Evidence for intriguingly complex transcription of human thioredoxin reductase 1

Free Radical Biology and Medicine

Volumn 36, Issue 5, 2004, Pages 641-656

  Rundlöf, Anna Klara ^a   Janard, Magnus ^a   Miranda Vizuete, Antonio ^a   Arner, Elias S J ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Alternative splicing; Free radicals; Promoter; Sp1; Sp3; Thioredoxin reductase

Indexed keywords

COMPLEMENTARY DNA; GLUTAREDOXIN; ISOENZYME; OCTAMER TRANSCRIPTION FACTOR 1; THIOREDOXIN; THIOREDOXIN REDUCTASE; THIOREDOXIN REDUCTASE 1; TRANSCRIPTION FACTOR SP1; TRANSCRIPTION FACTOR SP3; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CELL TYPE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; GENETIC TRANSCRIPTION; HELA CELL; HUMAN; HUMAN CELL; LUNG CARCINOMA; MITOCHONDRION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DOMAIN; RNA SPLICING; UNINDEXED SEQUENCE; UTERINE CERVIX CANCER;

EID: 1242338754     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2003.12.004     Document Type: Article

References (46)

1. Arnér E.S.J., Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267:2000;6102-6109.
2. Nordberg J., Arnér E.S.J. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic. Biol. Med. 31:2001;1287-1312.
3. Tamura T., Stadtman T.C. A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proc. Natl. Acad. Sci. USA. 93:1996;1006-1011.
4. Gladyshev V.N., Jeang K.-T., Stadtman T.C. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proc. Natl. Acad. Sci. USA. 93:1996;6146-6151.
5. Zhong L., Arnér E.S.J., Ljung J., Åslund F., Holmgren A. Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue. J. Biol. Chem. 273:1998;8581-8591.
6. Zhong L., Holmgren A. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. J. Biol. Chem. 275:2000;18121-18128.
7. Zhong L., Arnér E.S.J., Holmgren A. Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proc. Natl. Acad. Sci. USA. 97:2000;5854-5859.
8. Holmgren A. Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction. J. Biol. Chem. 252:1977;4600-4606.
9. Arnér E.S.J., Nordberg J., Holmgren A. Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. Biochem. Biophys. Res. Commun. 225:1996;268-274.
10. Kumar S., Björnstedt M., Holmgren A. Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen. Eur. J. Biochem. 207:1992;435-439.
11. Holmgren A., Lyckeborg C. Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductase. Proc. Natl. Acad. Sci. USA. 77:1980;5149-5152.
12. Björnstedt M., Hamberg M., Kumar S., Xue J., Holmgren A. Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols. J. Biol. Chem. 270:1995;11761-11764.
13. Sun Q.A., Wu Y., Zappacosta F., Jeang K.T., Lee B.J., Hatfield D.L., Gladyshev V.N. Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases. J. Biol. Chem. 274:1999;24522-24530.
14. Miranda-Vizuete A., Damdimopoulos A.E., Pedrajas J.R., Gustafsson J.Å., Spyrou G. Human mitochondrial thioredoxin reductase cDNA cloning, expression, and genomic organization. Eur. J. Biochem. 261:1999;405-412.
15. Lee S.R., Kim J.R., Kwon K.S., Yoon H.W., Levine R.L., Ginsburg A., Rhee S.G. Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver. J. Biol. Chem. 274:1999;4722-4734.
16. Sun Q.A., Kirnarsky L., Sherman S., Gladyshev V.N. Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems. Proc. Natl. Acad. Sci. USA. 98:2001;3673-3678.
17. Fujiwara N., Fujii T., Fujii J., Taniguchi N. Functional expression of rat thioredoxin reductase: selenocysteine insertion sequence element is essential for the active enzyme. Biochem. J. 340:1999;439-444.
18. Gasdaska J.R., Harney J.W., Gasdaska P.Y., Powis G., Berry M.J. Regulation of human thioredoxin reductase expression and activity by 3′-untranslated region selenocysteine insertion sequence and mRNA instability elements. J. Biol. Chem. 274:1999;25379-25385.
19. Kawai H., Ota T., Suzuki F., Tatsuka M. Molecular cloning of mouse thioredoxin reductases. Gene. 242:2000;321-330.
20. Lescure A., Gautheret D., Carbon P., Krol A. Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J. Biol. Chem. 274:1999;38147-38154.
21. Koishi R., Kawashima I., Yoshimura C., Sugawara M., Serizawa N. Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102. J. Biol. Chem. 272:1997;2570-2577.
22. Chen C.Y., Shyu A.B. AU-rich elements: characterization and importance in mRNA degradation. Trends Biochem. Sci. 20:1995;465-470.
23. Rozell B., Hansson H.A., Luthman M., Holmgren A. Immunohistochemical localization of thioredoxin and thioredoxin reductase in adult rats. Eur. J. Cell Biol. 38:1985;79-86.
24. Gasdaska J.R., Gasdaska P.Y., Gallegos A., Powis G. Human thioredoxin reductase gene localization to chromosomal position 12q23-q24.1 and mRNA distribution in human tissue. Genomics. 37:1996;257-259.
25. Berggren M., Gallegos A., Gasdaska J.R., Gasdaska P.Y., Warneke J., Powis G. Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia. Anticancer Res. 16:1996;3459-3466.
26. Rundlöf A.-K., Carlsten M., Arnér E.S.J. The core promoter of human thioredoxin reductase 1: cloning, transcriptional activity, and Oct1, Sp1, and Sp3 binding reveal a housekeeping-type promoter for the AU-rich element-regulated gene. J. Biol. Chem. 376:2001;30542-30551.
27. Swick A.G., Blake M.C., Kahn J.W., Azizkhan J.C. Functional analysis of GC element binding and transcription in the hamster dihydrofolate reductase gene promoter. Nucleic Acids Res. 17:1989;9291-9304.
28. Jensen D.E., Black A.R., Swick A.G., Azizkhan J.C. Distinct roles for Sp1 and E2F sites in the growth/cell cycle regulation of the DHFR promoter. J. Cell. Biochem. 67:1997;24-31.
29. Ryan A.K., Rosenfeld M.G. POU domain family values: flexibility, partnerships, and developmental codes. Genes Dev. 11:1997;1207-1225.
30. Rundlöf A.K., Carlsten M., Giacobini M.M., Arnér E.S.J. Prominent expression of the selenoprotein thioredoxin reductase in the medullary rays of the rat kidney and thioredoxin reductase mRNA variants differing at the 5′ untranslated region. Biochem. J. 347:2000;661-668.
31. Sun Q.A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N. Heterogeneity within animal thioredoxin reductases. Evidence for alternative first exon splicing. J. Biol. Chem. 276:2001;3106-3114.
32. Osborne S.A., Tonissen K.F. Genomic organisation and alternative splicing of mouse and human thioredoxin reductase 1 genes. BMC Genomics. 2:2001;10.
33. Wein H.M., Bruford E.A., Lovering R.C., Lush M.J., Wright M.W., Povey S. Guidelines for human gene nomenclature. Genomics. 79:2002;464-470.
34. Luthman M., Holmgren A. Rat liver thioredoxin and thioredoxin reductase: purification and characterization. Biochemistry. 21:1982;6628-6633.
35. Oblong J.E., Gasdaska P.Y., Sherrill K., Powis G. Purification of human thioredoxin reductase: properties and characterization by absorption and circular dichroism spectroscopy. Biochemistry. 32:1993;7271-7277.
36. Hintze K.J., Wald K.A., Zeng H., Jeffery E.H., Finley J.W. Thioredoxin reductase in human hepatoma cells is transcriptionally regulated by sulforaphane and other electrophiles via an antioxidant response element. J. Nutr. 133:2003;2721-2727.
37. Sadek C.M., Jimenez A., Damdimopoulos A.E., Kieselbach T., Nord M., Gustafsson J.A., Spyrou G., Davis E.C., Oko R., van der Hoorn F.A., Miranda-Vizuete A. Characterization of human thioredoxin-like 2. A novel microtubule-binding thioredoxin expressed predominantly in the cilia of lung airway epithelium and spermatid manchette and axoneme. J. Biol. Chem. 278:2003;13133-13142.
38. Miranda-Vizuete A., Ljung J., Damdimopoulos A.E., Gustafsson J.A., Oko R., Pelto-Huikko M., Spyrou G. Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa. J. Biol. Chem. 276:2001;31567-31574.
39. Miranda-Vizuete A., Tsang K., Yu Y., Jimenez A., Pelto-Huikko M., Flickinger C.J., Sutovsky P., Oko R. Cloning and developmental analysis of murid spermatid-specific thioredoxin-2 (Sptrx-2), a novel sperm fibrous sheath protein and autoantigen. J. Biol. Chem. 278(45):2003;44874-44885.
40. Sadek C.M., Damdimopoulos A.E., Pelto-Huikko M., Gustafsson J.A., Spyrou G., Miranda-Vizuete A. Sptrx-2, a fusion protein composed of one thioredoxin and three tandemly repeated NDP-kinase domains, is expressed in human testis germ cells. Genes Cells. 6:2001;1077-1090.
41. Yu Y., Oko R., Miranda-Vizuete A. Developmental expression of spermatid-specific thioredoxin-1 protein: transient association to the longitudinal columns of the fibrous sheath during sperm tail formation. Biol. Reprod. 67:2002;1546-1554.
42. Agorio A., Chalar C., Cardozo S., Salinas G. Alternative mRNAs arising from trans-splicing code for mitochondrial and cytosolic variants of Echinococcus granulosus thioredoxin glutathione reductase. J. Biol. Chem. 278:2003;12920-12928.
43. Ladd A.N., Cooper T.A. Finding signals that regulate alternative splicing in the post-genomic era. Genome Biol. 3:2002;. reviews0008.
44. Black D.L. Mechanisms of alternative pre-messenger RNA splicing. Annu. Rev. Biochem. 72:2003;291-336.
45. Stamm S. Signals and their transduction pathways regulating alternative splicing: a new dimension of the human genome. Hum. Mol. Genet. 11:2002;2409-2416.
46. Venables J.P. Alternative splicing in the testes. Curr. Opin. Genet. Dev. 12:2002;615-619.