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J Biol Chem, Vol. 274, Issue 50, 36015-36024, December 10, 1999

Growth Hormone-induced Alteration in ErbB-2 Phosphorylation Status in 3T3-F442A Fibroblasts*

Sung-Oh KimDagger §, Jon C. D. Houtman||, Jing JiangDagger **, J. Michael RuppertDagger Dagger , Paul J. Bertics, and Stuart J. FrankDagger §**§§

From the Department of Medicine, Divisions of Dagger  Endocrinology and Metabolism and Dagger Dagger  Hematology/Oncology and the § Department of Cell Biology, University of Alabama at Birmingham, the ** Veterans Affairs Medical Center, Birmingham, Alabama 35294, and the  Department of Biomolecular Chemistry, University of Wisconsin Medical School, Madison, Wisconsin 53706

The growth hormone receptor (GHR), a cytokine receptor superfamily member, requires the JAK2 tyrosine kinase for signaling. We now examine functional interactions between growth hormone (GH) and epidermal growth factor (EGF) in 3T3-F442A fibroblasts. Although EGF enhanced ErbB-2 tyrosine phosphorylation, GH, while causing retardation of its migration on SDS-polyacrylamide gel electrophoresis, decreased ErbB-2's tyrosine phosphorylation. GH-induced retardation was reversed by treatment of anti-ErbB-2 precipitates with both alkaline phosphatase and protein phosphatase 2A, suggesting that GH induced serine/threonine phosphorylation of ErbB-2. Both GH-induced shift in ErbB-2 migration and GH-induced MAP kinase activation were unaffected by a protein kinase C inhibitor but were blocked by the mitogen-activated protein kinase/extracellular signal-regulated kinase kinase 1 (MEK1) inhibitor, PD98059. Notably, leukemia inhibitory factor, but not interferon-gamma , also promoted ErbB-2 shift and mitogen-activated protein kinase activation. Cotreatment with EGF and GH versus EGF alone resulted in a 35% decline in acute ErbB-2 tyrosine 1248 autophosphorylation, a marked decline (approximately 50%) in DNA synthesis, and substantially decreased cyclin D1 expression. We conclude that in 3T3-F442A cells, 1) the GH-induced decrease in ErbB-2 tyrosine phosphorylation correlates with MEK1/mitogen-activated protein kinase activity and 2) GH antagonizes EGF-induced DNA synthesis and cyclin D1 expression in a pattern consistent with its alteration in ErbB-2 phosphorylation status.

* This work was supported in part by National Institutes of Health (NIH) Grants DK46395 (to S. J. F.), GM53271 (to P. J. B.), and CA65686 (to J. M. R.) and a VA Merit Review award (to S.J.F.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| Supported in part by NIH Grant T32HD07259.

§§ To whom correspondence should be addressed: University of Alabama at Birmingham, Rm. 756, DREB, UAB Station, Birmingham, AL 35294. Tel.: 205-934-9856; Fax: 205-934-4389; E-mail: frank@endo.dom.uab.edu.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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