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Volume 272, Number 7, Issue of February 14, 1997 pp. 4187-4194
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Phosphatidylinositol-3 Kinase Is Necessary for 12-O-Tetradecanoylphorbol-13-acetate-induced Cell Transformation and Activated Protein 1 Activation

(Received for publication, August 5, 1996, and in revised form, November 26, 1996)

Chuanshu Huang , Patricia C. Schmid , Wei-Ya Ma , Harald H. O. Schmid and Zigang Dong

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.


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