Mammalian thioredoxin reductase 1: Roles in redox homoeostasis and characterization of cellular targets

Biochemical Journal

Volumn 430, Issue 2, 2010, Pages 285-293

  Turanov, Anton A ^a,b   Kehr, Sebastian ^a,d   Marino, Stefano M ^a,b   Min Hyuk, Y O O ^c   Carlson, Bradley A ^c   Hatfield, Dolph L ^c   Gladyshev, Vadim N ^a,b  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b BRIGHAM AND WOMEN S HOSPITAL   (United States)

^c NATIONAL CANCER INSTITUTE   (United States)

^d JUSTUS LIEBIG UNIVERSITY   (Germany)

Author keywords

Cellular target; Redox control; Thioredoxin; Thioredoxin reductase 1

Indexed keywords

BODY FLUIDS; HYDROGEN PEROXIDE; LIVER; MAMMALS; RESINS; SUBSTRATES;

AFFINITY RESINS; BIOLOGICAL SAMPLES; CELLULAR TARGETS; CELLULAR THIOLS; CYTOSOLIC; DIAMIDES; GLUTATHIONE REDUCTASE; HOMOEOSTASIS; IN-VITRO ASSAYS; IN-VIVO; MOLECULAR TARGETS; MOUSE LIVER; MOUSE SERUM; OXIDIZED STATE; PROTEIN SUBSTRATE; RAT BRAIN; REDOX CONTROL; REDOX PAIRS; REDOX REGULATION; SELENOCYSTEINE; SELENOCYSTEINE TRNA; SUBSTRATE SPECIFICITY; THIOREDOXIN REDUCTASE; THIOREDOXINS;

PROTEINS;

DIAMIDE; HYDROGEN PEROXIDE; PROTEIN; RESIN; SELENOCYSTEINE; THIOREDOXIN 1; THIOREDOXIN REDUCTASE 1; PROTEIN BINDING; THIOREDOXIN; THIOREDOXIN REDUCTASE;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; BINDING AFFINITY; BRAIN; CELL; CONTROLLED STUDY; CYTOSOL; HOMEOSTASIS; LIVER; LIVER FUNCTION; MAMMAL; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN SYNTHESIS; PROTEIN TARGETING; RAT; SERUM; 3T3 CELL LINE; ANIMAL; CHEMISTRY; CONFORMATION; ENZYME SPECIFICITY; GENETICS; HUMAN; KNOCKOUT MOUSE; METABOLISM; OXIDATION REDUCTION REACTION;

MAMMALIA; MUS; RATTUS;

ANIMALS; HOMEOSTASIS; HUMANS; LIVER; MICE; MICE, KNOCKOUT; MOLECULAR CONFORMATION; NIH 3T3 CELLS; OXIDATION-REDUCTION; OXIDATIVE STRESS; PROTEIN BINDING; RATS; SUBSTRATE SPECIFICITY; THIOREDOXIN REDUCTASE 1; THIOREDOXIN-DISULFIDE REDUCTASE; THIOREDOXINS;

EID: 77956655098     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20091378     Document Type: Article

References (23)

1. Holmgren, A. and Bjornstedt, M. (1995) Thioredoxin and thioredoxin reductase. Methods Enzymol. 252, 199-208
2. Gromer, S., Urig, S. and Becker, K. (2004) The thioredoxin system: from science to clinic. Med. Res. Rev. 24, 40-89
3. Mustacich, D. and Powis, G. (2000) Thioredoxin reductase. Biochem. J. 346, 1-8
4. Arner, E. S. (2009) Focus on mammalian thioredoxin reductases: important selenoproteins with versatile function. Biochim. Biophys. Acta 1790, 495-526
5. Zhong, L. and Holmgren, A. (2000) Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J. Biol. Chem. 275, 18121-18128
6. Lee, S. R., Kim, J. R., Kwon, K. S., Yoon, H. W., Levine, R. L., Ginsburg, A. and Rhee, S. G. (1999) Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. J. Biol. Chem. 274, 4722-4734
7. Turanov, A. A., Su, D. and Gladyshev, V. N. (2006) Mouse mitochondrial thioredoxin reductase: characterization of alternative cytosolic forms and cellular targets. J. Biol. Chem. 281, 22953-22963
8. Sun, Q. A., Kirnarsky, L., Sherman, S. and Gladyshev, V. N. (2001) Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems. Proc. Natl. Acad. Sci. U.S.A. 98, 3673-3678
9. Su, D., Novoselov, S. V., Sun, Q. A., Moustafa, M. E., Zhou, Y., Oko, R., Hatfield, D. L. and Gladyshev, V.N. (2005) Mammalian selenoprotein thioredoxin/glutathione reductase: Roles in disulfide bond formation and sperm maturation. J. Biol. Chem. 280, 26491-26498
10. Arner, E. S. and Holmgren, A. (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267, 6102-6109
11. Matsui, M., Oshima, M., Oshima, H., Takaku, K., Maruyama, T., Yodoi, J. and Taketo, M. M. (1996) Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene. Dev. Biol. 178, 179-185
12. Nonn, L., Williams, R. R., Erickson, R. P. and Powis, G. (2003) The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice. Mol. Cell. Biol. 23, 916-922
13. Jakupoglu, C., Przemeck, G. K., Schneider, M., Moreno, S. G., Mayr, N., Hatzopoulos, A. K., de Angelis, M. H., Wurst, W., Bornkamm, G. W., Brielmeier, M. and Conrad, M. (2005) Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development. Mol. Cell. Biol. 25, 1980-1988
14. Conrad, M., Jakupoglu, C., Moreno, S. G., Lippl, S., Banjac, A., Schneider, M., Beck, H., Hatzopoulos, A. K., Just, U., Sinowatz, F. et al. (2004) Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development and heart function. Mol. Cell. Biol. 24, 9414-9223
15. Holmgren, A. (2006) Selenoproteins in thioredoxin system. In Selenium. Its Molecular Biology and Role in Human Health, 2nd edition (Hatfield, D. L., Berry, M. J. and Gladyshev V. N., eds), pp. 183-194, Springer, New York
16. Arner, E. S., Sarioglu, H., Lottspeich, F., Holmgren, A. and Böck, A. (1999) High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes. J. Mol. Biol. 292, 1003-1016
17. Yoo, M. H., Xu, X. M., Turanov, A. A., Carlson, B. A., Gladyshev, V. N. and Hatfield, D. L. (2007) A new strategy for assessing selenoprotein function: siRNA knockdown/knock-in targeting the 3′-UTR. RNA 13, 1-9
18. Carlson, B. A., Novoselov, S. V., Kumaraswamy, E., Lee, B. J., Anver, M. R., Gladyshev, V. N. and Hatfield, D. L. (2004) Specific excision of the selenocysteine tRNA[Ser]Sec (Trsp) gene in mouse liver demonstrates an essential role of selenoproteins in liver function. J. Biol. Chem. 279, 8011-8017
19. Okuyama, H., Son, A., Ahsan, M. K., Masutani, H., Nakamura, H. and Yodoi, J. (2008) Thioredoxin and thioredoxin binding protein 2 in the liver. IUBMB Life 60, 656-660
20. Nakamura, H., Masutani, H. and Yodoi, J. (2006) Extracellular thioredoxin and thioredoxin-binding protein 2 in control of cancer. Semin. Cancer Biol. 16, 444-451
21. Cheng, Q., Sandalova, T., Lindqvist, Y. and Arner, E.S. (2009) Crystal structure and catalysis of the selenocysteine thioredoxin reductase 1. J. Biol. Chem. 284, 3998-4008
22. Patenaude, A., Ven Murthy, M. R. and Mirault, M. E. (2004) Mitochondrial thioredoxin system: effects of TrxR2 overexpression on redox balance, cell growth, and apoptosis. J. Biol. Chem. 279, 27302-27314
23. Chen, Y., Cai, J. and Jones, D. P. (2006) Mitochondrial thioredoxin in regulation of oxidant-induced cell death. FEBS Lett. 580, 6596-6602 (Pubitemid 44830129)