Differential Effects of Secretin-fragments imply a dual Mechanism of Action for Secretin

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Differential Effects of Secretin-fragments imply a dual Mechanism of Action for Secretin. / Kofod, Hans; Thams, P; Holst, J J.

In: International Journal of Peptide and Protein Research, Vol. 37, No. 2, 02.1991, p. 134-139.

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

Harvard

Kofod, H, Thams, P & Holst, JJ 1991, 'Differential Effects of Secretin-fragments imply a dual Mechanism of Action for Secretin', International Journal of Peptide and Protein Research, vol. 37, no. 2, pp. 134-139.

APA

Kofod, H., Thams, P., & Holst, J. J. (1991). Differential Effects of Secretin-fragments imply a dual Mechanism of Action for Secretin. International Journal of Peptide and Protein Research, 37(2), 134-139.

Vancouver

Kofod H, Thams P, Holst JJ. Differential Effects of Secretin-fragments imply a dual Mechanism of Action for Secretin. International Journal of Peptide and Protein Research. 1991 Feb;37(2):134-139.

Author

Kofod, Hans ; Thams, P ; Holst, J J. / Differential Effects of Secretin-fragments imply a dual Mechanism of Action for Secretin. In: International Journal of Peptide and Protein Research. 1991 ; Vol. 37, No. 2. pp. 134-139.

Bibtex

@article{4fd09c2074d111dbbee902004c4f4f50,
title = "Differential Effects of Secretin-fragments imply a dual Mechanism of Action for Secretin",
abstract = "The effects of synthetic peptides, representing different parts of the secretin molecule in isolated mouse pancreatic islets have been investigated in perifusion studies. In the presence of 10 mM D-glucose the C-terminal nonapeptide Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 (S19-27) showed a 2-fold higher activity than that earlier shown for S22-27 and had the same effect on the dynamic pattern of insulin release as secretin, while the elongating sequence Leu-Gln-Arg (S19-21) had no effect on the insulin release. The nonapeptide Leu-Ser-Arg-Leu-Arg-Asp-Ser-Ala-Arg (S10-18) had no influence on the insulin release. Glucagon release seen after intact secretin could not be shown for any of the smaller fragments. Accumulation of cAMP in the islets as seen with secretin, could at 10 mmol/L D-glucose only be demonstrated with S22-27 or S19-27 but not with S10-18 or S1-6. Our results indicate that full size secretin has to be present to stimulate glucagon release while insulin-releasing activity can be confined to the C-terminal part of the hormone.",
keywords = "Amino Acid Sequence, Animals, Cyclic AMP, Glucagon, Glucose, Insulin, Islets of Langerhans, Male, Mice, Molecular Sequence Data, Peptide Fragments, Secretin",
author = "Hans Kofod and P Thams and Holst, {J J}",
year = "1991",
month = feb,
language = "English",
volume = "37",
pages = "134--139",
journal = "International Journal of Peptide and Protein Research",
number = "2",

}

RIS

TY - JOUR

T1 - Differential Effects of Secretin-fragments imply a dual Mechanism of Action for Secretin

AU - Kofod, Hans

AU - Thams, P

AU - Holst, J J

PY - 1991/2

Y1 - 1991/2

N2 - The effects of synthetic peptides, representing different parts of the secretin molecule in isolated mouse pancreatic islets have been investigated in perifusion studies. In the presence of 10 mM D-glucose the C-terminal nonapeptide Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 (S19-27) showed a 2-fold higher activity than that earlier shown for S22-27 and had the same effect on the dynamic pattern of insulin release as secretin, while the elongating sequence Leu-Gln-Arg (S19-21) had no effect on the insulin release. The nonapeptide Leu-Ser-Arg-Leu-Arg-Asp-Ser-Ala-Arg (S10-18) had no influence on the insulin release. Glucagon release seen after intact secretin could not be shown for any of the smaller fragments. Accumulation of cAMP in the islets as seen with secretin, could at 10 mmol/L D-glucose only be demonstrated with S22-27 or S19-27 but not with S10-18 or S1-6. Our results indicate that full size secretin has to be present to stimulate glucagon release while insulin-releasing activity can be confined to the C-terminal part of the hormone.

AB - The effects of synthetic peptides, representing different parts of the secretin molecule in isolated mouse pancreatic islets have been investigated in perifusion studies. In the presence of 10 mM D-glucose the C-terminal nonapeptide Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val-NH2 (S19-27) showed a 2-fold higher activity than that earlier shown for S22-27 and had the same effect on the dynamic pattern of insulin release as secretin, while the elongating sequence Leu-Gln-Arg (S19-21) had no effect on the insulin release. The nonapeptide Leu-Ser-Arg-Leu-Arg-Asp-Ser-Ala-Arg (S10-18) had no influence on the insulin release. Glucagon release seen after intact secretin could not be shown for any of the smaller fragments. Accumulation of cAMP in the islets as seen with secretin, could at 10 mmol/L D-glucose only be demonstrated with S22-27 or S19-27 but not with S10-18 or S1-6. Our results indicate that full size secretin has to be present to stimulate glucagon release while insulin-releasing activity can be confined to the C-terminal part of the hormone.

KW - Amino Acid Sequence

KW - Animals

KW - Cyclic AMP

KW - Glucagon

KW - Glucose

KW - Insulin

KW - Islets of Langerhans

KW - Male

KW - Mice

KW - Molecular Sequence Data

KW - Peptide Fragments

KW - Secretin

M3 - Journal article

C2 - 1850389

VL - 37

SP - 134

EP - 139

JO - International Journal of Peptide and Protein Research

JF - International Journal of Peptide and Protein Research

IS - 2

ER -

ID: 308473