4, and in some cases with ectopic synthesis often by small oat-cell carcinoma of the lung5. Evidence from mRNA-directed cell-free protein synthesis suggests that in common with other small peptide hormones6, human calcitonin is synthesized as a high-molecular-weight precursor protein7–9. Recently, we described the construction and partial characterization of recombinant plasmids containing human calcitonin cDNA sequences9. Here we demonstrate by nucleotide sequence analysis of these cloned cDNA sequences that human calcitonin resides towards the carboxy terminal of a precursor polyprotein, and is flanked at the amino and carboxy termini by cryptic peptide sequences of unknown biological significance. The cryptic peptide present at the carboxy terminus differs significantly in amino acid sequence from that present in the rat calcitonin precursor polyprotein10–12.

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Authors and Affiliations

  1. Courtauld Institute of Biochemistry, Middlesex Hospital Medical School, Mortimer Street, London, W1P 7PN, UK

    Roger K. Craig, Len Hall & Janette Allison

  2. Endocrine Unit, Royal Postgraduate Medical School, Hammersmith Hospital, Du Cane Road, London, W12 0HS, UK

    Mark R. Edbrooke & Iain MacIntyre

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Craig, R., Hall, L., Edbrooke, M. et al. Partial nucleotide sequence of human calcitonin precursor mRNA identifies flanking cryptic peptides. Nature 295, 345–347 (1982). https://doi.org/10.1038/295345a0

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