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Volumn 52, Issue 11, 1996, Pages 1741-1747

Oxidative inactivation of thioredoxin as a cellular growth factor and protection by a Cys73→Ser mutation

Author keywords

growth factor; homodimer; oxidation; thioredoxin

Indexed keywords

CYSTEINE; DIMER; DITHIOTHREITOL; GROWTH FACTOR; MONOMER; MUTANT PROTEIN; OXIDIZING AGENT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SERINE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 0030582835     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(96)00595-3     Document Type: Article
Times cited : (71)

References (35)
  • 1
  • 2
    • 0020488534 scopus 로고
    • Rat liver chioredoxin and thioredoxin reductase: Purification and characterization
    • 2. Luthman M and Holmgren A, Rat liver chioredoxin and thioredoxin reductase: purification and characterization. Biochem 21: 6628-6633, 1982.
    • (1982) Biochem , vol.21 , pp. 6628-6633
    • Luthman, M.1    Holmgren, A.2
  • 3
    • 78651146370 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides VI. Isolation and characterization of thioredixon, the hydrogen donor from Escherichia coli B
    • 3. Laurent TC, Moore EC and Reichard P, Enzymatic synthesis of deoxyribonucleotides VI. Isolation and characterization of thioredixon, the hydrogen donor from Escherichia coli B. J Biol Chem 239: 3436-3444, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 3436-3444
    • Laurent, T.C.1    Moore, E.C.2    Reichard, P.3
  • 4
    • 0026644806 scopus 로고
    • Unfolding intermediates of the extracellular domain of the interferon gamma receptor
    • 4. Fountoulakis M, Unfolding intermediates of the extracellular domain of the interferon gamma receptor. J Biol Chem 267: 7095-7100, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 7095-7100
    • Fountoulakis, M.1
  • 5
    • 0027136038 scopus 로고
    • Disulfide formation in reduced tetanus toxin by thioredoxin: The pharmacological role of interchain covalent and noncovalent bonds
    • 5. Kistner A, Sanders D and Habermann E, Disulfide formation in reduced tetanus toxin by thioredoxin: The pharmacological role of interchain covalent and noncovalent bonds. Toxicon 31: 1423-1434, 1993.
    • (1993) Toxicon , vol.31 , pp. 1423-1434
    • Kistner, A.1    Sanders, D.2    Habermann, E.3
  • 6
    • 0023734861 scopus 로고
    • Reduced thioredoxin: A possible physiological cotactor for vitamin K epoxide reductase. Further support for an active site disulfide
    • 6. Silverman RB and Nandi DL, Reduced thioredoxin: A possible physiological cotactor for vitamin K epoxide reductase. Further support for an active site disulfide. Biochem Biophys Res Commun 155: 1248-1254, 1988.
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 1248-1254
    • Silverman, R.B.1    Nandi, D.L.2
  • 7
    • 0027217531 scopus 로고
    • Oxidoreductive regulation of nuclear factor KB: Involvement of a cellular reducing catalyst thioredoxin
    • 7. Hayashi T, Ueno Y and Okamoto T, Oxidoreductive regulation of nuclear factor KB: Involvement of a cellular reducing catalyst thioredoxin. J Biol Chem 268: 11380-11388, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 11380-11388
    • Hayashi, T.1    Ueno, Y.2    Okamoto, T.3
  • 8
    • 0028348239 scopus 로고
    • Distinct effects of glutathione disulfide on the nuclear transcription factors KB and the activator protein-1
    • 8. Galter D, Mihm S and Dröge W, Distinct effects of glutathione disulfide on the nuclear transcription factors KB and the activator protein-1. Eur J Biochem 221: 639-648, 1994.
    • (1994) Eur J Biochem , vol.221 , pp. 639-648
    • Galter, D.1    Mihm, S.2    Dröge, W.3
  • 9
    • 0021078605 scopus 로고
    • Evidence that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxin
    • 9. Grippo JF, Tienrungroj W, Dahmer MK, Housley PR and Pratt WB, Evidence that the endogenous heat-stable glucocorticoid receptor-activating factor is thioredoxin. J Biol Chem 258: 13658-13664, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 13658-13664
    • Grippo, J.F.1    Tienrungroj, W.2    Dahmer, M.K.3    Housley, P.R.4    Pratt, W.B.5
  • 10
    • 0024421652 scopus 로고
    • Human transcription factor IIIC (TFIIC). Purification, polypeptide structure, and the involvement of thiol groups in specific DNA binding
    • 10. Cromlish JA and Roeder RG, Human transcription factor IIIC (TFIIC). Purification, polypeptide structure, and the involvement of thiol groups in specific DNA binding. J Biol Chem 264: 18100-18109, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 18100-18109
    • Cromlish, J.A.1    Roeder, R.G.2
  • 11
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • 11. Freedman RB, Hirst TR and Tuite MF, Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci 19: 331-336, 1994.
    • (1994) Trends Biochem Sci , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 12
    • 0030499036 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia
    • in press
    • 12. Berggren M, Gallegos A, Gasdaska JR, Gasdaska PY, Warneke J and Powis G, Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia. Anticancer Res (in press).
    • Anticancer Res
    • Berggren, M.1    Gallegos, A.2    Gasdaska, J.R.3    Gasdaska, P.Y.4    Warneke, J.5    Powis, G.6
  • 13
    • 0027991841 scopus 로고
    • The predicted amino acid sequence of human thioredoxin is identical to that of the autocrine growth factor human adult T-cell derived factor (ADF): Thioredoxin mRNA is elevated in some human tumors
    • 13. Gasdaska PY, Oblong JE, Cotgreave IA and Powis G, The predicted amino acid sequence of human thioredoxin is identical to that of the autocrine growth factor human adult T-cell derived factor (ADF): Thioredoxin mRNA is elevated in some human tumors. Biochim Biophys Acta 1218: 292-296, 1994.
    • (1994) Biochim Biophys Acta , vol.1218 , pp. 292-296
    • Gasdaska, P.Y.1    Oblong, J.E.2    Cotgreave, I.A.3    Powis, G.4
  • 14
    • 0026563593 scopus 로고
    • Expression and growth-promoting effect of adult T-cell leukemia-derived factor. A human thioredoxin homologue in hepatocellular carcinoma
    • 14. Nakamura H, Masutani H, Tagaya Y, Yamauchi A, Inamoto Y, Nanbu Y, Fujii S, Ozawa K and Yodoi J, Expression and growth-promoting effect of adult T-cell leukemia-derived factor. A human thioredoxin homologue in hepatocellular carcinoma. Cancer 69: 2091-2097, 1992.
    • (1992) Cancer , vol.69 , pp. 2091-2097
    • Nakamura, H.1    Masutani, H.2    Tagaya, Y.3    Yamauchi, A.4    Inamoto, Y.5    Nanbu, Y.6    Fujii, S.7    Ozawa, K.8    Yodoi, J.9
  • 15
    • 0029778527 scopus 로고    scopus 로고
    • Transfection with human thioredoxin increases cell proliferation and a dominant negative mutant thioredoxin reverses the transformed phenotype of breast cancer cells
    • in press
    • 15. Gallegos A, Gasdaska JR, Goodman D, Gasdaska PY, Berggren M, Briehl MM and Powis G, Transfection with human thioredoxin increases cell proliferation and a dominant negative mutant thioredoxin reverses the transformed phenotype of breast cancer cells. Cancer Res (in press).
    • Cancer Res
    • Gallegos, A.1    Gasdaska, J.R.2    Goodman, D.3    Gasdaska, P.Y.4    Berggren, M.5    Briehl, M.M.6    Powis, G.7
  • 16
    • 0028304630 scopus 로고
    • Site-directed mutagenesis of active site cysteines in human thioredoxin produces competitive inhibitors of human thioredoxin reductase and elimination of mitogenic properties of thioredoxin
    • 16. Oblong JE, Berggren M, Gasdaska PY and Powis G, Site-directed mutagenesis of active site cysteines in human thioredoxin produces competitive inhibitors of human thioredoxin reductase and elimination of mitogenic properties of thioredoxin. J Biol Chem 269: 117H-11720, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 11714-11720
    • Oblong, J.E.1    Berggren, M.2    Gasdaska, P.Y.3    Powis, G.4
  • 17
    • 0025066731 scopus 로고
    • Adult T-cell leukemia-derived factor/ Thioredoxin produced by both human T-lymphotropic virus type 1 and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergized with interleukin-1 and interleukin-2
    • 17. Wakasugi N, Tagaya Y, Wakasugi A, Mitsui M, Maeda M, Yodoi J and Tursz T, Adult T-cell leukemia-derived factor/ Thioredoxin produced by both human T-lymphotropic virus type 1 and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergized with interleukin-1 and interleukin-2. Proc Natl Acad Sci USA 87: 8282-8286, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8282-8286
    • Wakasugi, N.1    Tagaya, Y.2    Wakasugi, A.3    Mitsui, M.4    Maeda, M.5    Yodoi, J.6    Tursz, T.7
  • 18
    • 0028818288 scopus 로고
    • Cell growth stimulation by the redox protein thioredoxin occurs by a novel helper mechanism
    • 18. Gasdaska JR, Berggren M and Powis G, Cell growth stimulation by the redox protein thioredoxin occurs by a novel helper mechanism. Cell Growth Differ 6: 1643-1650, 1995.
    • (1995) Cell Growth Differ , vol.6 , pp. 1643-1650
    • Gasdaska, J.R.1    Berggren, M.2    Powis, G.3
  • 19
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • 19. Rubartelli A, Bajetto A, Allavena G, Wollman E and Sitia R, Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J Biol Chem 267: 24161-24164,1992.
    • (1992) J Biol Chem , vol.267 , pp. 24161-24164
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia, R.5
  • 20
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
    • 20. Weichsel A, Gasdaska JR, Powis G and Montfort WR, Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer. Structure 4: 735-751, 1996.
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3    Montfort, W.R.4
  • 21
    • 0025909444 scopus 로고
    • High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution
    • 21. Forman-Kay JD, Clore GM, Wingfield PT and Gronenborn AM, High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochem 30: 2685-2698, 1991.
    • (1991) Biochem , vol.30 , pp. 2685-2698
    • Forman-Kay, J.D.1    Clore, G.M.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 23
    • 0027186030 scopus 로고
    • Purification of human thioredoxin reductase: Properties and characterization by absorption and circular dichroism spectroscopy
    • 23. Oblong JE, Gasdaska PY, Sherrill K and Powis G, Purification of human thioredoxin reductase: Properties and characterization by absorption and circular dichroism spectroscopy. Biochem 32: 7271-7277, 1993.
    • (1993) Biochem , vol.32 , pp. 7271-7277
    • Oblong, J.E.1    Gasdaska, P.Y.2    Sherrill, K.3    Powis, G.4
  • 24
    • 0015216928 scopus 로고
    • Reduced triphosphopyridine nucleotide oxidase-catalyzed alterations of membrane phospholipids
    • 24. Poyer JL and McCay PB, Reduced triphosphopyridine nucleotide oxidase-catalyzed alterations of membrane phospholipids. J Biol Chem 246: 263-269, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 263-269
    • Poyer, J.L.1    McCay, P.B.2
  • 25
    • 0029006990 scopus 로고
    • Diamide: An oxidant probe for thiols
    • 25. Kosower NS and Kosower EM, Diamide: An oxidant probe for thiols. Methods Enzymol 251: 123-132, 1995.
    • (1995) Methods Enzymol , vol.251 , pp. 123-132
    • Kosower, N.S.1    Kosower, E.M.2
  • 26
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • 26. Gilbert HF, Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol 251: 8-30, 1995.
    • (1995) Methods Enzymol , vol.251 , pp. 8-30
    • Gilbert, H.F.1
  • 27
    • 0021199710 scopus 로고
    • Disulfide bond formation in proteins
    • 27. Creighton TE, Disulfide bond formation in proteins. Methods Enzymol 107: 305-329, 1984.
    • (1984) Methods Enzymol , vol.107 , pp. 305-329
    • Creighton, T.E.1
  • 28
    • 3042934967 scopus 로고
    • Tissue Sulfhydryl groups
    • 28. Ellman GL, Tissue Sulfhydryl groups. Arch Biochem Biophys 82: 70-77, 1959.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 29
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • 29. Claiborne A, Miller H, Parsonage D and Ross RP, Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J 7: 1483-1490, 1993.
    • (1993) FASEB J , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 30
    • 0024339293 scopus 로고
    • The non-flavin redox center of the streptococcal NADH peroxidase II, evidence for a stabilized cystein-sulfenic acid
    • 30. Poole LB and Claiborne A, The non-flavin redox center of the streptococcal NADH peroxidase II, Evidence for a stabilized cystein-sulfenic acid. J Biol Chem 264: 12330-12338, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 12330-12338
    • Poole, L.B.1    Claiborne, A.2
  • 31
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • 31. Weissman JS and Kim PS, Reexamination of the folding of BPTI: Predominance of native intermediates. Science 253: 1386-1393, 1995.
    • (1995) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 32
    • 0026244229 scopus 로고
    • MOLESCRIPT: A program to produce both detailed and schematic plots of protein structures
    • 32. Kraulis PJ, MOLESCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24: 946-950, 1991.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 33
    • 0025916196 scopus 로고
    • Prognosis and breast cancer. Recognition of lethal and favorable prognostic types
    • 33. Page DL, Prognosis and breast cancer. Recognition of lethal and favorable prognostic types. Am J Surg Pathol 15: 334-349, 1991.
    • (1991) Am J Surg Pathol , vol.15 , pp. 334-349
    • Page, D.L.1
  • 34
    • 0027443868 scopus 로고
    • Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione
    • 34. Ren X, Bjornstedt M, Shen B, Ericson ML and Holmgren A, Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione. Biochem 32: 9701-9705, 1993.
    • (1993) Biochem , vol.32 , pp. 9701-9705
    • Ren, X.1    Bjornstedt, M.2    Shen, B.3    Ericson, M.L.4    Holmgren, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.