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J. Biol. Chem. 279 (5): 3142-3150

© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

Identification and Characterization of TRP14, a Thioredoxin-related Protein of 14 kDa

NEW INSIGHTS INTO THE SPECIFICITY OF THIOREDOXIN FUNCTION*

Woojin Jeong{ddagger}§¶, Hae Won Yoon{ddagger}||, Seung-Rock Lee{ddagger}**, , and Sue Goo Rhee{ddagger}{ddagger}{ddagger}

{ddagger}Laboratory of Cell Signaling, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 and the §Center for Cell Signaling Research, Ewha Women's University, Seoul 120-750, Korea

Abstract: We have identified and characterized a 14-kDa human thioredoxin (Trx)-related protein designated TRP14. This cytosolic protein was expressed in all tissues and cell types examined, generally in smaller amounts than Trx1. Although TRP14 contains five cysteines, only the two Cys residues in its WCPDC motif were exposed and redox sensitive. Unlike Trx1, which was an equally good substrate for both Trx reductase 1 (TrxR1) and TrxR2, oxidized TRP14 was reduced by TrxR1 but not by TrxR2. Biochemical characterization of TRP14 suggested that, like Trx1, TRP14 is a disulfide reductase; its active site cysteine is sufficiently nucleophilic with the pKa value of 6.1; and its redox potential (–257 mV) is similar to those of other cellular thiol reductants. However, although TRP14 reduced small disulfide-containing peptides, it did not reduce the disulfides of known Trx1 substrates, ribonucleotide reductase, peroxiredoxin, and methionine sulfoxide reductase. These results suggest that TRP14 and Trx1 might act on distinct substrate proteins.

Received for publication July 21, 2003. Revision received October 15, 2003.

* This work was supported in part by the Korean Science and Engineering Foundation Center of Excellence grant to the Center for Cell signaling Research at Ewha Women's University (to W. J.). 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.

Both authors contributed equally to this work.

|| Present address: Division of Applied Life Science (BK21 program), Gyeongsang National University, Jinju, Gyeongnam 660-701, Korea.

** Present address: Center for Cell Signaling Research, Ewha Women's University, Seoul 120-750, Korea.

{ddagger}{ddagger} To whom correspondence should be addressed: Bldg. 50, Room 3523, South Drive, MSC 8015, Bethesda, MD 20892. Tel.: 301-496-9646; Fax: 301-480-0357; E-mail: sgrhee{at}nih.gov.

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