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Secretin N-terminal hexapeptide potentiates insulin release in mouse islets

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  • Hans Kofod
Peptides representing the N-terminal part of secretin were synthesized and their effects tested on column-perifused isolated mouse pancreatic islets. Insulin release induced by D-glucose was potentiated by the two peptides His-Ser-Asp-Gly-Thr-Phe-OMe (S1-6) and Ser-Asp-Gly-Thr-Phe-OMe (S2-6). The consecutive smaller N-terminal peptides Asp-Gly-Thr-Phe-OMe (S3-6) and Gly-Thr-Phe-OMe (S4-6) had no effects while the dipeptide ester Thr-Phe-OMe (S5-6) also potentiated the release of insulin. The results suggest that the N-terminal part of secretin may be involved in the marked in vitro glucose-dependent insulin release induced by secretin.
OriginalsprogEngelsk
TidsskriftRegulatory Peptides
Vol/bind15
Udgave nummer3
Sider (fra-til)229-37
Antal sider9
ISSN0167-0115
StatusUdgivet - okt. 1986

ID: 45575228