Abstract
The widely occurring1–3 tetradecapeptide somatostatin (SRIF-14) has been variously implicated4–8 as a neurotransmitter, a neurohormone, a cybernin (local regulatory factor) and a hormone. In the first isolation of SRIF-14 from hypothalamic extracts9,10 and subsequent extracts of other tissues11–15, peptides of higher molecular weight but with similar activity have been noted. Recently two such peptides have been characterized as the 28-amino acid SRIF-28 (from porcine gastro-intestinal tract16 and porcine and ovine hypothalamus17,18) and the 25-amino acid SRIF-25 (from ovine hypothalamus17), each of which consists of an N–terminal extension of SRIF-14. We now report that SRIF-28 and SRIF-25 are more potent than SRIF-14 in the inhibition of insulin release, but that SRIF-14 preferentially inhibits glucagon release. This suggests that SRIF-28 and SRIF-25 are not mere biosynthetic precursors of SRIF-14 and that their differential release may be physiologically important.
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Mandarino, L., Stenner, D., Blanchard, W. et al. Selective effects of somatostatin-14, -25 and -28 on in vitro insulin and glucagon secretion. Nature 291, 76–77 (1981). https://doi.org/10.1038/291076a0
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DOI: https://doi.org/10.1038/291076a0
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