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Åke Lernmark

Principal investigator

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Secretin and its C-terminal hexapeptide potentiates insulin release in mouse islets


  • H. Kofod
  • B. Hansen
  • A. Lernmark
  • C. J. Hedeskov

Summary, in English

Peptides representing the C-terminal end of secretin were synthetized and their effects tested along with secretin on column-perifused isolated mouse pancreatic islets. Insulin release induced by 10 mmol/l D-glucose was potentiated by secretin tested in a concentration range of 0.01-10 μg/ml; the maximal effect was obtained with 1 μg/ml secretin. This effect was mimicked by 50-500 μg/ml NH2-Leu-Leu-Gln-Gly-Leu-Val-NH2, [S-(22-27)], which represents an amidated C-terminal sequence of the secretin molecule. The consecutive smaller secretin C-terminal peptides had either no effects [Val-NH2, S-(24-27)] or only marginally [S-(26-27), S-(23-27)]potentiating effects on insulin release in the presence of 10 mmol/l D-glucose. The effects of secretin and S-(22-27) were not influenced by 2 mmol/l glutamine. The intact hormone and the five synthetic peptides as well as Val-NH2 had no stimulatory effect on islet glutamate dehydrogenase activity. In fact, S-(23-27), S-(24-27), and S-(25-27) inhibited the islet glutamate dehydrogenase activity, the activation by which amino acids and amino acid derivatives are known to elicit a potentiation of insulin release. Our results suggest that the C-terminal part is important to the marked potentiation of glucose-induced insulin release in vitro by secretin.

Publishing year





American Journal of Physiology - Endocrinology and Metabolism





Document type

Journal article


American Physiological Society




  • ISSN: 0193-1849