Identification by differential display PCR of the selenoprotein thioredoxin reductase as a 1α,25(OH)2-vitamin D3-responsive gene in human osteoblasts - Regulation by selenite

BioFactors

Volumn 7, Issue 4, 1998, Pages 299-310

  Schutze N ^a   Bachthaler, M ^a   Lechner, A ^a   Kohrle J ^a   Jakob, F ^a,b  

^a UNIVERSITY OF WÜRZBURG   (Germany)

^b Klinische Forschergruppe   (Germany)

Author keywords

ddPCR; Osteoblasts; Selenoproteins; Thioredoxin reductase; Vitamin D

Indexed keywords

CALCITRIOL; SELENITE; SELENOPROTEIN; THIOREDOXIN REDUCTASE;

ARTICLE; BONE GROWTH; CALCIUM METABOLISM; CELL DIFFERENTIATION; HUMAN; HUMAN CELL; OSTEOBLAST; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; TARGET CELL;

EID: 0031800144     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520070402     Document Type: Article

References (59)

1. L.D. Arscott, S. Gromer, R.H. Schirmer, K. Becker and C.H. Williams, Jr., The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli, Proc. Natl. Acad. Sci. USA 94 (1997), 3621-3626.
2. 3, J. Cell Biochem. 56 (1994), 303-306.
3. D. Behne, C. Weiss-Nowak, M. Kalcklösch, C. Westphal, H. Gessner and A. Kyriakopoulos, Studies on the distribution and characteristics of new mammalian selenium-containing proteins, Analyst 120 (1995), 823-825.
4. M. Berggren, A. Gallegos, J.R. Gasdaska, P.Y. Gasdaska, J. Warneke and G. Powis, 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.
5. G. Bermano, F. Nicol, J.A. Dyer, R.A. Sunde, G.J. Beckett, J.R. Arthur and J.E. Hesketh, Tissue-specific regulation of selenoenzyme gene expression during selenium deficiency in rats, Biochem. J. 311 (1995), 425-430.
6. M.J. Berry and P.R. Larsen, Recognition of UGA as a selenocysteine codon in eucaryotes: a review of recent progress, Biochem. Soc. Trans. 21 (1993), 827-832.
7. R. Bouillon, W.H. Okamura and A.W. Norman, Structure-function relationships in the vitamin D endocrine system, Endocrine Rev. 16 (1995), 200-257.
8. M.M. Bradford, A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding, Anal. Biochem. 7 (1976), 248-254.
9. R. Brigelius-Flohé, K.D. Aumann, H. Blocker, G. Gross, M. Kiess, K.D. Kloppel, M. Maiorino, A. Roveri, R. Schuckelt, F. Ursini, E. Wingender and L. Flohé, Phospholipid-hydroperoxide glutathione peroxidase. Genomic DNA, cDNA, and deduced amino acid sequence, J. Biol. Chem. 269 (1994), 7342-7348.
10. R. Brigelius-Flohé, K. Lötzer, S. Maurer, M. Schultz and M. Leist, Utilisation of selenium from different chemical entities for selenoprotein biosynthesis by mammalian cell lines, Biofactors 5 (1995), 125-131.
11. R.F. Burk and K.E. Hill, Selenoprotein P. A selenium-rich extracellular glycoprotein, J. Nutr. 124 (1994), 1891-1897.
12. C.C. Chen, B.L. McCall and E.C. Moore, Purification of thioredoxin reductase from the Novikoff rat tumor, Prep. Biochem. 7 (1977), 165-177.
13. J.M. Chirgwin, A.E. Przybyla, R.J. MacDonald and W.J. Rutter, Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease, Biochemistry 18 (1979), 5294-5299.
14. P. Chomczynski and N. Sacchi, Single-step method of RNA isolation by acid guanidinium thiocyanate-phenolchloroform extraction, Anal. Biochem. 162 (1987), 156-159.
15. 3, Biochem. J. 316 (1996), 361-371.
16. M.J. Christensen, P.M. Cammack and C.D. Wray, Tissue specificity of selenoprotein gene expression in rats, J. Nutr. Biochem. 6 (1995), 367-372.
17. I. Dreher, T. Jakobs and J. Köhrle, Humanes Selenoprotein P: Promotorcharakterisierung und Expressionsmuster, in: Mineralstoffe und Spurenelemente - Molekularbiologie - Interaktion mit dem Hormonsystem - Analytik, J. Köhrle, ed., Wissenschaftliche Verlagsgesellschaft, Stuttgart, 1998, pp. 19-22.
18. I. Dreher, C. Schmutzler, F. Jakob and J. Köhrle, Trace Elem. Med. Biol. 11 (1997), 83-91.
19. H. Follmann and I. Häberlein, Thioredoxins: universal, yet specific thiol-disulfide redox cofactors, Biofactors 5 (1995), 147-156.
20. P.Y. Gasdaska, J.R. Gasdaska, S. Cochran and G. Powis, Cloning and sequencing of a human thioredoxin reductase, FEBS Lett. 373 (1995), 5-9.
21. V.N. Gladyshev, K.T. Jeang and T.C. Stadtman, 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.
22. M. Gross, M. Oertel and J. Köhrle, Differential selenium-dependent regulation of type I 5′-deiodinase and glutathione peroxidase in the porcine epithelial kidney cell line LLC-PK1, Biochem. J. 306 (1995), 851-856.
23. M.J. Guimarares, D. Peterson, A. Vicari, B.G. Cocks, N.G. Copeland, D.J. Gilbert, N.A. Jenkins, D.A. Ferrick, R.A. Kastelein, J.F. Bazan and A. Zlotnik, Identification of a novel selD homolog from eucaryotes, bacteria, and archae: is there an autoregulatory mechanism in selenocysteine metabolism, Proc. Natl. Acad. Sci. USA 93 (1996), 15 086-15 091.
24. S.A. Harris, R.J. Enger, B.L. Riggs and T.C. Spelsberg, Development and characterisation of a conditionally immortalised human fetal osteoblast cell line, J. Bone Miner. Res. 10 (1995), 178-186.
25. M.R. Haussler, P.W. Jurutka, J.C. Hsieh, P.D. Thompson, S.H. Selznick, C.A. Haussler and G.K. Whitfield, New understanding of the molecular mechanism of receptor-mediated genomic actions of the vitamin D hormone, Bone 17(2) (1995), 33S-38S.
26. K.E. Hill, G.W. McCollum, M.E. Boeglin and R.F. Burk, Thioredoxin reductase activity is decreased by selenium deficiency, Biochem. Biophys. Res. Comm. 234 (1997), 293-295.
27. K. Hirota, M. Matsui, S. Iwata, A. Nishiyama, K. Mori and J. Yodoi, AP-1 transcriptional activity is regulated by a direct association between thioredoxin and ref-1, Proc. Natl. Acad. Sci. USA 94 (1997), 3633-3638.
28. 3 and clinical applications, Bone 17(2) (1995), 107S-111S.
29. A. Holmgren, Thioredoxin and glutaredoxin systems, J. Biol. Chem. 264 (1989), 13 963-13 966.
30. A. Holmgren and M. Björnstedt, Thioredoxin and thioredoxin reductase, Methods Enzymol. 252 (1995), 199-208.
31. J. Köhrle, Thyroid hormone deiodinases - a selenoenzyme family acting as gate keepers to thyroid hormone action, Acta Med. Austriaca 1 (1996), 17-30.
32. J. Köhrle, Non-thyroidal health hazards of selenium deficiency, in: Thyroid and Trace Elements. 6th Thyroid Symposium, Graz, Austria, Blackwell Wissenschaft, Berlin, 1996, pp. 58-73.
33. R. Koishi, I. Kawashima, C. Yoshimura, M. Sugawara and N. Serizawa, Cloning and characterisation of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell-line KM-102, J. Biol. Chem. 272 (1997), 2570-2577.
34. L. Leist, B. Raab, S. Maurer, U. Rösick and R. Brigelius-Flohé, Conventional cell culture media does not adequately supply cells with antioxidants and thus facilitate peroxide-induced genotoxicity, Free Rad. Biol. Med. 21 (1996), 297-306.
35. J.B. Lian and G.S. Stein, Transcriptional control of vitamin D-regulated proteins, J. Cell Biochem. 49 (1992), 37-45.
36. P. Liang and A.B. Pardee, Differential display of eucaryotic messenger RNA by means of the polymerase chain reaction, Science 257 (1992), 967-970.
37. 3 leads to the induced differentiation of the myelomonocytic cell-line U937, Genes Development 10 (1996), 142-153.
38. M. Luthman and A. Holmgren, Rat liver thioredoxin and thioredoxin reductase: purification and characterisation, Biochemistry 21 (1982), 6628-6633.
39. L. Marcocci, L. Flohé and L. Packer, Evidence for a functional relevance of the selenocysteine residue in mammalian thioredoxin reductase, Biofactors 6 (1997), 351-358.
40. E. Martinez-Galisteo, C.A. Padilla, C. Garcia-Alfonso, J. Lopez-Barea and J.A. Barcena, Purification and properties of bovine thioredoxin system, Biochimie 75 (1993), 803-809.
41. A. Miranda-Vizuette and G. Spyrou, The novel oxidoreductase KDRF (KM-102-derived reductase-like factor) is identical with human thioredoxin reductase, Biochem. J. 325 (1997), 287-288.
42. G.R. Mundy, Cytokines and growth factors in the regulation of bone remodelling, J. Bone Miner. Res. 8(2) (1993), S505-S510.
43. 3 function as ligands for the D-binding protein, nuclear receptor and membrane receptor: a status report, J. Steroid Biochem. Mol. Biol. 56 (1996), 1-6.
44. J.E. Oblong, P.Y. Gasdaska, K. Sherril and G. Powis, Purification of human thioredoxin reductase: properties and characterisation by absorption and circular dicroism spectroscopy, Biochemistry 32 (1993), 7271-7277.
45. G.D. Roodman, Role of cytokines in the regulation of bone resorption, Calcif. Tissue Int. 53(1) (1993), S94-S98.
46. N. Schoene, V.C. Morris and P.D. Roath, Response of thioredoxin reductase (TR) activity to selenium (Se) supply, FASEB J. 11 (1997), A403.
47. K. Schwartz and C.M. Foltz, Selenium as an integral part of factor 3 against dietary necrotic liver degeneration, J. Am. Chem. Soc. 79 (1957), 3292-3293.
48. A. Scutt, H. Mayer and E. Wingender, New perspectives in the differentiation of bone-forming cells, Biofactors 4 (1992), 1-13.
49. G. Shaw and R. Kamen, A conserved AU sequence from the 3′-untranslated region of GM-CSF mRNA mediates selective mRNA degradation, Cell 46 (1986), 659-667.
50. Q. Shen, J.L. Leonard and P.E. Newburger, Structure and function of the selenium translation element in the 3′-un-translated region of human cellular glutathione peroxidase mRNA, RNA 1 (1995), 519-525.
51. T.C. Stadtman, Selenocysteine, Ann. Rev. Biochem. 65 (1996), 83-100.
52. S.A. Strugnell and H.F. Deluca, The vitamin D receptor - structure and transcriptional activation, Proc. Soc. Exp. Biol. Med. 215 (1997), 223-228.
53. R.A. Sunde, Intracellular glutathione peroxidases - structure, regulation, and function, in: Selenium in Biology and Human Health, R.F. Burk, ed., Springer, New York, 1994, pp. 45-77.
54. T. Tamura, V. Gladyshev, S.-Y. Liu and T.C. Stadtman, The mutual sparing effects of selenium and vitamin E in animal nutrition may be further explained by the discovery that mammalian thioredoxin reductase is a selenoenzyme, Biofactors 5 (1995), 99-102.
55. T. Tamura and T.C. Stadtman, A new selenoprotein from human lung adenocarcinoma cells. Purification, properties, and thioredoxin reductase activity, Proc. Natl. Acad. Sci. USA 93 (1996), 1006-1011.
56. M.L. Tsang and J.A. Weatherbee, Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured Hela cells, Proc. Natl. Acad. Sci. USA 78 (1981), 7478-7482.
57. F. Ursini, M. Maiorino, R. Brigelius-Flohé, K.D. Aumann, A. Roveri, D. Schomburg and L. Flohé, Diversity of glutathione peroxidases, Methods Enzymol. 252 (1995), 38-53.
58. S.C. Vendeland, M.A. Beilstein, C.L. Chen, O.N. Jensen, E. Barofsky and P.D. Whanger, Purification and properties of selenoprotein W from rat muscle, J. Biol. Chem. 268 (1993), 17 103-17 107.
59. R. Walczak, E. Westhof, P. Carbon and A. Krol, A novel structural motif in the selencysteine insertion element of eucaryotic selenoprotein mRNAs, RNA 2 (1996), 367-379.