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

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Standard

Secretin and its C-terminal hexapeptide potentiates insulin release in mouse islets. / Kofod, Hans; Hansen, B; Lernmark, A; Hedeskov, C J.

I: American Journal of Physiology (Consolidated), Bind 250, Nr. 2 Pt 1, 02.1986, s. E107-13.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Kofod, H, Hansen, B, Lernmark, A & Hedeskov, CJ 1986, 'Secretin and its C-terminal hexapeptide potentiates insulin release in mouse islets', American Journal of Physiology (Consolidated), bind 250, nr. 2 Pt 1, s. E107-13.

APA

Kofod, H., Hansen, B., Lernmark, A., & Hedeskov, C. J. (1986). Secretin and its C-terminal hexapeptide potentiates insulin release in mouse islets. American Journal of Physiology (Consolidated), 250(2 Pt 1), E107-13.

Vancouver

Kofod H, Hansen B, Lernmark A, Hedeskov CJ. Secretin and its C-terminal hexapeptide potentiates insulin release in mouse islets. American Journal of Physiology (Consolidated). 1986 feb.;250(2 Pt 1):E107-13.

Author

Kofod, Hans ; Hansen, B ; Lernmark, A ; Hedeskov, C J. / Secretin and its C-terminal hexapeptide potentiates insulin release in mouse islets. I: American Journal of Physiology (Consolidated). 1986 ; Bind 250, Nr. 2 Pt 1. s. E107-13.

Bibtex

@article{0bc6e76fa648499e967c7e904d35bd34,
title = "Secretin and its C-terminal hexapeptide potentiates insulin release in mouse islets",
abstract = "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 micrograms/ml; the maximal effect was obtained with 1 microgram/ml secretin. This effect was mimicked by 50-500 micrograms/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.",
keywords = "Animals, Chemical Phenomena, Chemistry, Drug Synergism, Glucose, Glutamate Dehydrogenase, Glutamine, Insulin, Islets of Langerhans, Male, Mice, Mice, Inbred Strains, Peptides, Secretin, Structure-Activity Relationship, Swine",
author = "Hans Kofod and B Hansen and A Lernmark and Hedeskov, {C J}",
year = "1986",
month = feb,
language = "English",
volume = "250",
pages = "E107--13",
journal = "American Journal of Physiology - Cell Physiology",
issn = "0363-6143",
publisher = "American Physiological Society",
number = "2 Pt 1",

}

RIS

TY - JOUR

T1 - Secretin and its C-terminal hexapeptide potentiates insulin release in mouse islets

AU - Kofod, Hans

AU - Hansen, B

AU - Lernmark, A

AU - Hedeskov, C J

PY - 1986/2

Y1 - 1986/2

N2 - 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 micrograms/ml; the maximal effect was obtained with 1 microgram/ml secretin. This effect was mimicked by 50-500 micrograms/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.

AB - 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 micrograms/ml; the maximal effect was obtained with 1 microgram/ml secretin. This effect was mimicked by 50-500 micrograms/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.

KW - Animals

KW - Chemical Phenomena

KW - Chemistry

KW - Drug Synergism

KW - Glucose

KW - Glutamate Dehydrogenase

KW - Glutamine

KW - Insulin

KW - Islets of Langerhans

KW - Male

KW - Mice

KW - Mice, Inbred Strains

KW - Peptides

KW - Secretin

KW - Structure-Activity Relationship

KW - Swine

M3 - Journal article

C2 - 3513606

VL - 250

SP - E107-13

JO - American Journal of Physiology - Cell Physiology

JF - American Journal of Physiology - Cell Physiology

SN - 0363-6143

IS - 2 Pt 1

ER -

ID: 45575248