메뉴 건너뛰기




Volumn 14, Issue 2, 2005, Pages 149-153

Thioredoxin: A multifunctional antioxidant enzyme in kidney, heart and vessels

Author keywords

Antioxidants; Cardiovascular disease; Endothelium; Signal transduction; Smooth muscle

Indexed keywords

ANTIOXIDANT; APOPTOSIS SIGNAL REGULATING KINASE 1; BINDING PROTEIN; GLUTATHIONE DISULFIDE; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

EID: 15444377306     PISSN: 10624821     EISSN: None     Source Type: Journal    
DOI: 10.1097/00041552-200503000-00010     Document Type: Review
Times cited : (80)

References (41)
  • 1
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J, Arner ES. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 2001; 31:1287-1312.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 2
    • 0028824707 scopus 로고
    • Redox signalling and the control of cell growth and death
    • Powis G, Briehl M, Oblong J. Redox signalling and the control of cell growth and death. Pharmacol Ther 1995; 68:149-173.
    • (1995) Pharmacol Ther , vol.68 , pp. 149-173
    • Powis, G.1    Briehl, M.2    Oblong, J.3
  • 3
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae HZ, Chung SJ, Rhee SG. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 1994; 269:27670-27678.
    • (1994) J Biol Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 4
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha
    • Kang SW, Chae HZ, Seo MS, et al. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem 1998; 273:6297-6302.
    • (1998) J Biol Chem , vol.273 , pp. 6297-6302
    • Kang, S.W.1    Chae, H.Z.2    Seo, M.S.3
  • 5
    • 0031028975 scopus 로고    scopus 로고
    • Cloning and expression of a novel mammalian thioredoxin
    • Spyrou G, Enmark E, Miranda-Vizuete A, et al. Cloning and expression of a novel mammalian thioredoxin. J Biol Chem 1997; 272:2936-2941.
    • (1997) J Biol Chem , vol.272 , pp. 2936-2941
    • Spyrou, G.1    Enmark, E.2    Miranda-Vizuete, A.3
  • 6
    • 18444365267 scopus 로고    scopus 로고
    • Thioredoxin-2 (TRX-2) is an essential gene regulating mitochondria-dependent apoptosis
    • Tanaka T, Hosoi F, Yamaguchi-Iwai Y, et al. Thioredoxin-2 (TRX-2) is an essential gene regulating mitochondria-dependent apoptosis. EMBO J 2002; 21:1695-1703.
    • (2002) EMBO J , vol.21 , pp. 1695-1703
    • Tanaka, T.1    Hosoi, F.2    Yamaguchi-Iwai, Y.3
  • 7
    • 0026715172 scopus 로고
    • Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62
    • Matthews JR, Wakasugi N, Virelizier JL, et al. Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res 1992; 20:3821-3830.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3821-3830
    • Matthews, J.R.1    Wakasugi, N.2    Virelizier, J.L.3
  • 8
    • 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, et al. AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci USA 1997; 94:3633-3638.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3633-3638
    • Hirota, K.1    Matsui, M.2    Iwata, S.3
  • 9
    • 0033796101 scopus 로고    scopus 로고
    • The role of the redox protein thioredoxin in cell growth and cancer
    • Powis G, Mustacich D, Coon A. The role of the redox protein thioredoxin in cell growth and cancer. Free Radic Biol Med 2000; 29:312-322.
    • (2000) Free Radic Biol Med , vol.29 , pp. 312-322
    • Powis, G.1    Mustacich, D.2    Coon, A.3
  • 10
    • 0035575162 scopus 로고    scopus 로고
    • Expression of glutaredoxin in human coronary arteries: Its potential role in antioxidant protection against atherosclerosis
    • Okuda M, Inoue N, Azumi H, et al. Expression of glutaredoxin in human coronary arteries: its potential role in antioxidant protection against atherosclerosis. Arterioscler Thromb Vasc Biol 2001; 21:1483-1487.
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 1483-1487
    • Okuda, M.1    Inoue, N.2    Azumi, H.3
  • 11
    • 0028151137 scopus 로고
    • Adult T cell leukemia-derived factor/ human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide
    • Nakamura H, Matsuda M, Furuke K, et al. Adult T cell leukemia-derived factor/ human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide. Immunol Lett 1994; 42:75-80.
    • (1994) Immunol Lett , vol.42 , pp. 75-80
    • Nakamura, H.1    Matsuda, M.2    Furuke, K.3
  • 12
    • 0037130962 scopus 로고    scopus 로고
    • Vitamin D3-upregulated protein-1 (VDUP-1) regulates redox-dependent vascular smooth muscle cell proliferation through interaction with thioredoxin
    • Schulze PC, De Keulenaer GW, Yoshioka J, et al. Vitamin D3-upregulated protein-1 (VDUP-1) regulates redox-dependent vascular smooth muscle cell proliferation through interaction with thioredoxin. Circ Res 2002; 91:689-695.
    • (2002) Circ Res , vol.91 , pp. 689-695
    • Schulze, P.C.1    De Keulenaer, G.W.2    Yoshioka, J.3
  • 13
    • 0031846343 scopus 로고    scopus 로고
    • Expression of thioredoxin is enhanced in atherosclerotic plaques and during neointima formation in rat arteries
    • Takagi Y, Gon Y, Todaka T, et al. Expression of thioredoxin is enhanced in atherosclerotic plaques and during neointima formation in rat arteries. Lab Invest 1998; 78:957-966.
    • (1998) Lab Invest , vol.78 , pp. 957-966
    • Takagi, Y.1    Gon, Y.2    Todaka, T.3
  • 14
    • 2942567844 scopus 로고    scopus 로고
    • Thioredoxin reductase 1 is upregulated in atherosclerotic plaques: Specific induction of the promoter in human macrophages by oxidized low-density lipoproteins
    • Furman C, Rundlof AK, Larigauderie G, et al. Thioredoxin reductase 1 is upregulated in atherosclerotic plaques: specific induction of the promoter in human macrophages by oxidized low-density lipoproteins. Free Radic Biol Med 2004; 37:71-85.
    • (2004) Free Radic Biol Med , vol.37 , pp. 71-85
    • Furman, C.1    Rundlof, A.K.2    Larigauderie, G.3
  • 15
    • 0347600939 scopus 로고    scopus 로고
    • Enhanced oxidative stress and impaired thioredoxin expression in spontaneously hypertensive rats
    • Tanito M, Nakamura H, Kwon YW, et al. Enhanced oxidative stress and impaired thioredoxin expression in spontaneously hypertensive rats. Antioxid Redox Signal 2004; 6:89-97.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 89-97
    • Tanito, M.1    Nakamura, H.2    Kwon, Y.W.3
  • 16
    • 0034724793 scopus 로고    scopus 로고
    • Altered gene expressions during hypoxia and reoxygenation in cortical neurons isolated from stroke-prone spontaneously hypertensive rats
    • Yamagata K, Tagami M, Ikeda K, et al. Altered gene expressions during hypoxia and reoxygenation in cortical neurons isolated from stroke-prone spontaneously hypertensive rats. Neurosci Lett 2000; 284:131-134.
    • (2000) Neurosci Lett , vol.284 , pp. 131-134
    • Yamagata, K.1    Tagami, M.2    Ikeda, K.3
  • 17
    • 0141563542 scopus 로고    scopus 로고
    • Protective roles of thioredoxin, a redox-regulating protein, in renal ischemia/reperfusion injury
    • Kasuno K, Nakamura H, Ono T, et al. Protective roles of thioredoxin, a redox-regulating protein, in renal ischemia/reperfusion injury. Kidney Int 2003; 64:1273-1282. The authors show that thioredoxin is retained in medullary-tubule ascending limb of the kidney and secreted from proximal tubuli into urine during renal ischemia/ reperfusion. The retention of thioredoxin may have a protective effect against renal ischemia/reperfusion injury.
    • (2003) Kidney Int , vol.64 , pp. 1273-1282
    • Kasuno, K.1    Nakamura, H.2    Ono, T.3
  • 18
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman JS, Koppenol WH. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol Cell Physiol 1996; 271:C1424-C1437.
    • (1996) Am J Physiol Cell Physiol , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 19
    • 0038279860 scopus 로고    scopus 로고
    • Thioredoxin redox signaling in the ischemic heart: An insight with transgenic mice overexpressing Trx1
    • Turoczi T, Chang VW, Engelman RM, et al. Thioredoxin redox signaling in the ischemic heart: an insight with transgenic mice overexpressing Trx1. J Mol Cell Cardiol 2003; 35:695-704.
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 695-704
    • Turoczi, T.1    Chang, V.W.2    Engelman, R.M.3
  • 20
    • 0347986778 scopus 로고    scopus 로고
    • Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy
    • Yamamoto M, Yang G, Hong C, et al. Inhibition of endogenous thioredoxin in the heart increases oxidative stress and cardiac hypertrophy. J Clin Invest 2003; 112:1395-1406. The authors show that endogenous thioredoxin is an essential component of the cardiomyocyte antioxidant mechanisms and plays a critical role in regulating oxidative stress in the heart in vivo. Furthermore, inhibiting endogenous thioredoxin in the heart promoted hypertrophy, both under basal conditions and in response to pressure overload through redox-sensitive mechanisms.
    • (2003) J Clin Invest , vol.112 , pp. 1395-1406
    • Yamamoto, M.1    Yang, G.2    Hong, C.3
  • 21
    • 0029913674 scopus 로고    scopus 로고
    • Protection against reperfusion-induced arrhythmias by human thioredoxin
    • Aota M, Matsuda K, Isowa N, et al. Protection against reperfusion-induced arrhythmias by human thioredoxin. J Cardiovasc Pharmacol 1996; 27:727-732.
    • (1996) J Cardiovasc Pharmacol , vol.27 , pp. 727-732
    • Aota, M.1    Matsuda, K.2    Isowa, N.3
  • 22
    • 0037056109 scopus 로고    scopus 로고
    • Overexpression of thioredoxin-1 in transgenic mice attenuates adriamycin-induced cardiotoxicity
    • Shioji K, Kishimoto C, Nakamura H, et al. Overexpression of thioredoxin-1 in transgenic mice attenuates adriamycin-induced cardiotoxicity. Circulation 2002; 106:1403-1409.
    • (2002) Circulation , vol.106 , pp. 1403-1409
    • Shioji, K.1    Kishimoto, C.2    Nakamura, H.3
  • 23
    • 3843054499 scopus 로고    scopus 로고
    • Cardioprotective effects of thioredoxin in myocardial ischemia and the reperfusion role of S-nitrosation
    • Tao L, Gao E, Bryan NS, et al. Cardioprotective effects of thioredoxin in myocardial ischemia and the reperfusion role of S-nitrosation. Proc Natl Acad Sci USA 2004; 101:11471-11476. The authors show that thioredoxin is taken up by the myocardium and exerts cardioprotective effects that are further potentiated by S-nitrosation.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11471-11476
    • Tao, L.1    Gao, E.2    Bryan, N.S.3
  • 24
    • 14444281569 scopus 로고    scopus 로고
    • Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways
    • Ichijo H, Nishida E, Irie K, et al. Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 1997; 275:90-94.
    • (1997) Science , vol.275 , pp. 90-94
    • Ichijo, H.1    Nishida, E.2    Irie, K.3
  • 25
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M, Nishitoh H, Fujii M, et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 1998; 17:2596-2606.
    • (1998) EMBO J , vol.17 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3
  • 26
    • 0028023143 scopus 로고
    • Isolation and characterization of a novel cDNA from HL-60 cells treated with 1,25-dihydroxyvitamin D-3
    • Chen KS, DeLuca HF. Isolation and characterization of a novel cDNA from HL-60 cells treated with 1,25-dihydroxyvitamin D-3. Biochim Biophys Acta 1994; 1219:26-32.
    • (1994) Biochim Biophys Acta , vol.1219 , pp. 26-32
    • Chen, K.S.1    DeLuca, H.F.2
  • 27
    • 0033618398 scopus 로고    scopus 로고
    • Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression
    • Nishiyama A, Matsui M, Iwata S, et al. Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression. J Biol Chem 1999; 274:21645-21650.
    • (1999) J Biol Chem , vol.274 , pp. 21645-21650
    • Nishiyama, A.1    Matsui, M.2    Iwata, S.3
  • 28
    • 0034658976 scopus 로고    scopus 로고
    • Vitamin D3 up-regulated protein 1 mediates oxidative stress via suppressing the thioredoxin function
    • Junn E, Han SH, Im JY, et al. Vitamin D3 up-regulated protein 1 mediates oxidative stress via suppressing the thioredoxin function. J Immunol 2000; 164:6287-6295.
    • (2000) J Immunol , vol.164 , pp. 6287-6295
    • Junn, E.1    Han, S.H.2    Im, J.Y.3
  • 29
    • 3142751251 scopus 로고    scopus 로고
    • Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein
    • Schulze PC, Yoshioka J, Takahashi T, et al. Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein. J Biol Chem 2004; 279:30369-30374. These studies implicate reduced thioredoxin activity secondary to TXNIP induction as an important mechanism for vascular oxidative stress in diabetes mellitus.
    • (2004) J Biol Chem , vol.279 , pp. 30369-30374
    • Schulze, P.C.1    Yoshioka, J.2    Takahashi, T.3
  • 30
    • 0142249401 scopus 로고    scopus 로고
    • Vitamin D3 up-regulated protein-1 regulates collagen expression in mesangial cells
    • Kobayashi T, Uehara S, Ikeda T, et al. Vitamin D3 up-regulated protein-1 regulates collagen expression in mesangial cells. Kidney Int 2003; 64:1632-1642.
    • (2003) Kidney Int , vol.64 , pp. 1632-1642
    • Kobayashi, T.1    Uehara, S.2    Ikeda, T.3
  • 31
    • 2642579153 scopus 로고    scopus 로고
    • Thioredoxin-interacting protein controls cardiac hypertrophy through regulation of thioredoxin activity
    • Yoshioka J, Schulze PC, Cupesi M, et al. Thioredoxin-interacting protein controls cardiac hypertrophy through regulation of thioredoxin activity. Circulation 2004; 109:2581-2586. In this paper it is shown that activation of thioredoxin contributes to the development of pressure-overload cardiac hypertrophy, demonstrating the dual function of thioredoxin as both an antioxidant and a signaling protein. The results also support the emerging concept that TXNIP is a critical regulator of biomechanical signaling.
    • (2004) Circulation , vol.109 , pp. 2581-2586
    • Yoshioka, J.1    Schulze, P.C.2    Cupesi, M.3
  • 32
    • 85039408817 scopus 로고    scopus 로고
    • Thioredoxin: A multifunctional antioxidant enzyme in kidney, heart and vessels
    • in press
    • Yamawaki H and Berk BC. Thioredoxin: a multifunctional antioxidant enzyme in kidney, heart and vessels. J Clin Invest (in press).
    • J Clin Invest
    • Yamawaki, H.1    Berk, B.C.2
  • 33
    • 0141506872 scopus 로고    scopus 로고
    • Chronic physiological shear stress inhibits tumor necrosis factor-induced proinflammatory responses in rabbit aorta perfused ex vivo
    • Yamawaki H, Lehoux S, Berk BC. Chronic physiological shear stress inhibits tumor necrosis factor-induced proinflammatory responses in rabbit aorta perfused ex vivo. Circulation 2003; 108:1619-1625.
    • (2003) Circulation , vol.108 , pp. 1619-1625
    • Yamawaki, H.1    Lehoux, S.2    Berk, B.C.3
  • 34
    • 0041856170 scopus 로고    scopus 로고
    • Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif
    • Watson WH, Pohl J, Montfort WR, et al. Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif. J Biol Chem 2003; 278:33408-33415.
    • (2003) J Biol Chem , vol.278 , pp. 33408-33415
    • Watson, W.H.1    Pohl, J.2    Montfort, W.R.3
  • 35
    • 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, et al. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure 1996; 4:735-751.
    • (1996) Structure , vol.4 , pp. 735-751
    • Weichsel, A.1    Gasdaska, J.R.2    Powis, G.3
  • 36
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S, Fang FC. Nitrosylation: the prototypic redox-based signaling mechanism. Cell 2001; 106:675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 37
    • 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, et al. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat Cell Biol 2002; 4:743-749.
    • (2002) Nat Cell Biol , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3
  • 38
    • 0038511319 scopus 로고    scopus 로고
    • S-nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1
    • Sumbayev VV. S-nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1. Arch Biochem Biophys 2003; 415:133-136.
    • (2003) Arch Biochem Biophys , vol.415 , pp. 133-136
    • Sumbayev, V.V.1
  • 39
    • 4143102291 scopus 로고    scopus 로고
    • Antioxidant effects of statins via S-nitrosylation and activation of thioredoxin in endotheliat cells: A novel vasculoprotective function of statins
    • Haendeler J, Hoffmann J, Zeiher AM, et al. Antioxidant effects of statins via S-nitrosylation and activation of thioredoxin in endotheliat cells: A novel vasculoprotective function of statins. Circulation 2004; 110:856-861. In this report statin-mediated S-nitrosylation of thioredoxin enhanced the enzymatic activity of thioredoxin, resulting in a significant reduction in intracellular ROS.
    • (2004) Circulation , vol.110 , pp. 856-861
    • Haendeler, J.1    Hoffmann, J.2    Zeiher, A.M.3
  • 40
    • 18444369324 scopus 로고    scopus 로고
    • Glutathionylation of human thioredoxin: A possible crosstalk between the glutathione and thioredoxin systems
    • Casagrande S, Bonetto V, Fratelli M, et al. Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems. Proc Natl Acad Sci USA 2002; 99:9745-9749.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9745-9749
    • Casagrande, S.1    Bonetto, V.2    Fratelli, M.3
  • 41
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • Adachi T, Pimentel DR, Heibeck T, et al. S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J Biol Chem 2004; 279:29857-29862.
    • (2004) J Biol Chem , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.