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Volumn 8, Issue 9-10, 2006, Pages 1723-1728

Thioredoxin-1 and posttranslational modifications

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; THIOREDOXIN; THIOREDOXIN 1; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

EID: 33750915613     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.8.1723     Document Type: Review
Times cited : (54)

References (56)
  • 1
    • 0030903691 scopus 로고    scopus 로고
    • Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues
    • Akamatsu Y, Ohno T, Hirota K, Kagoshima H, Yodoi J, and Shigesada K. Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues. J Biol Chem 272: 14497-14500, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 14497-14500
    • Akamatsu, Y.1    Ohno, T.2    Hirota, K.3    Kagoshima, H.4    Yodoi, J.5    Shigesada, K.6
  • 2
    • 0035683686 scopus 로고    scopus 로고
    • Endothelial atheroprotective and anti-inflammatory mechanisms
    • discussion 109-111
    • Berk BC, Abe JI, Min W, Surapisitchat J, and Van C. Endothelial atheroprotective and anti-inflammatory mechanisms. Ann NY Acad Sci 947: 93-109; discussion 109-111, 2001.
    • (2001) Ann NY Acad Sci , vol.947 , pp. 93-109
    • Berk, B.C.1    Abe, J.I.2    Min, W.3    Surapisitchat, J.4    Van, C.5
  • 3
    • 0020025906 scopus 로고
    • Increase in hepatic mixed disulphide and glutathione disulphide levels elicited by paraquat
    • Brigelius R, Lenzen R, and Sies H. Increase in hepatic mixed disulphide and glutathione disulphide levels elicited by paraquat. Biochem Pharmacol 31: 1637-1641, 1982.
    • (1982) Biochem Pharmacol , vol.31 , pp. 1637-1641
    • Brigelius, R.1    Lenzen, R.2    Sies, H.3
  • 4
    • 0020624295 scopus 로고
    • Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide
    • Brigelius R, Muckel C, Akerboom TP, and Sies H. Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide. Biochem Pharmacol 32: 2529-2534, 1983.
    • (1983) Biochem Pharmacol , vol.32 , pp. 2529-2534
    • Brigelius, R.1    Muckel, C.2    Akerboom, T.P.3    Sies, H.4
  • 5
    • 0029885126 scopus 로고    scopus 로고
    • Endothelial dysfunction in atherosclerosis
    • Busse R and Fleming I. Endothelial dysfunction in atherosclerosis. J Vasc Res 33: 181-194, 1996.
    • (1996) J Vasc Res , vol.33 , pp. 181-194
    • Busse, R.1    Fleming, I.2
  • 6
    • 0031945876 scopus 로고    scopus 로고
    • Pulsatile stretch and shear: Physiological stimuli determining the production of endothelial-derived relaxing factor
    • Busse R and Fleming I. Pulsatile stretch and shear: physiological stimuli determining the production of endothelial-derived relaxing factor. J Vasc Res 35: 73-84, 1998.
    • (1998) J Vasc Res , vol.35 , pp. 73-84
    • Busse, R.1    Fleming, I.2
  • 8
    • 0035895885 scopus 로고    scopus 로고
    • c-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: Role of thioredoxin in NF-kappaB activation
    • Epub 2000 Nov 4663
    • Das KC. c-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: role of thioredoxin in NF-kappaB activation. J Biol Chem 276: 4662-4670 Epub 2000 Nov 4663, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 4662-4670
    • Das, K.C.1
  • 9
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman JC, Ellis L, Blacher RW, Roth RA, and Rutter WJ. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317: 267-270, 1985.
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 10
    • 0025883245 scopus 로고
    • Structural and functional relations among thioredoxins of different species
    • Eklund H, Gleason FK, and Holmgren A. Structural and functional relations among thioredoxins of different species. Proteins 11: 13-28, 1991.
    • (1991) Proteins , vol.11 , pp. 13-28
    • Eklund, H.1    Gleason, F.K.2    Holmgren, A.3
  • 11
    • 0025909444 scopus 로고
    • High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution
    • Forman-Kay JD, Clore GM, Wingfield PT, and Gronenborn AM. High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. Biochemistry 30: 2685-2698, 1991.
    • (1991) Biochemistry , vol.30 , pp. 2685-2698
    • Forman-Kay, J.D.1    Clore, G.M.2    Wingfield, P.T.3    Gronenborn, A.M.4
  • 12
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • Furchgott RF and Zawadzki JY. The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine. Nature 288: 373-376, 1980.
    • (1980) Nature , vol.288 , pp. 373-376
    • Furchgott, R.F.1    Zawadzki, J.Y.2
  • 13
    • 0024390169 scopus 로고
    • Endothelium-derived relaxing and contracting factors
    • Furchgott RF and Vanhoutte PM. Endothelium-derived relaxing and contracting factors. FASEB J 3: 2007-2018, 1989.
    • (1989) FASEB J , vol.3 , pp. 2007-2018
    • Furchgott, R.F.1    Vanhoutte, P.M.2
  • 15
    • 0021284165 scopus 로고
    • Redox control of enzyme activities by thiol/disulfide exchange
    • Gilbert HF. Redox control of enzyme activities by thiol/disulfide exchange. Methods Enzymol 107: 330-351, 1984.
    • (1984) Methods Enzymol , vol.107 , pp. 330-351
    • Gilbert, H.F.1
  • 16
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • Gilbert HF. Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol 251: 8-28, 1995.
    • (1995) Methods Enzymol , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 17
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • Haendeler J, Hoffmann J, Tischler V, Berk BC, Zeiher AM and Dimmeler S. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat Cell Biol 4: 743-749, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 18
    • 4143102291 scopus 로고    scopus 로고
    • Antioxidant effects of statins via S-nitrosylation and activation of thioredoxin in endothelial cells. A novel vasculoprotective function of statins
    • Haendeler J, Hoffmann J, Zeiher AM, and Dimmeler S. Antioxidant effects of statins via S-nitrosylation and activation of thioredoxin in endothelial cells. A novel vasculoprotective function of statins. Circulation 110: 856-861, 2004.
    • (2004) Circulation , vol.110 , pp. 856-861
    • Haendeler, J.1    Hoffmann, J.2    Zeiher, A.M.3    Dimmeler, S.4
  • 19
    • 28744434298 scopus 로고    scopus 로고
    • Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions
    • Epub 2005 Oct 2019
    • Hansen JM, Zhang H, and Jones DP. Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Radic Biol Med 40: 138-145 Epub 2005 Oct 2019, 2006.
    • (2006) Free Radic Biol Med , vol.40 , pp. 138-145
    • Hansen, J.M.1    Zhang, H.2    Jones, D.P.3
  • 20
    • 0034864796 scopus 로고    scopus 로고
    • Activation of nuclear factor-kappa b transcriptional activity in airway epithelial cells by thioredoxin but not by N-acetyl-cysteine and glutathione
    • Harper R, Wu K, Chang MM, Yoneda K, Pan R, Reddy SP, and Wu R. Activation of nuclear factor-kappa b transcriptional activity in airway epithelial cells by thioredoxin but not by N-acetyl-cysteine and glutathione. Am J Respir Cell Mol Biol 25: 178-185, 2001.
    • (2001) Am J Respir Cell Mol Biol , vol.25 , pp. 178-185
    • Harper, R.1    Wu, K.2    Chang, M.M.3    Yoneda, K.4    Pan, R.5    Reddy, S.P.6    Wu, R.7
  • 22
    • 0028138916 scopus 로고
    • Endothelial dysfunction in atherosclerosis
    • Harrison DG. Endothelial dysfunction in atherosclerosis. Basic Res Cardiol 1: 87-102, 1994.
    • (1994) Basic Res Cardiol , vol.1 , pp. 87-102
    • Harrison, D.G.1
  • 23
    • 0030936568 scopus 로고    scopus 로고
    • AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1
    • Hirota K, Matsui M, Iwata S, Nishiyama A, Mori K, and Yodoi J. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci USA 94: 3633-3638, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3633-3638
    • Hirota, K.1    Matsui, M.2    Iwata, S.3    Nishiyama, A.4    Mori, K.5    Yodoi, J.6
  • 24
    • 0033600744 scopus 로고    scopus 로고
    • Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB
    • Hirota K, Murata M, Sachi Y, Nakamura H, Takeuchi J, Mori K, and Yodoi J. Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB. J Biol Chem 274: 27891-27897, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 27891-27897
    • Hirota, K.1    Murata, M.2    Sachi, Y.3    Nakamura, H.4    Takeuchi, J.5    Mori, K.6    Yodoi, J.7
  • 25
    • 0142102540 scopus 로고    scopus 로고
    • Shear stress increases the amount of S-nitrosylated molecules in endothelial cells: Important role for signal transduction
    • Hoffmann J, Dimmeler S, and Haendeler J. Shear stress increases the amount of S-nitrosylated molecules in endothelial cells: Important role for signal transduction. FEBS Lett 551: 153-158, 2003.
    • (2003) FEBS Lett , vol.551 , pp. 153-158
    • Hoffmann, J.1    Dimmeler, S.2    Haendeler, J.3
  • 26
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 264: 13963-13966, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 27
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren A. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 3: 239-243, 1995.
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 28
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • Holmgren A. Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid Redox Signal 2: 811-820, 2000.
    • (2000) Antioxid Redox Signal , vol.2 , pp. 811-820
    • Holmgren, A.1
  • 29
    • 10644245123 scopus 로고    scopus 로고
    • Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1
    • Hwang CY, Ryu YS, Chung MS, Kim KD, Park SS, Chae SK, Chae HZ, and Kwon KS. Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1. Oncogene 23: 8868-8875, 2004.
    • (2004) Oncogene , vol.23 , pp. 8868-8875
    • Hwang, C.Y.1    Ryu, Y.S.2    Chung, M.S.3    Kim, K.D.4    Park, S.S.5    Chae, S.K.6    Chae, H.Z.7    Kwon, K.S.8
  • 30
    • 0023084124 scopus 로고
    • Formation of disulfides with diamide
    • Kosower NS and Kosower EM. Formation of disulfides with diamide. Methods Enzymol 143: 264-270, 1987.
    • (1987) Methods Enzymol , vol.143 , pp. 264-270
    • Kosower, N.S.1    Kosower, E.M.2
  • 31
    • 0035849714 scopus 로고    scopus 로고
    • S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: Head-to-head comparison with O-phosphorylation
    • Lane P, Hao G, and Gross SS. S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation. Sci STKE 2001: RE1, 2001.
    • (2001) Sci STKE , vol.2001
    • Lane, P.1    Hao, G.2    Gross, S.S.3
  • 32
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • Liu H, Nishitoh H, Ichijo H, and Kyriakis JM. Activation of apoptosis signal-regulating kinase 1 (ASK1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol Cell Biol 20: 2198-2208, 2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 33
    • 0037188936 scopus 로고    scopus 로고
    • Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner
    • Liu Y and Min W. Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner. Circ Res 90: 1259-1266, 2002.
    • (2002) Circ Res , vol.90 , pp. 1259-1266
    • Liu, Y.1    Min, W.2
  • 34
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin JL. Thioredoxin-a fold for all reasons. Structure 3: 245-250, 1995.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 35
    • 2042470971 scopus 로고    scopus 로고
    • Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene
    • Matsui M, Oshima M, Oshima H, Takaku K, Maruyama T, Yodoi J, and Taketo MM. Early embryonic lethality caused by targeted disruption of the mouse thioredoxin gene. Dev Biol 178: 179-185, 1996.
    • (1996) Dev Biol , vol.178 , pp. 179-185
    • Matsui, M.1    Oshima, M.2    Oshima, H.3    Takaku, K.4    Maruyama, T.5    Yodoi, J.6    Taketo, M.M.7
  • 38
    • 33644818614 scopus 로고    scopus 로고
    • Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine
    • Epub 2005 Jul 2010
    • Mitchell DA and Marietta MA. Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. Nat Chem Biol 1: 154-158 Epub 2005 Jul 2010, 2005.
    • (2005) Nat Chem Biol , vol.1 , pp. 154-158
    • Mitchell, D.A.1    Marietta, M.A.2
  • 39
    • 0027752805 scopus 로고
    • The L-arginine-nitric oxide pathway
    • Moncada S and Higgs A. The L-arginine-nitric oxide pathway. N Engl J Med 329: 2002-2012, 1993.
    • (1993) N Engl J Med , vol.329 , pp. 2002-2012
    • Moncada, S.1    Higgs, A.2
  • 41
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J and Arner ES. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31: 1287-1312, 2001.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 42
    • 0028220114 scopus 로고
    • Extension of lifespan by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • Orr WC and Sohal RS. Extension of lifespan by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 263: 1128-1130, 1994.
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 43
    • 0034990527 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • Powis G and Montfort WR. Properties and biological activities of thioredoxins. Annu Rev Biophys Biomol Struct 30: 421-455, 2001.
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 421-455
    • Powis, G.1    Montfort, W.R.2
  • 44
    • 0028773644 scopus 로고
    • The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin
    • Qin J, Clore GM, and Gronenborn AM. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 2: 503-522, 1994.
    • (1994) Structure , vol.2 , pp. 503-522
    • Qin, J.1    Clore, G.M.2    Gronenborn, A.M.3
  • 45
    • 0027443868 scopus 로고
    • Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione
    • 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. Biochemistry 32: 9701-9708, 1993.
    • (1993) Biochemistry , vol.32 , pp. 9701-9708
    • Ren, X.1    Bjornstedt, M.2    Shen, B.3    Ericson, M.L.4    Holmgren, A.5
  • 49
    • 0029939584 scopus 로고    scopus 로고
    • A novel promoter sequence is involved in the oxidative stress-induced expression of the adult T-cell leukemia-derived factor (ADF)/human thioredoxin (Trx) gene
    • Taniguchi Y, Taniguchi-Ueda Y, Mori K, and Yodoi J. A novel promoter sequence is involved in the oxidative stress-induced expression of the adult T-cell leukemia-derived factor (ADF)/human thioredoxin (Trx) gene. Nucleic Acids Res 24: 2746-2752, 1996.
    • (1996) Nucleic Acids Res , vol.24 , pp. 2746-2752
    • Taniguchi, Y.1    Taniguchi-Ueda, Y.2    Mori, K.3    Yodoi, J.4
  • 51
    • 0041856170 scopus 로고    scopus 로고
    • Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif
    • Epub 32003 Jun 33419
    • Watson WH, Pohl J, Montfort WR, Stuchlik O, Reed MS, Powis G, and Jones DP. Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif. J Biol Chem 278: 33408-33415 Epub 32003 Jun 33419, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 33408-33415
    • Watson, W.H.1    Pohl, J.2    Montfort, W.R.3    Stuchlik, O.4    Reed, M.S.5    Powis, G.6    Jones, D.P.7
  • 52
    • 0034544555 scopus 로고    scopus 로고
    • Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation
    • Wei SJ, Botero A, Hirota K, Bradbury CM, Markovina S, Laszlo A, Spitz DR, Goswami PC, Yodoi J, and Gius D. Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation. Cancer Res 60: 6688-6695, 2000.
    • (2000) Cancer Res , vol.60 , pp. 6688-6695
    • Wei, S.J.1    Botero, A.2    Hirota, K.3    Bradbury, C.M.4    Markovina, S.5    Laszlo, A.6    Spitz, D.R.7    Goswami, P.C.8    Yodoi, J.9    Gius, D.10
  • 53
    • 0030585429 scopus 로고    scopus 로고
    • Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer
    • 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
  • 56
    • 33750904465 scopus 로고    scopus 로고
    • Role of thioredoxin in cell growth through interactions with signaling molecules
    • in press
    • Yoshioka J, Schreiter ER, and Lee RT. Role of thioredoxin in cell growth through interactions with signaling molecules. Antioxid Redox Signal 2006 (in press).
    • (2006) Antioxid Redox Signal
    • Yoshioka, J.1    Schreiter, E.R.2    Lee, R.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.