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(Received for publication, August 5, 1996, and in revised form, November 26, 1996)
From The Hormel Institute, University of Minnesota,
Austin, Minnesota 55912
Phorbol esters, which activate isoforms of
protein kinase C, are general activators of the transcription factor
activated protein 1 (AP-1). The pathway involved in this signal
transduction is not very clear. Currently, little is known about
whether phosphatidylinositol-3 (PI-3) kinase plays any role in phorbol
ester 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced
signal transduction. We demonstrate here that TPA not only has markedly
synergistic effects on insulin-induced PI-3 kinase activity, but it
also can induce PI-3 kinase activity and the PI-3 phosphates by itself.
We also found that insulin, a PI-3 kinase activator, enhanced
TPA-induced AP-1 trans-activation and transformation in JB6
promotion-sensitive cells. Furthermore, wortmannin and LY294002,
two PI-3 kinase inhibitors, markedly decreased AP-1
activity induced by insulin, TPA, or TPA and insulin and inhibited JB6
promotion-sensitive cell transformation induced by TPA or TPA and
insulin. Most importantly, constitutive overexpression of the dominant
negative PI-3 kinase P85 mutants completely blocked insulin- or
TPA-induced AP-1 trans-activation and TPA-induced cell transformation.
All evidence from present studies suggests that PI-3 kinase acts as a
mediator in TPA-induced AP-1 activation and transformation in JB6
cells.
Volume 272, Number 7,
Issue of February 14, 1997
pp. 4187-4194
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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