Effects of galanin fragments on insulin release from the isolated perfused rat pancreas

T. Mochizuki, J. Ishikawa, K. Ohshima, G. H. Greeley, N. Yanaihara

    Research output: Contribution to journalArticle

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    Abstract

    The objective of this study was to examine the effects of galanin and novel synthetic galanin-related peptides on glucose-induced insulin release from the isolated perfused rat pancreas. Galanin(1-29) (10-8M) inhibited glucose-induced insulin secretion significantly (P<0.05). Galanin(2-29) did not inhibit insulin release, however galanin(3-29) and C-terminal fragments of galanin stimulated insulin secretion significantly, indicating that the N-terminal residue of galanin, in part, is crucial for the inhibitory effect of galanin(1-29) on insulin release. [D-Trp2], [Phe2], and [Ile2]-galanin significantly inhibited glucose-induced insulin release, however [Tyr2]-galanin was inactive. [Ala2]-galanin enhanced glucose-induced insulin release, suggesting a structural requirement for the amino acid in the second position from the amino terminal for inhibitory activity. N(α)-acetylated galanin(2-29) [Ac-galanin(2-29)] showed the same inhibitory effect as galanin, however Ac-galanin(1-29) was not active, indicating that the N-terminal Gly or des-amino Gly residue is essential for inhibitory activity. Ac-[Tyr2]-galanin(2-29) inhibited insulin release, but not significantly. Galanin(1-15), (1-19) and (1-15)-ol had little effect on glucose-induced insulin release indicating that this region is not adequate for biologic activity despite a conservation of primary structure of this region among several species. These findings indicate that the Trp2 residue of galanin is important for its inhibitory activity on insulin release, and that the N-terminal 1-15 portion is essential for the development of a galanin antagonist.

    Original languageEnglish (US)
    Pages (from-to)203-213
    Number of pages11
    JournalBiomedical Research
    Volume13
    Issue number3
    StatePublished - 1992

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    Galanin
    Rats
    Pancreas
    Insulin
    Glucose

    ASJC Scopus subject areas

    • Biochemistry, Genetics and Molecular Biology(all)

    Cite this

    Mochizuki, T., Ishikawa, J., Ohshima, K., Greeley, G. H., & Yanaihara, N. (1992). Effects of galanin fragments on insulin release from the isolated perfused rat pancreas. Biomedical Research, 13(3), 203-213.

    Effects of galanin fragments on insulin release from the isolated perfused rat pancreas. / Mochizuki, T.; Ishikawa, J.; Ohshima, K.; Greeley, G. H.; Yanaihara, N.

    In: Biomedical Research, Vol. 13, No. 3, 1992, p. 203-213.

    Research output: Contribution to journalArticle

    Mochizuki, T, Ishikawa, J, Ohshima, K, Greeley, GH & Yanaihara, N 1992, 'Effects of galanin fragments on insulin release from the isolated perfused rat pancreas', Biomedical Research, vol. 13, no. 3, pp. 203-213.
    Mochizuki T, Ishikawa J, Ohshima K, Greeley GH, Yanaihara N. Effects of galanin fragments on insulin release from the isolated perfused rat pancreas. Biomedical Research. 1992;13(3):203-213.
    Mochizuki, T. ; Ishikawa, J. ; Ohshima, K. ; Greeley, G. H. ; Yanaihara, N. / Effects of galanin fragments on insulin release from the isolated perfused rat pancreas. In: Biomedical Research. 1992 ; Vol. 13, No. 3. pp. 203-213.
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    AB - The objective of this study was to examine the effects of galanin and novel synthetic galanin-related peptides on glucose-induced insulin release from the isolated perfused rat pancreas. Galanin(1-29) (10-8M) inhibited glucose-induced insulin secretion significantly (P<0.05). Galanin(2-29) did not inhibit insulin release, however galanin(3-29) and C-terminal fragments of galanin stimulated insulin secretion significantly, indicating that the N-terminal residue of galanin, in part, is crucial for the inhibitory effect of galanin(1-29) on insulin release. [D-Trp2], [Phe2], and [Ile2]-galanin significantly inhibited glucose-induced insulin release, however [Tyr2]-galanin was inactive. [Ala2]-galanin enhanced glucose-induced insulin release, suggesting a structural requirement for the amino acid in the second position from the amino terminal for inhibitory activity. N(α)-acetylated galanin(2-29) [Ac-galanin(2-29)] showed the same inhibitory effect as galanin, however Ac-galanin(1-29) was not active, indicating that the N-terminal Gly or des-amino Gly residue is essential for inhibitory activity. Ac-[Tyr2]-galanin(2-29) inhibited insulin release, but not significantly. Galanin(1-15), (1-19) and (1-15)-ol had little effect on glucose-induced insulin release indicating that this region is not adequate for biologic activity despite a conservation of primary structure of this region among several species. These findings indicate that the Trp2 residue of galanin is important for its inhibitory activity on insulin release, and that the N-terminal 1-15 portion is essential for the development of a galanin antagonist.

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