Secretin N-terminal hexapeptide potentiates insulin release in mouse islets

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Secretin N-terminal hexapeptide potentiates insulin release in mouse islets. / Kofod, Hans.

In: Regulatory Peptides, Vol. 15, No. 3, 10.1986, p. 229-37.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kofod, H 1986, 'Secretin N-terminal hexapeptide potentiates insulin release in mouse islets', Regulatory Peptides, vol. 15, no. 3, pp. 229-37.

APA

Kofod, H. (1986). Secretin N-terminal hexapeptide potentiates insulin release in mouse islets. Regulatory Peptides, 15(3), 229-37.

Vancouver

Kofod H. Secretin N-terminal hexapeptide potentiates insulin release in mouse islets. Regulatory Peptides. 1986 Oct;15(3):229-37.

Author

Kofod, Hans. / Secretin N-terminal hexapeptide potentiates insulin release in mouse islets. In: Regulatory Peptides. 1986 ; Vol. 15, No. 3. pp. 229-37.

Bibtex

@article{b2e4336d96ab4513880af8d6efc1d08f,
title = "Secretin N-terminal hexapeptide potentiates insulin release in mouse islets",
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.",
keywords = "Amino Acid Sequence, Animals, Glucose, Insulin, Islets of Langerhans, Male, Mice, Mice, Inbred Strains, Peptide Fragments, Secretin, Structure-Activity Relationship",
author = "Hans Kofod",
year = "1986",
month = oct,
language = "English",
volume = "15",
pages = "229--37",
journal = "Regulatory Peptides",
issn = "0167-0115",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - Secretin N-terminal hexapeptide potentiates insulin release in mouse islets

AU - Kofod, Hans

PY - 1986/10

Y1 - 1986/10

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Glucose

KW - Insulin

KW - Islets of Langerhans

KW - Male

KW - Mice

KW - Mice, Inbred Strains

KW - Peptide Fragments

KW - Secretin

KW - Structure-Activity Relationship

M3 - Journal article

C2 - 3538223

VL - 15

SP - 229

EP - 237

JO - Regulatory Peptides

JF - Regulatory Peptides

SN - 0167-0115

IS - 3

ER -

ID: 45575228