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J. Biol. Chem., Vol. 275, Issue 21, 15977-15984, May 26, 2000
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Glucose-stimulated Preproinsulin Gene Expression and Nuclear trans-Location of Pancreatic Duodenum Homeobox-1 Require Activation of Phosphatidylinositol 3-Kinase but Not p38 MAPK/SAPK2*

Imran RafiqDagger , Gabriela da Silva Xavier, Steven Hooper§, and Guy A. Rutter||

From the Department of Biochemistry, School of Medical Sciences, University Walk, University of Bristol, Bristol BS8 1TD, United Kingdom and the § Institute of Cancer Research, Chester Beatty Laboratories, 237 Fulham Road, London SW3 6JB, United Kingdom

Exposure of islet beta -cells to elevated glucose concentrations (30 versus 3 mM) prompts enhanced preproinsulin (PPI) gene transcription and the trans-location to the nucleoplasm of pancreatic duodenum homeobox-1 (PDX-1; Rafiq, I., Kennedy, H., and Rutter, G. A. (1998) J. Biol. Chem. 273, 23241-23247). Here, we show that in MIN6 beta -cells, over-expression of p110.CAAX, a constitutively active form of phosphatidylinositol 3-kinase (PI3K) mimicked the activatory effects of glucose on PPI promoter activity, whereas Delta p85, a dominant negative form of the p85 subunit lacking the p110-binding domain, and the PI3K inhibitor LY 294002, blocked these effects. Similarly, glucose-stimulated nuclear trans-location of endogenous PDX-1 was blocked by Delta p85 expression, and wortmannin or LY 294002 blocked the trans-location from the nuclear membrane to the nucleoplasm of epitope-tagged PDX-1.c-myc. By contrast, SB 203580, an inhibitor of stress-activated protein kinase-2 (SAPK2)/p38 MAP kinase, had no effect on any of the above parameters, and PPI promoter activity and PDX-1.c-myc localization were unaffected by over-expression of the upstream kinase MKK6 (MAP kinase kinase-6) or wild-type p38/SAPK2, respectively. Furthermore, no change in the activity of extracted p38/SAPK2 could be detected after incubation of cells at either 3 or 30 mM glucose. These data suggest that stimulation of PI3K is necessary and sufficient for the effects of glucose on PPI gene transcription, acting via a downstream signaling pathway that does not involve p38/SAPK2.

* This work was supported by grants from the Medical Research Council, U.K., The Wellcome Trust, and the British Diabetic Association. Work at the Chester Beatty Institute was supported by the Cancer Research Campaign.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by a British Diabetic Association post-graduate Research Scholarship.

|| To whom correspondence should be addressed. Tel.: 44.117.928. 9724; Fax: 44.117.928.8274; E-mail: g.a.rutter@bris.ac.uk.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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