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Originally published In Press as doi:10.1074/jbc.C100325200 on June 25, 2001

J. Biol. Chem., Vol. 276, Issue 32, 30183-30187, August 10, 2001
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The Human Type 2 Iodothyronine Deiodinase Is a Selenoprotein Highly Expressed in a Mesothelioma Cell Line*

Cyntia Curcio, Munira M. A. Baqui, Domenico Salvatore, Bertrand H. RihnDagger , Steve MohrDagger , John W. Harney, P. Reed Larsen, and Antonio C. Bianco§

From the Department of Medicine, Thyroid Division, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115 and Dagger  Institut National de Recherche et de Securite, 54501 Vandoeuvre Cedex, France

Types 1 and 3 iodothyronine deiodinases are known to be selenocysteine-containing enzymes. Although a putative human type 2 iodothyronine deiodinase (D2) gene (hDio2) encoding a similar selenoprotein has been identified, basal D2 activity is not selenium (Se)-dependent nor has D2 been labeled with 75Se. A human mesothelioma cell line (MSTO-211H) has recently been shown to have ~40-fold higher levels of hDio2 mRNA than mesothelial cells. Mesothelioma cell lysates activate thyroxine (T4) to 3,5,3'-triiodothyronine with typical characteristics of D2 such as low Km (T4), 1.3 nM, resistance to propylthiouracil, and a short half-life (~30 min). D2 activity is ~30-fold higher in Se-supplemented than in Se-depleted medium. An antiserum prepared against a peptide deduced from the Dio2 mRNA sequence precipitates a 75Se protein of the predicted 31-kDa size from 75Se-labeled mesothelioma cells. Bromoadenosine 3'5' cyclic monophosphate increases D2 activity and 75Se-p31 ~2.5-fold whereas substrate (T4) reduces both D2 activity and 75Se-p31 ~2-3-fold. MG132 or lactacystin (10 µM), inhibitors of the proteasome pathway by which D2 is degraded, increase both D2 activity and 75Se-p31 3-4-fold and prevent the loss of D2 activity during cycloheximide or substrate (T4) exposure. Immunocytochemical studies with affinity-purified anti-hD2 antibody show a Se-dependent increase in immunofluorescence. Thus, human D2 is encoded by hDio2 and is a member of the selenodeiodinase family accounting for its highly catalytic efficiency in T4 activation.

* This work was supported by National Institutes of Health Research Grants DK36256 and DK58538.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: Brigham and Women's Hospital, 77 Ave. Louis Pasteur, HIM Bldg. 550, Boston, MA 02115. Tel.: 617-525-5158; Fax: 617-731-4718; E-mail: abianco@rics.bwh.harvard.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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