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J Biol Chem, Vol. 274, Issue 35, 24522-24530, August 27, 1999

Redox Regulation of Cell Signaling by Selenocysteine in Mammalian Thioredoxin Reductases

Qi-An SunDagger , Yalin Wu§, Francesca Zappacosta, Kuan-Teh Jeang§, Byeong Jae Lee**, Dolph L. HatfieldDagger Dagger , and Vadim N. GladyshevDagger

From the Dagger  Department of Biochemistry, University of Nebraska, Lincoln, Nebraska 68588, the § Laboratory of Molecular Microbiology, NIAID, National Institutes of Health, Bethesda, Maryland 20892, the  Laboratory of Molecular Structure, NIAID, National Institutes of Health, Rockville, Maryland 20852, the ** Laboratory of Molecular Genetics, Institute for Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea, and the Dagger Dagger  Basic Research Laboratory, NCI, National Institutes of Health, Bethesda, Maryland 20892

The intracellular generation of reactive oxygen species, together with the thioredoxin and glutathione systems, is thought to participate in redox signaling in mammalian cells. The activity of thioredoxin is dependent on the redox status of thioredoxin reductase (TR), the activity of which in turn is dependent on a selenocysteine residue. Two mammalian TR isozymes (TR2 and TR3), in addition to that previously characterized (TR1), have now been identified in humans and mice. All three TR isozymes contain a selenocysteine residue that is located in the penultimate position at the carboxyl terminus and which is encoded by a UGA codon. The generation of reactive oxygen species in a human carcinoma cell line was shown to result in both the oxidation of the selenocysteine in TR1 and a subsequent increase in the expression of this enzyme. These observations identify the carboxyl-terminal selenocysteine of TR1 as a cellular redox sensor and support an essential role for mammalian TR isozymes in redox-regulated cell signaling.

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


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