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Originally published In Press as doi:10.1074/jbc.M301362200 on April 7, 2003

J. Biol. Chem., Vol. 278, Issue 25, 22696-22702, June 20, 2003
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Acute Control of Insulin-like Growth Factor-I Gene Transcription by Growth Hormone through Stat5b*

Joachim Woelfle, Julia Billiard and Peter Rotwein {ddagger}

From the Molecular Medicine Division, Department of Medicine, Oregon Health & Science University, Portland, Oregon 97239-3098

Many of the effects of growth hormone (GH) are mediated by insulin-like growth factor-I (IGF-I), a secreted peptide whose gene transcription is induced by GH by unknown mechanisms. Recent studies in mice have implicated Stat5b as part of a GH-regulated somatic growth pathway, because mice lacking this transcription factor show diminished growth rates and a decline in serum IGF-I levels. To test the role of Stat5b in GH-stimulated IGF-I gene expression, we have delivered modified versions of the protein to pituitary-deficient male rats by quantitative adenovirus-mediated gene transfer. In pilot studies in cell culture, both constitutively active and dominant-negative Stat5b appropriatelyregulatedtranscriptionfromaGH-responsiveStat5-dependent reporter gene. After in vivo expression, neither protein impaired GH-induced activation of cytoplasmic signaling pathways or blocked nuclear accumulation of Stats 1 and 3 in the liver, the major site of IGF-I production. Dominant-negative Stat5b completely prevented GH-stimulated IGF-I gene transcription, whereas constitutively active Stat5b led to robust IGF-I gene expression in the absence of hormone. An adenovirus encoding enhanced green fluorescent protein was without effect. Similar results were seen with the GH-responsive Stat5b-dependent Spi 2.1 gene, whereas GH-stimulated c-fos transcription was minimally altered. These results establish Stat5b as a key component of GH-stimulated IGF-I gene transcription, and they demonstrate the feasibility of using in vivo gene transfer to target distinct components of hormone-activated signaling pathways.

Received for publication, February 7, 2003 , and in revised form, March 21, 2003.

* This work was supported by National Institutes of Health Grants 5RO1DK37449 (to P. R.) and 5F32DK09802 (to J. B.) and by a Research Fellowship of the European Society for Pediatric Endocrinology, sponsored by Novo Nordisk and the Eli Lilly International Foundation (to J. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} To whom correspondence should be addressed: Oregon Health & Science University, Molecular Medicine Division, 3181 S.W. Sam Jackson Park Rd., Mail code HRC3, Portland, OR 97239-3098. Tel.: 503-494-0536; Fax: 503-494-7368; E-mail: rotweinp{at}ohsu.edu.


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