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Originally published In Press as doi:10.1074/jbc.M002354200 on July 10, 2000

J. Biol. Chem., Vol. 275, Issue 41, 31609-31615, October 13, 2000
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Thyrotropin-releasing Hormone and Epidermal Growth Factor Regulate Iron-regulatory Protein Binding in Pituitary Cells via Protein Kinase C-dependent and -independent Signaling Pathways*

Andrew M. ThomsonDagger , Jack T. Rogers§, and Peter J. LeedmanDagger

From the Dagger  Laboratory for Cancer Medicine and University Department of Medicine, University of Western Australia, Western Australian Institute for Medical Research, Royal Perth Hospital, Perth, Western Australia 6000, Australia and the § Genetics and Aging Unit, Massachusetts General Hospital (East), Harvard Medical School, Charlestown, Massachusetts 02129

Intracellular iron homeostasis is regulated, in part, by interactions between iron-regulatory proteins (IRP1 and IRP2) and iron-responsive elements (IREs) in ferritin and transferrin receptor mRNAs. In addition to iron, cellular oxidative stress induced by H2O2, nitric oxide, and hypoxia, and hormonal activation by thyroid hormone and erythropoeitin have each been shown to regulate IRP binding to IREs. Hormonal signals, in particular mediated through protein kinase C (PKC), play a central role in the modulation of IRP/IRE interactions since phorbol esters were shown to activate IRP binding (Eisenstein, R. S., Tuazon, P. T., Schalinske, K. L., Anderson, S. A., and Traugh, J. A. (1993) J. Biol. Chem. 268, 27363-27370). In pituitary thyrotrophs (TtT97), we found that thyrotropin releasing hormone (TRH) and epidermal growth factor (EGF) increased IRP binding to a ferritin IRE, dependent on PKC and mitogen-activated protein kinase (MAPK) activity. In contrast, TRH and EGF decreased IRP binding in pituitary lactotrophs (GH3), despite activation of PKC and MAPK. IRP1 and IRP2 levels remained constant and IRP2 binding was predominant throughout. TRH and EGF markedly decreased IRP binding in MAPK kinase inhibitor-treated GH3 cells, whereas, they increased IRP binding in phosphatase inhibitor-treated GH3 cells. IRE-dependent CAT reporter translational expression closely reflected IRP binding to the ferritin IRE in both GH3 and TtT97 cells. Interestingly, ferritin protein levels were regulated similarly by TRH in both cell lines. These data link two different cell receptor systems to common signaling pathways that regulate IRP binding and ferritin expression. Remarkably, for TRH and EGF, these effects may be PKC-dependent or -independent determined by the cell type.

* This work was supported in part by grants from the Medical Research Fund of Western Australia, the Raine Medical Research Foundation of Western Australia, and the Royal Perth Hospital Medical Research Foundation (to P. J. L.). The work was also supported by grants from the American Federation for Aging Research, the Institute for the Study of Aging (ISOA), and an RO3 pilot grant from the NIA, National Institutes of Health (to J. T. R.).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.

To whom correspondence should be addressed: University Dept. of Medicine, Royal Perth Hospital, Box X2213 GPO, Perth, Western Australia 6001, Australia. Tel.: 61-89-2240323; Fax: 61-89-2240246; E-mail: peterl@cyllene.uwa.edu.au.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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