Abstract
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 |
|---|---|
| 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 |
Keywords
- Amino Acid Sequence
- Animals
- Glucose
- Insulin
- Islets of Langerhans
- Male
- Mice
- Mice, Inbred Strains
- Peptide Fragments
- Secretin
- Structure-Activity Relationship