Cellular and molecular targets of protein S-glutathiolation

Antioxidants and Redox Signaling

Volumn 7, Issue 7-8, 2005, Pages 940-950

  Shackelford, Rodney E ^a   Heinloth, Alexandra N ^b   Heard, Steven C ^a   Paules, Richard S ^b  

^a LOUISIANA STATE UNIVERSITY   (United States)

^b NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ALCOHOL DEHYDROGENASE; ALDEHYDE REDUCTASE; BOVINE SERUM ALBUMIN; CALBINDIN; CARBONATE DEHYDRATASE III; CASPASE 3; CATHEPSIN K; CREATINE KINASE; CYSTEINE; ENOLASE; GLUTAREDOXIN; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCOGEN PHOSPHORYLASE; HEMOGLOBIN; LIPOCORTIN 2; MALATE DEHYDROGENASE; MATRIX METALLOPROTEINASE; NUCLEAR FACTOR I; PROTEIN C JUN; PROTEIN KINASE C; PROTEIN P50; PROTEIN P53; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEINASE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; THIOL GROUP; THIOREDOXIN;

ANTIOXIDANT ACTIVITY; APOPTOSIS; CARCINOGENESIS; CATALYSIS; CELL CYCLE; CELL METABOLISM; DNA REPAIR; ELECTRON TRANSPORT; FAMILIAL CANCER; HUMAN IMMUNODEFICIENCY VIRUS; ONCOGENE H RAS; OXIDATIVE STRESS; PENTOSE PHOSPHATE CYCLE; PRIORITY JOURNAL; PROTEIN STABILITY; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; CYSTEINE; GLUTATHIONE; HUMANS; OXIDANTS; PROTEIN S; SULFHYDRYL COMPOUNDS; TRANSCRIPTION FACTORS;

EID: 22044446501     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2005.7.940     Document Type: Review

References (166)

1. Abe MK, Kartha S, Karpova AY, Li J, Liu PT, Kuo WL, and Hershenson MB. Hydrogen peroxide activates extracellular signal-regulated kinase via protein kinase C, Raf-1, and MEK1. Am J Respir Cell Mol Biol 18: 562-569, 1998.
2. Adachi T, Pimentel DR, Heibeck T, Hou X, Lee YJ, Jiang B, Ido Y, and Cohen R A. S-Glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J Biol Chem 279: 29857-29862, 2004.
3. Al-Abed Y, Van Patten S, Li H, Lawson JA, FitzGerald GA, Manogue R, and Bucala R. Characterization of a novel hemoglobin-glutathione adduct that is elevated in diabetic patients. Mol Med 7: 619-623, 2001.
4. Ames BN and Shigenata MK. Oxidants are a major contributor to aging. Ann N Y Acad Sci 663: 85-96, 1992.
5. Aslan M and Ozben T. Oxidants in receptor tyrosine kinase signal transduction pathways. Antioxid Redox Signal 5: 781-788, 2003.
6. Aw TY. Cellular redox: a modulator of intestinal epithelial cell proliferation. News Physiol Sci 18: 201-204, 2003.
7. Bandyopadhyay S, Starke DW, Mieyal JJ, and Gronostajski RM. Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I. J Biol Chem 273: 392-397, 1998.
8. Barrett WC, DeGnore JP, Konig S, Fales HM, Keng YF, Zhang ZY, Yim MB, and Chock PB. Regulation of PTP1B via glutathionylation of the active site cysteine 215. Biochemistry 38: 6699-6705, 1999.
9. Basu A. Involvement of protein kinase C-delta in DNA damage-induced apoptosis. J Cell Mol Med 7: 341-350, 2003.
10. Berlett BS and Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272: 20313-20316, 1997.
11. Biteau B, Labarre J, and Toledano MB. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425: 980-984, 2003.
12. Buzek J, Latonen L, Kurki S, Peltonen K, and Laiho M. Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277. Nucleic Acids Res 30: 2340-2348, 2002.
13. Byrne JA, Grieve DJ, Cave AC, and Shah AM. Oxidative stress and heart failure. Arch Mal Coeur Vaiss 96: 214-221, 2003.
14. Cabiscol E and Levine RL. The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolation. Proc Natl Acad Sci U S A 93: 4170-4174, 1996.
15. Cacace AM, Guadagno SN, Krauss RS, Fabbro D, and Weinstein IB. The epsilon isoform of protein kinase C is an oncogene when overexpressed in rat fibroblasts. Oncogene 8: 2095-2104, 1993.
16. Cadenas E and Davies KJ. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic Biol Med 29: 222-230, 2000.
17. Cantor EJ, Mancini EV, Seth R, Yao XH. and Netticadan T. Oxidative stress and heart disease: cardiac dysfunction, nutrition, and gene therapy. Curr Hypertens Rep 5: 215-220, 2003.
18. Cappiello M, Voltarelli M, Giannessi M, Cecconi I, Camici G, Manao G, Del Corso A, and Mura U. Glutathione dependent modification of bovine lens aldose reductase. Exp Eye Res 58: 491-501, 1994.
19. Cappiello M, Voltarelli M, Cecconi I, Vilardo PG, Dal Monte M, Marini I, Del Corso A, Wilson DK, Quiocho FA, Petrash JM, and Mura U. Specifically targeted modification of human aldose reductase by physiological disulfides. J Biol Chem 271: 33539-33544, 1996.
20. Casey PJ, Solski PA, Der CJ, and Buss JE. p21ras is modified by a farnesyl isoprenoid. Proc Natl Acad Sci U S A 86: 8323-8327, 1989.
21. Celli N, Motos-Gallardo A, Tamburro A, Favaloro B, and Rotilio D. Liquid chromatography-electrospray mass spectrometry study of cysteine-10 S-glutathiolation in recombinant glutathione S-transferase of Ochrobactrum anthropi. J Chromatogr B Analyt Technol Biomed Life Sci 787: 405-413, 2003.
22. Chai YC, Hendrich S, and Thomas JA. Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils. Arch Biochem Biophys 310: 264-272, 1994.
23. Chandra A, Srivastava S, Petrash JM, Bhatnagar A, and Srivastava SK. Modification of aldose reductase by S-nitrosoglutathione. Biochemistry 36: 15801-15809, 1997.
24. Chatterjee S, Noack H, Possel H, Keilhoff G, and Wolf G. Glutathione levels in primary glial cultures: monochlorobimane provides evidence of cell type-specific distribution. Glia 27: 152-161, 1999.
25. 2 mediated cell signaling. FEBS Lett 560: 7-13, 2004.
26. Chu F, Ward NE, and O'Brian CA. Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine. Carcinogenesis 22: 1221-1229, 2001.
27. Chu F, Ward NE, and O'Brian CA. PKC isozyme S-cysteinylation by cysteine stimulates the pro-apoptotic isozyme PKC delta and inactivates the oncogenic isozyme PKC epsilon. Carcinogenesis 24: 317-325, 2003.
28. Cooke MS, Evans MD, Dizdaroglu M, and Lunec J. Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J 17: 1195-1214, 2003.
29. Cotgreave IA and Gerdes RG. Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem Biophys Res Commun 242: 1-9, 1998.
30. nd ed. New York, NY: WH Freeman & Co., 1993.
31. Crichton RR, Wilmet S, Legssyer R, and Ward RJ. Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells. J Inorg Biochem 91: 9-18, 2002.
32. Cuda G, Paterno R, Ceravolo R, Candigliota M, Perrotti N, Perticone F, Faniello MC, Schepis F, Ruocco A, Mele E, Cassano S, Bifulco M, Santillo M, and Avvedimento EV. Protection of human endothelial cells from oxidative stress: role of Ras-ERK1/2 signaling. Circulation 105: 968-974, 2002.
33. Dafre AL and Reischl E. Oxidative stress causes intracellular reversible S-thiolation of chicken hemoglobin under diamide and xanthine oxidase treatment. Arch Biochem Biophys 358: 291-296, 1998.
34. Dafre AL, Sies H, and Akerboom T. Protein S-thiolation and regulation of microsomal glutathione transferase activity by the glutathione redox couple. Arch Biochem Biophys 332: 288-294, 1996.
35. Darke PL, Jordan SP, Hall DL, Zugay JA, Shafer JA, and Kuo LC. Dissociation and association of the HIV-1 protease dimer subunits: equilibria and rates. Biochemistry 33: 98-105, 1994.
36. Davis DA, Dorsey K, Wingfield PT, Stahl SJ, Kaufman J, Fales HM, and Levine RL. Regulation of HIV-1 protease activity through cysteine modification. Biochemistry 35: 2482-2488, 1996.
37. Davis DA, Newcomb FM, Starke DW, Ott DE, Mieyal JJ, and Yarchoan R. Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. J Biol Chem 272: 25935-25940, 1997.
38. Delphin C, Cahen P, Lawrence JJ, and Baudier J. Characterization of baculovirus recombinant wild-type p53. Dimerization of p53 is required for high-affinity DNA binding and cysteine oxidation inhibits p53 DNA binding. Eur J Biochem 223: 683-692, 1994.
39. Denu JM and Tanner KG. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37: 5633-5642, 1998.
40. Donehower LA. The p53-deficient mouse: a model for basic and applied cancer studies. Semin Cancer Biol 7: 269-278, 1996.
41. Eaton P and Shattock MJ. Purification of proteins susceptible to oxidation at cysteine residues: identification of malate dehydrogenase as a target for S-glutathiolation. Ann N Y Acad Sci 973: 529-532, 2002.
42. Eaton P, Byers HL, Leeds N, Ward MA, and Shattock MJ. Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 277: 9806-9811, 2002.
43. Ehrhardt A, Ehrhardt GR, Guo X, and Schrader JW. Ras and relatives - job sharing and networking keep an old family together. Exp Hematol 30: 1089-1106, 2002.
44. Evans D and Cooke MS. Factors contributing to the outcome of oxidative damage to nucleic acids. Bioessays 26: 533-542, 2004.
45. Finkel T. Reactive oxygen species and signal transduction. IUBMB Life 52: 3-6, 2001.
46. Finkel T and Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature 408: 239-247, 2000.
47. Floyd RA. Role of oxygen free radicals in carcinogenesis and brain ischemia. FASEB J 4: 2587-2597, 1990.
48. Forman HJ and Azzi A. On the virtual existence of superoxide anions in the mitochondria: thoughts regarding its role in pathophysiology. FASEB J 11: 374-375, 1997.
49. Gaston BM, Carver J, Doctor A, and Palmer LA. S-Nitrosylation signaling in cell biology. Mol Interv 3: 253-263, 2003.
50. Gilbert HF. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 63: 69-172, 1990.
51. Giles GI and Jacob C. Reactive sulfur species: an emerging concept in oxidative stress. Biol Chem 383: 375-388, 2002.
52. Giles NM, Giles GI, and Jacob C. Multiple roles of cysteine in biocatalysis. Biochem Biophys Res Commun 300: 1-4, 2003.
53. Girotti AW. Lipid hydroperoxide generation, turnover, and effector action in biological systems. J Lipid Res 39: 1529-1542, 1998.
54. Goldschmidt-Clermont PJ and Moldovan L. Stress, superoxide, and signal transduction. Gene Expr 7: 255-260, 1999.
55. Goodman SR. The irreversibly sickled cell: a perspective. Cell Mol Biol 50: 53-58, 2004.
56. Goren I, Tavor E, Goldblum A, and Honigman A. Two cysteine residues in the DNA-binding domain of CREB control binding to CRE and CREB-mediated gene expression. J Mol Biol 313: 695-709, 2001.
57. Grant CM, Quinn KA, and Dawes IW. Differential protein S-thiolation of glyceraldehyde-3-phosphate dehydrogenase isoenzymes influences sensitivity to oxidative stress. Mol Cell Biol 19: 2650-2656, 1999.
58. Greenblatt MS, Bennett WP, Hollstein M, and Harris CC. Mutations in the p53 tumor suppressor gene: clues to cancer etiology and molecular pathogenesis. Cancer Res 54: 4855-4878, 1994.
59. Griffith OW and Meister A. Origin and turnover of mitochondrial glutathione. Proc Natl Acad Sci U S A 82: 4668-4672, 1985.
60. Grimm LM, Collison MW, Fisher RA, and Thomas JA. Protein mixed-disulfides in cardiac cells. S-Thiolation of soluble proteins in response to diamide. Biochim Biophys Acta 844: 50-54, 1985.
61. 2. Role in cell survival following oxidant injury. J Biol Chem 271: 4138-4142, 1996.
62. Hainaut P and Milner J. Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res 53: 4469-4473, 1993.
63. Halliwell B. Antioxidant defence mechanisms: from the beginning to the end (of the beginning). Free Radic Res 31: 261-272, 1999.
64. Halliwell B. Role of free radicals in the neurodegenerative diseases: therapeutic implications for antioxidant treatment. Drugs Aging 18: 685-716, 2001.
65. Hancock JF, Magee AI, Childs JE, and Marshall CJ. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57: 1167-1177, 1989.
66. Harman DJ. Aging: a theory based on free radical and radiation chemistry. Gerontology 11: 298-300, 1957.
67. Hausladen A and Stamler JS. Nitrosative stress. Methods Enzymol 300: 389-395, 1999.
68. Hayes JD and McLellan LI. Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Radic Res 31: 273-300, 1999.
69. Higuchi Y. Chromosomal DNA fragmentation in apoptosis and necrosis induced by oxidative stress. Biochem Pharmacol 66: 1527-1535, 2003.
70. Hofseth LJ, Hussain SP, and Harris CC. p53: 25 years after its discovery. Trends Pharmacol Sci 25: 177-181, 2002.
71. Hupp TR, Meek DW, Midgley CA, and Lane DP. Regulation of the specific DNA binding function of p53. Cell 71: 875-886, 1992.
72. Hwang C, Sinskey AJ, and Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502, 1992.
73. Irani K, Xia Y, Zweier JL, Sollott SJ, Der CJ, Fearon ER, Sundaresan M, Finkel T, and Goldschmidt-Clermont PJ. Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts. Science 275: 1649-1652, 1997.
74. Jaffrey SR, Erdjument-Bromage H, Ferris CD, Tempst P, and Snyder SH. Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Nat Cell Biol 3: 193-197, 2001.
75. Jahngen-Hodge J, Obin MS, Gong X, Shang F, Nowell TR Jr, Gong J, Abasi H, Blumberg J, and Taylor A. Regulation of ubiquitin-conjugating enzymes by glutathione following oxidative stress. J Biol Chem 272: 28218-28226, 1997.
76. Jenner P. Oxidative damage in neurodegenerative disease. Lancet 344: 796-798, 1994.
77. Ji Y, Akerboom TP, Sies H, and Thomas JA. S-Nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione. Arch Biochem Biophys 362: 67-78, 1999.
78. Jones DP. Redox potential of GSH/GSSG couple: assay and biological significance. Methods Enzymol 348: 93-112, 2002.
79. Klatt P, Molina EP, De Lacoba MG, Padilla CA, Martinez-Galesteo E, Barcena JA, and Lamas S. Redox regulation of c-Jun DNA binding by reversible S-glutathiolation. FASEB J 13: 1481-1490, 1999.
80. Klatt P, Molina EP, and Lamas S. Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation. J Biol Chem 27A: 15857-15864, 1999.
81. Klatt P, Pineda Molina E, Perez-Sala D, and Lamas S. Novel application of S-nitrosoglutathione-Sepharose to identify proteins that are potential targets for S-nitrosoglutathione-induced mixed-disulphide formation. Biochem J 349: 567-578, 2000.
82. Kleinman WA, Komninou D, Leutzinger Y, Colosimo S, Cox J, Lang CA, and Richie JP Jr. Protein glutathiolation in human blood. Biochem Pharmacol 65: 741-746, 2003.
83. Knickelbein RG, Ingbar DH, Seres T, Snow K, Johnston RB Jr, Fayemi O, Gumkowski F, Jamieson JD, and Warshaw JB. Hyperoxia enhances expression of gamma-glutamyl transpeptidase and increases protein S-glutathiolation in rat lung. Am J Physiol 270: 115-122, 1996.
84. Knight RJ, Kofoed KF, Schelbert HR, and Buxton DB. Inhibition of glyceraldehyde-3-phosphate dehydrogenase in post-ischaemic myocardium. Cardiovasc Res 32: 1016-1023, 1996.
85. Koester MK, Pullan LM, and Noltmann EA. The p-nitrophenyl phosphatase activity of muscle carbonic anhydrase. Arch Biochem Biophys 211: 632-642, 1981.
86. Kondo T, Higashiyama Y, Goto S, Iida T, Cho S, Iwanaga M, Mori K, Tani M, and Urata Y. Regulation of gamma-glutamylcysteine synthetase expression in response to oxidative stress. Free Radic Res 31: 325-334, 1999.
87. Kosower NS and Kosower EM. The glutathione status of cells. Int Rev Cytol 54: 109-160, 1978.
88. Kovacic P and Jacintho JD. Systemic lupus erythematosus and other autoimmune diseases from endogenous and exogenous agents: unifying theme of oxidative stress. Mini Rev Med Chem 3: 568-575, 2003.
89. Lander HM, Milbank AJ, Tauras JM, Hajjar DP, Hempstead BL, Schwartz GD, Kraemer RT, Mirza UA, Chait BT, Burk SC, and Quilliam LA. Redox regulation of cell signalling. Nature 381: 380-381, 1996.
90. Lehtonen J, Shen B, Vihinen M, Casini A, Scozzafava A, Supuran CT, Parkkila AK, Saarnio J, Kivela AJ, Waheed A, Sly WS, and Parkkila S. Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family. J Biol Chem 279: 2719-2727, 2004.
91. Li S, Yan T, Yang JQ, Oberley, TD, and Oberley LW. The role of cellular glutathione peroxidase redox regulation in the suppression of tumor cell growth by manganese superoxide dismutase. Cancer Res 60: 3927-3939, 2000.
92. Lim A, Prokaeva T, McComb ME, Connors LH, Skinner M, and Costello CE. Identification of S-sulfonation and S-thiolation of a novel transthyretin Phe33Cys variant from a patient diagnosed with familial transthyretin amyloidosis. Protein Sci 8: 1775-1785, 2003.
93. Lyon RP and Atkins WM. Kinetic characterization of native and cysteine 112-modified glutathione S-transferase A1-1: reassessment of nonsubstrate ligand binding. Biochemistry 41: 10920-10927, 2002.
94. Malkin D, Li FP, Strong LC, Fraumeni JF Jr, Nelson CE, Kim DH, Kassel J, Gryka MA, Bischoff FZ, Tainsky MA, et al. Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas, and other neoplasms. Science 250: 1233-1238, 1990.
95. Mallis RJ, Buss JE, and Thomas JA. Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines. Biochem J 355: 145-153, 2001.
96. Mallis RJ, Hamann MJ, Zhao W, Zhang T, Hendrich S, and Thomas JA. Irreversible thiol oxidation in carbonic anhydrase III: protection by S-glutathiolation and detection in aging rats. Biol Chem 383: 649-662, 2002.
97. Marshall AD, Darbyshire JF, Hunter AP, McPhie P, and Jakoby WB. Control of activity through oxidative modification at the conserved residue Cys66 of aryl sulfotransferase IV. J Biol Chem 272: 9153-9160, 1997.
98. Martinez-Ruiz A and Lamas S. S-Nitrosylation: a potential new paradigm in signal transduction. Cardiovasc Res 62: 43-52, 2004.
99. McAlister L and Holland MJ. Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes. J Biol Chem 260: 15019-15027, 1985.
100. McAlister L and Holland MJ. Isolation and characterization of yeast strains carrying mutations in the glyceraldehyde-3-phosphate dehydrogenase genes. J Biol Chem 260: 15013-15018, 1985.
101. Melino G, Bernassola F, Catani MV, Rossi A, Corazzari M, Sabatini S, Vilbois F, and Green DR. Nitric oxide inhibits apoptosis via AP-1-dependent CD95L transactivation. Cancer Res 60: 2377-2383, 2000.
102. Miller RM, Sies H, Park EM, and Thomas JA. Phosphorylase and creatine kinase modification by thiol-disulfide exchange and by xanthine oxidase-initiated S-thiolation. Arch Biochem Biophys 276: 355-363, 1990.
103. Mischak H, Goodnight JA, Kolch, W, Martiny-Baron G, Schaechtle C, Kazanietz MG, Blumberg PM, Pierce JH, and Mushinski J. F. Overexpression of protein kinase C-delta and -epsilon in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity. J Biol Chem 268: 6090-6096, 1993.
104. Morel F, Doussiere J, and Vignais PV The superoxide-generating oxidase of phagocytic cells. Physiological, molecular and pathological aspects. Eur J Biochem 201: 523-546, 1991.
105. Muller JM, Cahill MA, Rupec RA, Baeuerle PA, and Nordheim A. Antioxidants as well as oxidants activate c-fos via Ras-dependent activation of extracellular-signal-regulated kinase 2 and Elk-1. Eur J Biochem 244: 45-52, 1997.
106. Muscat JE, Kleinman W, Colosimo S, Muir A, Lazarus P, Park J, and Richie JP Jr. Enhanced protein glutathiolation and oxidative stress in cigarette smokers. Free Radic Biol Med 36: 464-470, 2004.
107. Mustacich D and Powis G. Thioredoxin reductase. Biochem J 346: 1-8, 2000.
108. Nerland DE, Cai J, and Benz FW. Selective covalent binding of acrylonitrile to Cys 186 in rat liver carbonic anhydrase III in vivo. Chem Res Toxicol 16: 583-589, 2003.
109. Nishi T, Shimizu N, Hiramoto M, Sato I, Yamaguchi Y, Hasegawa M, Aizawa S, Tanaka H, Kataoka K, Watanabe H, and Handa H. Spatial redox regulation of a critical cysteine residue of NF-kappaB in vivo. J Biol Chem 211: 44548-44556, 2002.
110. Nordstrand K, Slund F, Holmgren A, Otting G, and Berndt KD. NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism. J Mol Biol 286: 541-552, 1999.
111. Obin M, Shang F, Gong X, Handelman G, Blumberg J, and Taylor A. Redox regulation of ubiquitin-conjugating enzymes: mechanistic insights using the thiol-specific oxidant diamide. FASEB J 12: 561-569, 1998.
112. Okamoto T, Akaike, T, Sawa T, Miyamoto, Y, van der Vliet A, and Maeda H. Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J Biol Chem 276: 29596-29602, 2001.
113. Olivier M, Eeles R, Hollstein M, Khan MA, Harris CC, and Hainaut P. The IARC TP53 database: new online mutation analysis and recommendations to users. Hum Mutat 19: 607-614, 2002.
114. Paget MS and Buttner MJ. Thiol-based regulatory switches. Annu Rev Genet 37: 91-121, 2003.
115. Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, and Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J 9: 2351-2359, 1990.
116. Pastore A, Federici G, Bertini E, and Piemonte F. Analysis of glutathione: implication in redox and detoxification. Clin Chim Acta 333: 19-39, 2003.
117. Percival MD, Ouellet M, Campagnolo C, Claveau D, and Li C. Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid. Biochemistry 38: 13574-13583, 1999.
118. Perry G, Taddeo MA, Petersen RB, Castellani RJ, Harris PL, Siedlak SL, Cash, AD, Liu Q, Nunomura A, Atwood CS, and Smith MA. Adventiously-bound redox active iron and copper are at the center of oxidative damage in Alzheimer disease. Biometals 16: 77-81, 2003.
119. Porwol T, Ehleben W, Brand V, and Acker H. Tissue oxygen sensor function of NADPH oxidase isoforms, an unusual cytochrome aa3 and reactive oxygen species. Respir Physiol 128: 331-348, 2001.
120. Prior IA, Harding A, Yan J, Sluimer J, Parton RG, and Hancock JF. GTP-dependent segregation of H-ras from lipid rafts is required for biological activity. Nat Cell Biol 3: 368-375, 2001.
121. Rainwater R, Parks D, Anderson ME, Tegtmeyer P, and Mann K. Role of cysteine residues in regulation of p53 function. Mol Cell Biol 15: 3892-3903, 1995.
122. Raisanen SR, Lehenkari P, Tasanen M, Rahkila P, Harkonen, PL, and Vaananen HK. Carbonic anhydrase III protects cells from hydrogen peroxide-induced apoptosis. FASEB J 13: 13-22, 1999.
123. Ravichandran V, Seres T, Moriguchi, T, Thomas JA, and Johnston RB Jr. S-Thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. J Biol Chem 269: 25010-25015, 1994.
124. Reddig PJ, Dreckschmidt NE, Ahrens H, Simsiman R, Tseng CP, Zou J, Oberley TD, and Verma AK. Transgenic mice overexpressing protein kinase C delta in the epidermis are resistant to skin tumor promotion by 12-O- tetradecanoylphorbol-13-acetate. Cancer Res 59: 5710-5718, 1999.
125. Reddig PJ, Dreckschmidt NE, Zou J, Bourguignon SE, Oberley TD, and Verma AK. Transgenic mice overexpressing protein kinase C epsilon in their epidermis exhibit reduced papilloma burden but enhanced carcinoma formation after tumor promotion. Cancer Res 60: 595-602, 2000.
126. Reddy S, Jones, AD, Cross CE, Wong PS, and Van Der Vliet A. Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. Biochem J 347: 821-827, 2000.
127. Reichenbach J, Schubert R, Schindler D, Muller K, Bohles H, and Zielen S. Elevated oxidative stress in patients with ataxia telangiectasia. Antioxid Redox Signal 4: 465-469, 2002.
128. Rinaldi R, Eliasson E, Swedmark S, and Morgenstern R. Reactive intermediates and the dynamics of glutathione transferases. Drug Metab Dispos 30: 1053-1058, 2002.
129. Ron D and Kazanietz MG. New insights into the regulation of protein kinase C and novel phorbol ester receptors. FASEB J 13: 1658-1676, 1999.
130. Rubbo H, Radi R, Anselmi D, Kirk M, Barnes S, Butler J, Eiserich JP, and Freeman BA. Nitric oxide reaction with lipid peroxyl radicals spares alpha-tocopherol during lipid peroxidation. Greater oxidant protection from the pair nitric oxide/alpha-tocopherol than alpha-tocopherol/ascorbate. J Biol Chem 275: 10812-10818, 2000.
131. Schafer FQ and Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30: 1191-1212, 2001.
132. Schinina ME, Carlini P, Polticelli F, Zappacosta F, Bossa F, and Calabrese L. Amino acid sequence of chicken Cu,Zn-containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues. Eur J Biochem 237: 433-439, 1996.
133. Schuppe-Koistinen I, Gerdes R, Moldeus P, and Cotgreave IA. Studies on the reversibility of protein S-thiolation in human endothelial cells. Arch Biochem Biophys 315: 226-234, 1994.
134. Seres T, Ravichandran V, Moriguchi T, Rokutan K, Thomas JA, and Johnston RB Jr. Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress. J Immunol 156: 1973-1980, 1996.
135. Shackelford RE, Kaufmann WK, and Paules RS. Oxidative stress and cell cycle checkpoint function. Free Radic Biol Med 28: 1387-1404, 2000.
136. Shackelford RE, Innes CL, Sieber SO, Heinloth AN, Leadon SA, and Paules RS. The ataxia telangiectasia gene product is required for oxidative stress-induced G1 and G2 checkpoint function in human fibroblasts. J Biol Chem 15: 21951-21959, 2001.
137. Shaulian E and Karin M. AP-1 as a regulator of cell life and death. Nat Cell Biol 4: E131-E136, 2002.
138. Shenton D and Grant CM. Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. Biochem J 374: 513-519, 2003.
139. Sirover MA. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 1432: 159-184, 1999.
140. Spencer JP, Jenner P, Daniel SE, Lees AJ, Marsden DC, and Halliwell B. Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species. J Neurochem 71: 2112-2122, 1998.
141. Srivastava S, Zou ZQ, Pirollo K, Blattner W, and Chang EH. Germ-line transmission of a mutated p53 gene in a cancer-prone family with Li-Fraumeni syndrome. Nature 348: 747-749, 1990.
142. Srivastava SK, Ramana KV, Chandra D, Srivastava S, and Bhatnagar A. Regulation of aldose reductase and the polyol pathway activity by nitric oxide. Chem Biol Interact 143-144: 333-340, 2003.
143. 2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates. Cancer Res 54: 12-15, 1994.
144. Sullivan DM, Wehr NB, Fergusson M, Levine, RL, and Finkel T. Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation. Biochemistry 39: 11121-11128, 2000.
145. Sun XZ, Vinci C, Makmura L, Han S, Tran D, Nguyen J, Hamann M, Grazziani S, Sheppard S, Gutova M, Zhou F, Thomas J, and Momand J. Formation of disulfide bond in p53 correlates with inhibition of DNA binding and tetramerization. Antioxid Redox Signal 5: 655-665, 2003.
146. Sundaresan M, Yu ZX, Ferrans VJ, Sulciner DJ, Gutkind JS, Irani K, Goldschmidt-Clermont PJ, and Finkel T. Regulation of reactive-oxygen-species generation in fibroblasts by Rac1. Biochem J 318: 379-382, 1996.
147. Tamarit J, Belli G, Cabiscol E, Herrero E, and Ros J. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J Biol Chem 278: 25745-25751, 2003.
148. Tao L and English AM. Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione. Biochemistry 43: 4028-4038, 2004.
149. Thomas JA and Mallis RJ. Aging and oxidation of reactive protein sulfhydryls. Exp Gerontol 36: 1519-1526, 2001.
150. Thomas JA, Poland B, and Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 319: 1-9, 1995.
151. Tonks NK and Neel BG. From form to function: signaling by protein tyrosine phosphatases. Cell 87: 365-368, 1996.
152. Toyokuni S. Iron and carcinogenesis: from Fenton reaction to target genes. Redox Rep 7: 189-197, 2002.
153. Turrens JF. Superoxide production by the mitochondrial respiratory chain. Biosci Rep 17: 3-8, 1997.
154. Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol 552: 335-344, 2003.
155. Tyner SD, Venkatachalam S, Choi J, Jones S, Ghebranious N, Igelmann H, Lu X, Soron G, Cooper B, Brayton C, Hee Park S, Thompson T, Karsenty G, Bradley A, and Donehower LA. p53 mutant mice that display early ageing-associated phenotypes. Nature 415: 45-53, 2002.
156. Ulrich P and Cerami A. Protein glycation, diabetes, and aging. Recent Prog Horm Res 56: 1-21, 2001.
157. van der Geer P, Hunter T, and Lindberg RA. Receptor protein-tyrosine kinases and their signal transduction pathways. Annu Rev Cell Biol 10: 251-337, 1994.
158. van Montfort RL, Congreve M, Tisi D, Carr R, and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423: 773-777, 2003.
159. Viner RI, Williams TD, and Schoneich C. Peroxynitrite modification of protein thiols: oxidation, nitrosylation, and S-glutathiolation of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase. Biochemistry 38: 12408-12415, 1999.
160. Wang XW, Hussain SP, Huo TI, Wu CG, Forgues M, Hofseth LJ, Brechet C, and Harris CC. Molecular pathogenesis of human hepatocellular carcinoma. Toxicology 181-182: 43-47, 2002.
161. Ward NE, Chu F, and O'Brian CA. Regulation of protein kinase C isozyme activity by S-glutathiolation. Methods Enzymol 353: 89-100, 2002.
162. Wu HH and Momand J. Pyrrolidine dithiocarbamate prevents p53 activation and promotes p53 cysteine residue oxidation. J Biol Chem 273: 18898-18905, 1998.
163. Wu HH, Thomas JA, and Momand J. p53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: a novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes. Biochem J 351: 87-93, 2000.
164. Wu X, Bishopric NH, Bischer DJ, Murphy BJ, and Webster KA. Physical and functional sensitivity of zinc finger transcription factors to redox change. Mol Cell Biol 16: 1035-1046, 1996.
165. Young IS, McFarlane C, and McEneny J. Oxidative modification of triacylglycerol-rich lipoproteins. Biochem Soc Trans 31: 1062-1065, 2003.
166. Zech B, Wilm M, van Eldik, R, and Brune B. Mass spectrometric analysis of nitric oxide-modified caspase-3. J Biol Chem 274: 20931-20936, 1999.