Thiol/disulfide redox states in signaling and sensing

Critical Reviews in Biochemistry and Molecular Biology

Volumn 48, Issue 2, 2013, Pages 173-181

  Go, Young Mi ^a   Jones, Dean P ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Cadmium; Cysteine proteome; Environmental toxicant; Redox regulon; Redox sensor; Redox systems biology; Thiol redox circuit

Indexed keywords

ANTIOXIDANT; CADMIUM; CALCIUM; CYSTEINE; DISULFIDE; GLUTATHIONE; GLUTATHIONE DISULFIDE; OXIDIZING AGENT; PEROXIREDOXIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCING AGENT; SELENOCYSTEINE; THIOL; THIOREDOXIN; THIOREDOXIN REDUCTASE 1; THIOREDOXIN REDUCTASE 2;

BIOCHEMISTRY; BIOLOGICAL FUNCTIONS; CELL COMPARTMENTALIZATION; CELL ORGANELLE; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SYNTHESIS; HUMAN; MOLECULAR INTERACTION; MOLECULAR SENSOR; MOLECULAR WEIGHT; ORGANIZATIONAL STRUCTURE; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEOMICS; REVIEW; SIGNAL TRANSDUCTION; SYSTEMS BIOLOGY;

EID: 84875592333     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2013.764840     Document Type: Review

References (192)

1. Adimora NJ, Jones DP, Kemp ML. (2010). A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses. Antioxid Redox Signal 13:731-43
2. Anand P, Stamler JS. (2012). Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease. J Molecular Med 90:233-44
3. Anathy V, Roberson EC, Guala AS, et al. (2012). Redox-based regulation of apoptosis: S-glutathionylation as a regulatory mechanism to control cell death. Antioxid Redox Signal 16:496-505
4. Anderson CL, Iyer SS, Ziegler TR, Jones DP. (2007). Control of extracellular cysteine/cystine redox state by HT29 cells is independent of cellular glutathione. Am J Physiol Regul Integr Comp Physiol 293:R1069-75
5. Arita A, Costa M. (2009). Epigenetics in metal carcinogenesis: nickel, arsenic, chromium and cadmium. Metallomics: integr Biometal Sci 1:222-8
6. Arner ES, Holmgren A. (2000). Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem/FEBS 267:6102-9
7. Aw TY, Williams MW. (1992). Intestinal absorption and lymphatic transport of peroxidized lipids in rats: effect of exogenous GSH. Am J Physiol 263:G665-72
8. Aw TY Williams MW, Gray L. (1992). Absorption and lymphatic transport of peroxidized lipids by rat small intestine in vivo: role of mucosal GSH. Am J Physiol 262:G99-106
9. Bagchi D, Vuchetich PJ, Bagchi M, et al. (1997). Induction of oxidative stress by chronic administration of sodium dichromate [chromium VI] and cadmium chloride [cadmium II] to rats. Free Radic Biol Med 22:471-8
10. Baker JR, Satarug S, Urbenjapol S, et al. (2002). Associations between human liver and kidney cadmium content and immunochemically detected CYP4A11 apoprotein. Biochem Pharmacol 63:693-6
11. Barabasi AL (2009). Scale-free networks: a decade and beyond. Science 325:412-13
12. Bartosiewicz M, Penn S, Buckpitt A. (2001). Applications of gene arrays in environmental toxicology: fingerprints of gene regulation associated with cadmium chloride, benzo(a)pyrene, and trichloroethylene. Environ Health Persp 109:71-4
13. Bauer R, Demeter I, Hasemann V, Johansen JT. (1980). Structural properties of the zinc site in Cu,Zn-superoxide dismutase; perturbed angular correlation of gamma ray spectroscopy on the Cu, 111Cdsuperoxide dismutase derivative. Biochem Biophys Res Commun 94:1296-302
14. Belyaeva EA, Korotkov SM. (2003). Mechanism of primary Cd2induced rat liver mitochondria dysfunction: discrete modes of Cd2 action on calcium and thiol-dependent domains. Toxicol Appl Pharmacol 192:56-68
15. Bender A Hajieva P, Moosmann B. (2008). Adaptive antioxidant methionine accumulation in respiratory chain complexes explains the use of a deviant genetic code in mitochondria. Proc Natl Acad Sci USA 105:16496-501
16. Berg JM, Tymoczko JL, Stryer L. (2002). Deoxyribonucleotides synthesized by the reduction of ribonucleotides through a radical mechanism. In: Biochemistry. 5th ed. New York: W H Freeman. Available from: http://www.ncbi.nlm.nih.gov/books/NBK21154/ [last accessed 18 Jan 2013]
17. Beyersmann D, Block C, Malviya AN. (1994). Effects of cadmium on nuclear protein kinase C. Environ Health Persp 102:177-80
18. Beyersmann D, Hechtenberg S. (1997). Cadmium, gene regulation, and cellular signalling in mammalian cells. Toxicol Appl Pharmacol 144:247-61
19. Blanco RA, Ziegler TR, Carlson BA, et al. (2007). Diurnal variation in glutathione and cysteine redox states in human plasma. Am J Clin Nutr 86:1016-23
20. Brandes N, Schmitt S, Jakob U. (2009). Thiol-based redox switches in eukaryotic proteins. Antioxid Redox Signal 11:997-1014
21. Brzoska MM, Moniuszko-Jakoniuk J. (1998). The influence of calcium content in diet on cumulation and toxicity of cadmium in the organism. Arch Toxicol 72:63-73
22. Buchko GW, Hess NJ, Kennedy MA. (2000). Cadmium mutagenicity and human nucleotide excision repair protein XPA: CD, EXAFS and (1)H/(15)N-NMR spectroscopic studies on the zinc(II)- and cadmium(II)-associated minimal DNA-binding domain (M98-F219). Carcinogenesis 21:1051-7
23. Burk RF. (2002). Selenium, an antioxidant nutrient. Nutrition Clinical care: Official Publ Tufts Univ 5:75-9
24. Cadenas E, Davies KJ. (2000). Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 29:222-30
25. Cameron I, McNamee PM, Markham A, et al. (1986). The effects of cadmium on succinate and NADH-linked substrate oxidations in rat hepatic mitochondria. J Appl Toxicol 6:325-30
26. Candeias S, Pons B, Viau M, et al. (2010). Direct inhibition of excision/ synthesis DNA repair activities by cadmium: analysis on dedicated biochips. Mutation Res 694:53-9
27. Cannino G, Ferruggia E, Luparello C, Rinaldi AM. (2009). Cadmium and mitochondria. Mitochondrion 9:377-84
28. Casagrande S, Bonetto V, Fratelli M, et al. (2002). Glutathionylation of human thioredoxin: a possible crosstalk between the glutathione and thioredoxin systems. Proc Natl Acad Sci USA 99:9745-9
29. Cenci S, Sitia R. (2007). Managing and exploiting stress in the antibody factory. FEBS Lett 581:3652-7
30. Cenci S, van Anken E, Sitia R. (2011). Proteostenosis and plasma cell pathophysiology. Curr Opin Cell Biol 23:216-22
31. Chance B. (1952). Spectra and reaction kinetics of respiratory pigments of homogenized and intact cells. Nature 169:215-21
32. Chance B. (1954). Spectrophotometry of intracellular respiratory pigments. Science 120:767-75
33. Chawla RK, Lewis FW, Kutner MH, et al. (1984). Plasma cysteine, cystine, and glutathione in cirrhosis. Gastroenterology 87:770-6
34. Chen J, Goldsbrough PB. (1994). Increased activity of [gamma]- glutamylcysteine synthetase in tomato cells selected for cadmium tolerance. Plant Physiol 106:233-9
35. Chrestensen CA, Starke DW, Mieyal JJ. (2000). Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis. J Biol Chem 275:26556-65
36. Conterato GM, Bulcao RP, Sobieski R, et al. (2013). Blood thioredoxin reductase activity, oxidative stress and hematological parameters in painters and battery workers: relationship with lead and cadmium levels in blood. J Appl Toxicol 33:142-50
37. Crane D Haussinger D, Sies H. (1982). Rise of coenzyme A-glutathione mixed disulfide during hydroperoxide metabolism in perfused rat liver. Eur J Biochem/FEBS 127:575-8
38. Crow JP, Beckman JS, McCord JM. (1995). Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite. Biochemistry 34:3544-52
39. Cuypers A, Plusquin M, Remans T, et al. (2010). Cadmium stress: an oxidative challenge. Biometals: Int J Role Metal Ions Biol Biochem Med 23:927-40
40. D'Autreaux B, Toledano MB. (2007). ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 8:813-24
41. Deckert J. (2005). Cadmium toxicity in plants: is there any analogy to its carcinogenic effect in mammalian cells? Biometals: Int J Role Metal Ions Biol Biochem Med 18:475-81
42. Deneke SM, Fanburg BL. (1989). Regulation of cellular glutathione. Am J Physiol 257:L163-73
43. Dooley CT, Dore TM, Hanson GT, et al. (2004). Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators. J Biol Chem 279:22284-93
44. Early II JL, Nonavinakere VK, Weaver A. (1992). Effect of cadmium and/or selenium on liver mitochondria and rough endoplasmic reticulum in the rat. Toxicol Lett 62:73-83
45. El-Sharaky AS, Newairy AA, Badreldeen MM, et al. (2007). Protective role of selenium against renal toxicity induced by cadmium in rats. Toxicology 235:185-93
46. Elshorbagy AK, Nurk E, Gjesdal CG, et al. (2008). Homocysteine, cysteine, and body composition in the Hordaland Homocysteine Study: does cysteine link amino acid and lipid metabolism? Am J Clin Nutr 88:738-46
47. Essex DW, Li M. (2003). Redox control of platelet aggregation. Biochemistry 42:129-36
48. Forman HJ, Zhang H, Rinna A. (2009). Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med 30:1-12
49. Frazier JM. (1994). Need for physiologically based toxocokinetic models in estimating target organ dosage following oral ingestion of cadmium. In: Rhoda GMW, ed. Environmental science and pollution control. New York: Marcel Dekker, Inc., 281-304
50. Funato Y, Miki H. (2007). Nucleoredoxin, a novel thioredoxin family member involved in cell growth and differentiation. Antioxid Redox Signal 9:1035-57
51. Gadalla MM, Snyder SH. (2010). Hydrogen sulfide as a gasotransmitter. J Neurochem 113:14-26
52. Gallagher CM, Kovach JS, Meliker Jr. (2008). Urinary cadmium and osteoporosis in US Women 50 years of age: NHANES 1988-1994 and 1999-2004. Environ Health Persp 116:1338-43
53. Gerhard I, Monga B, Waldbrenner A, Runnebaum B. (1998). Heavy metals and fertility. J Toxicol Environ Health, Part A 54:593-611
54. Gilbert HF. (1990). Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 63:69-172
55. Giustarini D, Rossi R, Milzani A, et al. (2004). S-glutathionylation: from redox regulation of protein functions to human diseases. J Cell Mol Med 8:201-12
56. Gladyshev VN, Hatfield DL. (1999). Selenocysteine-containing proteins in mammals. J Biomed Sci 6:6151-60
57. Gleason FK, Holmgren A. (1981). Isolation and characterization of thioredoxin from the cyanobacterium, Anabaena sp. J Biol Chem 256:8306-9
58. Go YM, Duong DM, Peng J, Jones DP. (2011). Protein cysteines map to functional networks according to steady-state level of oxidation. J Proteomics Bioinform 4:196-209
59. Go YM, Gipp JJ, Mulcahy RT, Jones DP. (2004). H2O2-dependent activation of GCLC-ARE4 reporter occurs by mitogen-activated protein kinase pathways without oxidation of cellular glutathione or thioredoxin-1. J Biol Chem 279:5837-45
60. Go YM, Jones DP. (2008). Redox compartmentalization in eukaryotic cells. Biochim Biophys Acta 1780:1273-90
61. Go YM, Jones DP. (2010a). Redox clamp model for study of extracellular thiols and disulfides in redox signaling. Methods Enzymol 474:165-79
62. Go YM, Jones DP (2010b). Redox control systems in the nucleus: mechanisms and functions. Antioxid Redox Signal 13:489-509
63. Go YM, Park H, Koval M, et al. (2010). A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential. Free Radic Biol Med 48:275-83
64. Go YM, Pohl J, Jones DP. (2009). Quantification of redox conditions in the nucleus. Methods Mol Biol 464:303-17
65. Go YM, Orr M, Jones DP. (2013). Increased nuclear thioredoxin-1 potentiates cadmium-induced cytotoxicity. Toxicol Sci 131:84-94
66. Go YM, Ziegler TR, Johnson JM, et al. (2007). Selective protection of nuclear thioredoxin-1 and glutathione redox systems against oxidation during glucose and glutamine deficiency in human colonic epithelial cells. Free Radic Biol Med 42:363-70
67. Gonzalez Porque P, Baldesten A, Reichard P. (1970). The involvement of the thioredoxin system in the reduction of methionine sulfoxide and sulfate. J Biol Chem 245:2371-4
68. Gravina SA, Mieyal JJ. (1993). Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32:3368-76
69. Gutscher M, Pauleau AL, Marty L, et al. (2008). Real-time imaging of the intracellular glutathione redox potential. Nat Methods 5:553-9
70. Haendeler J, Hoffmann J, Tischler V, et al. (2002). Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat Cell Biol 4:743-9
71. Halvey PJ, Watson WH, Hansen JM, et al. (2005). Compartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling. Biochem J 386:215-9
72. Hansen JM, Watson WH, Jones DP. (2004). Compartmentation of Nrf-2 redox control: regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1. Toxicol Sci 82:308-17
73. Hansen JM, Zhang H, Jones DP. (2006). Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Radic Biol Med 40:138-45
74. Hanson GT, Aggeler R, Oglesbee D, et al. (2004). Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators. J Biol Chem 279:13044-53
75. Hashemy SI, Holmgren A. (2008). Regulation of the catalytic activity and structure of human thioredoxin 1 via oxidation and S-nitrosylation of cysteine residues. J Biol Chem 283:21890-8
76. Holmgren A. (1979). Glutathione-dependent synthesis of deoxyribonucleotides. Characterization of the enzymatic mechanism of Escherichia coli glutaredoxin. J Biol Chem 254:3672-8
77. Holmgren A. (1985). Thioredoxin. Annu Rev Biochem 54:237-71
78. Holmgren A. (1989). Thioredoxin and glutaredoxin systems. J Biol Chem 264:13963-6
79. Horiguchi H, Oguma E, Kayama F. (2011). Cadmium induces anemia through interdependent progress of hemolysis, body iron accumulation, and insufficient erythropoietin production in rats. Toxicol Sci: Official J Soc Toxicol 122:198-210
80. Hsiao CJ, Stapleton SR. (2009). Early sensing and gene expression profiling under a low dose of cadmium exposure. Biochimie 91:329-43
81. Huang YH, Shih CM, Huang CJ, et al. (2006). Effects of cadmium on structure and enzymatic activity of Cu,Zn-SOD and oxidative status in neural cells. J Cell Biochem 98:577-89
82. Hwang C, Sinskey AJ, Lodish HF. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257:1496-502
83. Ishima Y, Sawa T, Kragh-Hansen U, et al. (2007). S-Nitrosylation of human variant albumin Liprizzi (R410C) confers potent antibacterial and cytoprotective properties. J Pharmacol Experimental Therap 320:969-77
84. Jeong W, Jung Y, Kim H, et al. (2009). Thioredoxin-related protein 14, a new member of the thioredoxin family with disulfide reductase activity: implication in the redox regulation of TNF-alpha signaling. Free Radic Biol Med 47:1294-303
85. Jiang LJ, Maret W, Vallee BL. (1998). The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase. Proc Natl Acad Sci USA 95:3483-8
86. Jones DP. (2006). Disruption of mitochondrial redox circuitry in oxidative stress. Chem Biol Interact 163:38-53
87. Jones DP. (2008). Radical-free biology of oxidative stress. Am J Physiol Cell Physiol 295:C849-68
88. Jones DP. (2010). Redox sensing: orthogonal control in cell cycle and apoptosis signalling. JIinternal Med 268:432-48
89. Jones DP, Aw TY. (1990). Use of enzymes and transport systems as in situ probes of metabolite and ion gradients. In: Srere P, Jones ME, Mathews C, eds. Structural and organizational aspects of metabolic regulation. Vol. 134. UCLA Symposia on Molecular and Cellular Biology, New Series. New York: Alan R. Liss, 345-61
90. Jones DP, Carlson JL, Mody VC, et al. (2000). Redox state of glutathione in human plasma. Free Radic Biol Med 28:625-35
91. Jones DP, Eklow L, Thor H, Orrenius S. (1981). Metabolism of hydrogen peroxide in isolated hepatocytes: relative contributions of catalase and glutathione peroxidase in decomposition of endogenously generated H2O2. Arch Biochem Biophys 210:505-16
92. Jones DP, Go YM. (2010). Redox compartmentalization and cellular stress. Diabetes Obes Metabol 12:116-25
93. Jones DP, Go YM, Anderson CL, et al. (2004). Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control. Faseb J 18:1246-8
94. Jones DP, Liang Y. (2009). Measuring the poise of thiol/disulfide couples in vivo. Free Radic Biol Med 47:1329-38
95. Jones DP, Mody Jr, VC Carlson JL, et al. (2002). Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses. Free Radic Biol Med 33:1290-300
96. Kadokura H, Beckwith J. (2010). Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid Redox Signal 13:1231-46
97. Kamga CK, Zhang SX, Wang Y. (2010). Dicarboxylate carrier-mediated glutathione transport is essential for reactive oxygen species homeostasis and normal respiration in rat brain mitochondria. Am Journal of Physiology. Cell Physiol 299:C497-505
98. Karsai M, Kaski K, Barabasi AL, Kertesz J. (2012). Universal features of correlated bursty behaviour. Sci Rep 2:397
99. Kasaikina MV, Hatfield DL, Gladyshev VN. (2012). Understanding selenoprotein function and regulation through the use of rodent models. Biochim Biophys Acta 1823:1633-42
100. Kazantzis G. (2004). Cadmium, osteoporosis and calcium metabolism. Biometals: Int J Role Metal Ions Biol Biochem Med 17:493-8
101. Kemp M, Go YM, Jones DP. (2008). Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology. Free Radic Biol Med 44:921-37
102. Kippner LE, Finn NA, Shukla S, Kemp ML. (2011). Systemic remodeling of the redox regulatory network due to RNAi perturbations of glutaredoxin 1, thioredoxin 1, and glucose-6-phosphate dehydrogenase. BMC Syst Biol 5:164
103. Kirlin WG, Cai J, Thompson SA, et al. (1999). Glutathione redox potential in response to differentiation and enzyme inducers. Free Radic Biol Med 27:1208-18
104. Klaassen CD, Liu J, Choudhuri S. (1999). Metallothionein: an intracellular protein to protect against cadmium toxicity. Annu Rev Pharmacol Toxicol 39:267-94
105. Lampe BJ, Park SK, Robins T, et al. (2008). Association between 24-hour urinary cadmium and pulmonary function among community- exposed men: the VA Normative Aging Study. Environ Health Persp 116:1226-30
106. Lash LH. (2009). Renal glutathione transport: identification of carriers, physiological functions, and controversies. BioFactors 35:500-8
107. Laudanski T, Sipowicz M, Modzelewski P, et al. (1991). Influence of high lead and cadmium soil content on human reproductive outcome. Int J Gynaecol Obst: Official Organ Int Feder Gynaecol Obst 36:309-15
108. Le Moan N, Clement G, Le Maout S, et al. (2006). The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways. J Biol Chem 281:10420-30
109. Leichert LI, Gehrke F, Gudiseva HV, et al. (2008). Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proc Natl Acad Sci USA 105:8197-202
110. Leonard SE, Reddie KG, Carroll KS. (2009). Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem Biol 4:783-99
111. Li L, Rose P, Moore PK, (2011). Hydrogen sulfide and cell signaling. Annu Rev Pharmacol Toxicol 51:169-87
112. Lillig CH, Berndt C, Vergnolle O, Lonn ME, Hudemann C, Bill E, Holmgren A (2005). Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor. Proc Natl Acad Sci USA 102:8168-73
113. Low FM, Hampton MB, Peskin AV, Winterbourn CC. (2007). Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 109:2611-17
114. Lu SC. (1999). Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J: Official Publ Feder Am Soc Exp Biol 13:1169-83
115. Lyles MM, Gilbert HF. (1991). Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30:613-19
116. Mallis RJ, Buss JE, Thomas JA. (2001). Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines. Biochem J 355:145-53
117. Mandal PK, Seiler A, Perisic T, et al. (2010). System x(c)- and thioredoxin reductase 1 cooperatively rescue glutathione deficiency. J Biol Chem 285:22244-53
118. Mannervik B, Axelsson K, Sundewall AC, Holmgren A. (1983). Relative contributions of thioltransferase-and thioredoxin-dependent systems in reduction of low-molecular-mass and protein disulphides. Biochem J 213:519-23
119. Mannery YO, Ziegler TR, Hao L, et al. (2010). Characterization of apical and basal thiol-disulfide redox regulation in human colonic epithelial cells. Am J Physiol Gastrointes Liver Physiol 299:G523-30
120. Mansoor MA, Svardal AM, Schneede J, Ueland PM. (1992). Dynamic relation between reduced, oxidized, and protein-bound homocysteine and other thiol components in plasma during methionine loading in healthy men. Clin Chem 38:1316-21
121. Maret W, Vallee BL. (1998). Thiolate ligands in metallothionein confer redox activity on zinc clusters. Proc Natl Acad Sci USA 95:3478-82
122. Markovic J, Mora NJ, Broseta AM, et al. (2009). The depletion of nuclear glutathione impairs cell proliferation in 3t3 fibroblasts. PLoS One 4:e6413
123. Martinez-Ruiz A, Lamas S. (2004). S-nitrosylation: a potential new paradigm in signal transduction. Cardiovas Res 62:43-52
124. McCall KA, Huang C, Fierke CA. (2000). Function and mechanism of zinc metalloenzymes. J Nutr 130:1437S-46S
125. Mendoza-Cozatl D, Loza-Tavera H, Hernandez-Navarro A, Moreno- Sanchez R. (2005). Sulfur assimilation and glutathione metabolism under cadmium stress in yeast, protists and plants. FEMS Microbiol Rev 29:653-71
126. Mesonero JE, Rodriguez-Yoldi MC, Rodriguez-Yoldi MJ. (1995). Calcium-cadmium interaction on L-threonine intestinal transport. Reprod Nutr Dev 35:319-28
127. Mesonero JE, Yoldi MC, Yoldi MJ. (1996). Calcium-cadmium interaction on sugar absorption across the rabbit jejunum. Biological Trace Elem Res 51:149-59
128. Mieyal JJ, Chock PB. (2012). Posttranslational modification of cysteine in redox signaling and oxidative stress: focus on s-glutathionylation. Antioxid Redox Signal 16:471-5
129. Mikhailova MV, Littlefield NA, Hass BS, et al. (1997). Cadmiuminduced 8-hydroxydeoxyguanosine formation, DNA strand breaks and antioxidant enzyme activities in lymphoblastoid cells. Cancer Lett 115:141-8
130. Miller LT, Watson WH, Kirlin WG, et al. (2002). Oxidation of the glutathione/glutathione disulfide redox state is induced by cysteine deficiency in human colon carcinoma HT29 cells. J Nutr 132:2303-6
131. Miseta A, Csutora P. (2000). Relationship between the occurrence of cysteine in proteins and the complexity of organisms. Mol Biol Evol 17:1232-9
132. Misiti F, Martorana GE, Nocca G, et al. (2004). Methionine 35 oxidation reduces toxic and pro-apoptotic effects of the amyloid beta-protein fragment (31-35) on isolated brain mitochondria. Neuroscience 126:297-303
133. Moosmann B. (2011). Respiratory chain cysteine and methionine usage indicate a causal role for thiyl radicals in aging. Exp Gerontol 46:164-9
134. Morgan B, Ezerina D, Amoako TN, et al. (2012). Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat Chem Biol, in press
135. Moriarty-Craige SE, Jones DP. (2004). Extracellular thiols and thiol/ disulfide redox in metabolism. Annu Rev Nutr 24:481-509
136. Moss M, Guidot DM, Wong-Lambertina M, et al. (2000). The effects of chronic alcohol abuse on pulmonary glutathione homeostasis. Am J Resp Crit Care Med 161:414-19
137. Murphy MP. (2012). Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications. Antiox Redox Signal 16:476-95
138. Mustafa AK, Gadalla MM, Sen N, et al. (2009). H2S signals through protein S-sulfhydration. Sci Signal 2:ra72
139. Nagy P, Winterbourn CC. (2010). Redox chemistry of biological thiols. Adv Mol Toxicol 4:183-222
140. Nakamura T, Lipton SA. (2011). S-nitrosylation of critical protein thiols mediates protein misfolding and mitochondrial dysfunction in neurodegenerative diseases. Antiox Redox Signal 14:1479-92
141. Nemmiche S, Chabane-Sari D, Kadri M, Guiraud P. (2011). Cadmium chloride-induced oxidative stress and DNA damage in the human Jurkat T cell line is not linked to intracellular trace elements depletion. Toxicol In Vitro: Int J Publ Assoc BIBRA 25:191-8
142. Newairy AA, El-Sharaky AS, Badreldeen MM, et al. (2007). The hepatoprotective effects of selenium against cadmium toxicity in rats. Toxicology 242:23-30
143. Nigam D, Shukla GS, Agarwal AK. (1999). Glutathione depletion and oxidative damage in mitochondria following exposure to cadmium in rat liver and kidney. Toxicol Lett 106:151-7
144. Nishimoto M, Sakaue M, Hara S. (2006). Short-interfering RNAmediated silencing of thioredoxin reductase 1 alters the sensitivity of HeLa cells toward cadmium. Biol Pharmaceut Bull 29:543-6
145. Nkabyo YS, Ziegler TR, Gu LH, et al. (2002). Glutathione and thioredoxin redox during differentiation in human colon epithelial (Caco-2) cells. Am J Physiol Gastrointest Liver Physiol 283:G1352-9
146. Noonan CW, Sarasua SM, Campagna D, et al. (2002). Effects of exposure to low levels of environmental cadmium on renal biomarkers. Environ Health Persp 110:151-5
147. Ochi T, Takahashi K, Ohsawa M. (1987). Indirect evidence for the induction of a prooxidant state by cadmium chloride in cultured mammalian cells and a possible mechanism for the induction. Mut Res 180:257-66
148. Ookhtens M, Kaplowitz N. (1998). Role of the liver in interorgan homeostasis of glutathione and cyst(e)ine. Sem Liver Dis 18:313-29
149. Permina EA, Medvedeva YA, Baeck PM, et al. (2013). Identification of self-consistent modulons from bacterial microarray expression data with the help of structured regulon gene sets. J Biomol Struct Dyn 31: 115-24
150. Peters JL, Perlstein TS, Perry MJ, et al. (2010). Cadmium exposure in association with history of stroke and heart failure. Environ Res 110:199-206
151. Reed DJ, Brodie AE, Meredith MJ. (1983). Cellular heterogeneity in the status and functions of cysteine and glutathione. New York: Raven Press
152. Refsum H, Ueland PM, Nygard O, Vollset SE. (1998). Homocysteine and cardiovascular disease. Annu Rev Med 49:31-62
153. Reynaert NL, Ckless K, Guala AS, et al. (2006). In situ detection of S-glutathionylated proteins following glutaredoxin-1 catalyzed cysteine derivatization. Biochim Biophys Acta 1760:380-7
154. Roede JR, Go YM, Jones DP. (2012). Redox equivalents and mitochondrial bioenergetics. Methods Mol Biol 810:249-80
155. Sagher D, Brunell D, Hejtmancik JF, et al. (2006). Thionein can serve as a reducing agent for the methionine sulfoxide reductases. Proc Natl Acad Sci USA 103:8656-61
156. Sakurai A, Nishimoto M, Himeno S, et al. (2005). Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: role of NF-E2-related factor-2. J Cell Physiol 203:529-37
157. Sali A, Glaeser R, Earnest T, Baumeister W. (2003). From words to literature in structural proteomics. Nature 422:216-25
158. Sanz A, Caro P, Ayala V, et al. (2006). Methionine restriction decreases mitochondrial oxygen radical generation and leak as well as oxidative damage to mitochondrial DNA and proteins. FASEB J: Official Publ Feder Am Soc Exp Biol 20:1064-73
159. Satarug S, Garrett SH, Sens MA, Sens DA. (2011). Cadmium, environmental exposure, and health outcomes. Ciencia Saude Coletiva 16:2587-602
160. Sato N, Kamada T, Suematsu T, et al. (1978). Cadmium toxicity and liver mitochondria. I. Different effects of cadmium administered in vivo to adult, young, and ethionine-fed rats. J Biochem 84:117-25
161. Schafer FQ, Buettner GR. (2001). Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30:1191-212
162. Schutzendubel A, Schwanz P, Teichmann T, et al. (2001). Cadmium-induced changes in antioxidative systems, hydrogen peroxide content, and differentiation in Scots pine roots. Plant Physiol 127:887-98
163. Sethuraman M, McComb ME, Huang H, et al. (2004). Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J Proteome Res 3:1228-33
164. Shukla GS, Shukla A, Potts RJ, et al. (2000). Cadmium-mediated oxidative stress in alveolar epithelial cells induces the expression of gamma-glutamylcysteine synthetase catalytic subunit and glutathione S-transferase alpha and pi isoforms: potential role of activator protein-1. Cell Biol Toxicol 16:347-62
165. Sies H, Summer KH. (1975). Hydroperoxide-metabolizing systems in rat liver. Eur J Biochem 57:503-12
166. Singhal RK, Anderson ME, Meister A. (1987). Glutathione, a first line of defense against cadmium toxicity. FASEB J: Official Publ Feder Am Soc Exp Biol 1:220-3
167. U.S. Environmental Protection Agency: Technology Transfer Network Air Toxics Web Site. (2000). Cadmium compounds [Online]. US Environmental Protection Agency. Available from: http://www.epa.- gov/ttn/atw/hlthef/cadmium.html [last accessed 18 Jan 2013]
168. Smiri M, Chaoui A, Rouhier N, et al. (2011). Cadmium affects the glutathione/glutaredoxin system in germinating pea seeds. Biol Trace Elem Res 142:93-105
169. Stadtman ER, Van Remmen H, Richardson A, et al. (2005). Methionine oxidation and aging. Biochim Biophys Acta 1703:135-40
170. Tang W, Shaikh ZA. (2001). Renal cortical mitochondrial dysfunction upon cadmium metallothionein administration to Sprague-Dawley rats. J Toxicol Environ Health, Part A 63:221-35
171. Taniguchi M, Nagao K, Inoue K, Imaizumi K. (2008). Cholesterol lowering effect of sulfur-containing amino acids added to a soybean protein diet in rats. J Nutr Sci Vitaminol 54:448-53
172. Thevenod F, Friedmann JM, Katsen AD, Hauser IA. (2000). Upregulation of multidrug resistance P-glycoprotein via nuclear factorkappaB activation protects kidney proximal tubule cells from cadmium- and reactive oxygen species-induced apoptosis. J Biol Chem 275:1887-96
173. Thijssen S, Maringwa J, Faes C, et al. (2007). Chronic exposure of mice to environmentally relevant, low doses of cadmium leads to early renal damage, not predicted by blood or urine cadmium levels. Toxicology 229:145-56
174. Tonks NK. (2005). Redox redux: revisiting PTPs and the control of cell signaling. Cell 121:667-70
175. Truong TH, Garcia FJ, Seo YH, Carroll KS. (2011). Isotopecoded chemical reporter and acid-cleavable affinity reagents for monitoring protein sulfenic acids. Bioorg Med Chem Lett 21:5015-20
176. Valverde M, Trejo C, Rojas E. (2001). Is the capacity of lead acetate and cadmium chloride to induce genotoxic damage due to direct DNAmetal interaction? Mutagenesis 16:265-70
177. Vido K, Spector D, Lagniel G, et al. (2001). A proteome analysis of the cadmium response in Saccharomyces cerevisiae. J Biol Chem 276:8469-74
178. Waalkes MP. (2003). Cadmium carcinogenesis. Mut Res 533:107-20
179. Waisberg M, Joseph P, Hale B, Beyersmann D. (2003). Molecular and cellular mechanisms of cadmium carcinogenesis. Toxicology 192:95-117
180. Wang L, Li J, Liu Z. (2010). Effects of lead and/or cadmium on the oxidative damage of rat kidney cortex mitochondria. Biol Trace Elem Res 137:69-78
181. Watson WH, Chen Y, Jones DP. 2003a. Redox state of glutathione and thioredoxin in differentiation and apoptosis. Biofactors 17:307-14
182. Watson WH, Pohl J, Montfort WR, et al. 2003b. Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif. J Biol Chem 278:33408-15
183. Watson WH, Heilman JM, Hughes LL, Spielberger JC. (2008). Thioredoxin reductase-1 knock down does not result in thioredoxin- 1 oxidation. Biochem Biophys Res Commun 368:832-6
184. Winterbourn CC, Metodiewa D (1994). The reaction of superoxide with reduced glutathione. Arch Biochem Biophys 314:284-90
185. Xanthoudakis S, Curran T. (1992). Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J 11:653-65
186. Yang MS, Yu LC, Gupta RC. (2004). Analysis of changes in energy and redox states in HepG2 hepatoma and C6 glioma cells upon exposure to cadmium. Toxicology 201:105-13
187. Yeh MY, Burnham EL, Moss M, Brown LA. (2007). Chronic alcoholism alters systemic and pulmonary glutathione redox status. Am J Resp Crit Care Med 176:270-6
188. Yuan L, Kaplowitz N. (2009). Glutathione in liver diseases and hepatotoxicity. Mol Aspects Med 30:29-41
189. Zeneli L, Daci N, Paçarizi H, Daci-Ajvazi M. (2010). Interaction between cadmium and calcium in human blood at the smokers. Am J Pharmacol Toxicol 5:48-51
190. Zhang H, Go YM, Jones DP. (2007). Mitochondrial thioredoxin-2/ peroxiredoxin-3 system functions in parallel with mitochondrial GSH system in protection against oxidative stress. Arch Biochem Biophys 465:119-26
191. Zhong Q, Putt DA, Xu F, Lash LH. (2008). Hepatic mitochondrial transport of glutathione: studies in isolated rat liver mitochondria and H4IIE rat hepatoma cells. Arch Biochem Biophys 474:119-27
192. Ziegler DM. (1985). Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu Rev Biochem 54:305-29