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J. Biol. Chem., Vol. 278, Issue 10, 8106-8111, March 7, 2003
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From the Steroid hormone biosynthesis in the adrenal
cortex is controlled by adrenocorticotropin (ACTH), which increases
intracellular cAMP, resulting in the activation of
cAMP-dependent protein kinase(PKA) and
subsequent increase in steroidogenic gene transcription. We have found
that a dual-specificity phosphatase is essential for conveying
ACTH/cAMP-stimulated transcription of several steroidogenic genes in
the human adrenal cortex. In the present study, the role of
mitogen-activated protein kinase phosphatase-1 (MKP-1), a nuclear dual-specificity phosphatase, in the transcriptional activation of
human CYP17 (hCYP17) in H295R human adrenocortical cells is established. Stimulation of H295R cells with dibutyryl-cAMP
(Bt2cAMP) induces MKP-1 mRNA and protein expression
within 30 min of exposure. In transient-transfection studies,
transcriptional activity of an hCYP17 promoter-reporter construct was
increased by Bt2cAMP and by overexpression of PKA or MKP-1.
Furthermore, PKA phosphorylated an MKP-1-glutathione
S-transferase fusion protein in in vitro assays and Bt2cAMP increased 32P associated
with MKP-1 that was immunoprecipitated from H295R cells. Finally,
silencing MKP-1 expression using antisense oligonucleotides attenuated
cAMP-stimulated hCYP17 expression, whereas silencing of ERK1/2
increased hCYP17 expression. These findings demonstrate integral roles
for MKP-1 and ERK1/2 via regulation of the phosphorylation state of
steroidogenic factor-1 (SF-1) in mediating
ACTH/cAMP-dependent transcription of hCYP17, thereby
maintaining the balance between transcriptional activation and repression.
cAMP-dependent Protein Kinase Enhances CYP17 Transcription via
MKP-1 Activation in H295R Human Adrenocortical Cells*
§ and School of Biology, Georgia Institute of
Technology, Atlanta, Georgia 30332-0230 and the ¶ Department of
Biochemistry and Center in Toxicology, Vanderbilt University School of
Medicine, Nashville, Tennessee 37232-0146
*
This work was supported by National Institutes of Health
Grants DK28350 and ES00267 (to M. R. W.), a UNCF/Merck Science
Initiative Postdoctoral Fellowship (to M. B. S.), and National
Institutes of Health Postdoctoral Training Grant CA09582 (to
M. B. S.).
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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