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Insulin and glucagon

  • Chapter
Peptide Hormones

Part of the book series: Biological Council ((BCSDA))

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Abstract

As discussed by Steiner in this volume (p. 49), insulin is synthesised within the beta-cell of the pancreas as a single-chain proinsulin of 86 amino acids (human), which then folds back on itself followed by closure of sulphur bridges (see figure 6.1). As shown by Steiner in the mid-1960s, the ‘connecting peptide’ is then split out, leaving two amino acid chains of 21 and 30 amino acids (A- and B-chains, respectively) connected by sulphur bridges. This splitting out of the connecting peptide occurs as the proinsulin is packaged into vesicles in the Golgi apparatus. Thus, when the beta-cell is stimulated to release insulin and secretory granules are brought to its surface for discharge, the hormonally inert connecting peptide passes together with insulin into the adjacent capillary. Normally a small amount of proin­sulin is also released, but this prohormone is much less active than insulin itself. In abnormal states such as islet cell tumour or in diabetes, the pro­portion of proinsulin which is secreted may be increased, and this has been of help in diagnosis.

Supported in part by USPHS Grants AM 15191, AM 05077 and FR-31.

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Authors and Affiliations

  1. Joslin Research Laboratory, Department of Medicine, Harvard Medical School, and the Peter Bent Brigham Hospital, Boston, USA

    G. F. Cahill Jr.

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  1. G. F. Cahill Jr.
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Editors and Affiliations

  1. National Institute for Medical Research, Mill Hill, London, UK

    J. A. Parsons M.A., B.M., B.Ch.

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© 1976 Institute of Biology Endowment Trust Fund

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Cahill, G.F. (1976). Insulin and glucagon. In: Parsons, J.A. (eds) Peptide Hormones. Biological Council. Palgrave, London. https://doi.org/10.1007/978-1-349-02718-7_6

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