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J Biol Chem, Vol. 274, Issue 39, 27529-27535, September 24, 1999
§,§,¶,
,¶,§
From the Departments of § Endocrinology and
¶ Pharmacology, University of Colorado Health Sciences Center,
Denver, Colorado 80262, Insulin-like growth factor-I (IGF-I) is known to
prevent apoptosis induced by diverse stimuli. The present study
examined the effect of IGF-I on the promoter activity of
bcl-2, a gene with antiapoptotic function. A luciferase
reporter driven by the promoter region of bcl-2 from Section of Endocrinology,
Veterans Affairs Medical Center, Denver, Colorado 80220, Molecular Immunology, SmithKline Beecham Pharmaceuticals, King
of Prussia, Pennsylvania 19406, and the ** Department of
Medicine, Stanford University School of Medicine,
Stanford, California 94305
1640
to 1287 base pairs upstream of the translation start site containing
a cAMP-response element was used in transient transfection assays.
Treatment of PC12 cells with IGF-I enhanced the bcl-2
promoter activity by 2.3-fold, which was inhibited significantly
(p < 0.01) by SB203580, an inhibitor of p38
mitogen-activated protein kinase (MAPK). Cotransfection of the
bcl-2 promoter with MAPK kinase 6 and the 
isozyme of p38 MAPK resulted in 2-3-fold increase in the reporter activity. The
dominant negative form of MAPKAP-K3, a downstream kinase activated by
p38 MAPK, and the dominant negative form of cAMP-response
element-binding protein, inhibited the reporter gene activation by
IGF-I and p38 MAPK significantly (p < 0.01). IGF-I
increased the activity of p38 MAPK introduced into the cells by
adenoviral infection. Thus, we have characterized a novel signaling
pathway (MAPK kinase 6/p38 MAPK/MAPKAP-K3) that defines a
transcriptional mechanism for the induction of the antiapoptotic
protein Bcl-2 by IGF-I through the nuclear transcription factor
cAMP-response element-binding protein in PC12 cells.
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