Secretin N-terminal hexapeptide potentiates insulin release in mouse islets
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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.
Original language | English |
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Journal | Regulatory Peptides |
Volume | 15 |
Issue number | 3 |
Pages (from-to) | 229-37 |
Number of pages | 9 |
ISSN | 0167-0115 |
Publication status | Published - Oct 1986 |
- Amino Acid Sequence, Animals, Glucose, Insulin, Islets of Langerhans, Male, Mice, Mice, Inbred Strains, Peptide Fragments, Secretin, Structure-Activity Relationship
Research areas
ID: 45575228