PHI structural requirements for potentiation of glucose-induced insulin release

C. Yanaihara, Y. Hashimoto, Y. Takeda, I. Kato, N. S. Track, K. Nokihara, H. Manaka, T. Iwanaga, T. Fujita, H. Okamoto, N. Yanaihara

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Immunoreactive PHI was detected in rat pancreas. The potentiating effect of 10-9 M PHI upon insulin release from the isolated perfused rat pancreas was significant and most consistent when 250 mg% glucose was present in the perfusion medium. PHI(1-15) retained a substantial potentiating effect on insulin release, while PHI(14-27) was essentially inactive. Replacement of amino-terminal decapeptide portion of the PHI molecule with the corresponding part of VIP resulted in a drastic decrease of the potentiating effect of PHI on insulin release. 10-8 M PHI(14-27) substantially diminished the potentiation by 10-9 M PHI while PHI(1-15) was without an inhibitory effect. The present results indicate that the PHI active site for potentiation of glucose-induced insulin release resides in the amino-terminal segment of the molecule but requires the carboxyl terminal segment primarily for binding to exhibit full biological activity.

Original languageEnglish
Pages (from-to)83-88
Number of pages6
JournalPeptides
Volume7
Issue numberSUPPL. 1
DOIs
Publication statusPublished - 1986
Externally publishedYes

Keywords

  • Insulin release potentiation
  • Isolated perfused rat pancreas
  • PHI
  • PHI fragments
  • Structure-function relationship

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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  • Cite this

    Yanaihara, C., Hashimoto, Y., Takeda, Y., Kato, I., Track, N. S., Nokihara, K., Manaka, H., Iwanaga, T., Fujita, T., Okamoto, H., & Yanaihara, N. (1986). PHI structural requirements for potentiation of glucose-induced insulin release. Peptides, 7(SUPPL. 1), 83-88. https://doi.org/10.1016/0196-9781(86)90169-5