Inositol hexakisphophate stimulates non-Ca2+-mediated and primes Ca2+-mediated exocytosis of insulin by activation of protein kinase C

A. M. Efanov, S. V. Zaitsev, P. O. Berggren

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

D-myo-inositol 1,2,3,4,5,6-hexakisphosphate (InsP6) formed via complex pathways of inositol phosphate metabolism, composes the main bulk of inositol polyphosphates in the cell. Relatively little is known regarding possible biological functions for InsP6. We now show that InsP6 can modulate insulin exocytosis in permeabilized insulin-secreting cells. Concentration of InsP6 above 20 μM stimulated insulin secretion at basal Ca2+-concentration (30 nM) and primed Ca2+-induced exocytosis (10 μM), both effects being due to activation of protein kinase C. Our results suggest that InsP6 can play an important modulatory role in the regulation of processes such as exocytosis in insulin-secreting cells. The specific role for InsP6 can then be to recruit secretory granules to the site of exocytosis.

Original languageEnglish
Pages (from-to)4435-4439
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number9
DOIs
StatePublished - Jan 1 1997
Externally publishedYes

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Exocytosis
Inositol
Protein Kinase C
Insulin
Insulin-Secreting Cells
Polyphosphates
Inositol Phosphates
Secretory Vesicles

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Inositol hexakisphophate stimulates non-Ca2+-mediated and primes Ca2+-mediated exocytosis of insulin by activation of protein kinase C. / Efanov, A. M.; Zaitsev, S. V.; Berggren, P. O.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, No. 9, 01.01.1997, p. 4435-4439.

Research output: Contribution to journalArticle

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