Oxidative stress interference with the nuclear factor-κB activation pathways

Biochemical Pharmacology

Volumn 60, Issue 8, 2000, Pages 1075-1083

  Schoonbroodt, Sonia ^a   Piette, Jacques ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

Cytokines; NF B; Oxidative stress; Signal transduction; Tyrosine kinase

Indexed keywords

ADAPTOR PROTEIN; HYDROGEN PEROXIDE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR KAPPA B; INHIBITOR PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

ENZYME ACTIVATION; HOMEOSTASIS; HUMAN; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN PHOSPHORYLATION; REVIEW; SIGNAL TRANSDUCTION; TRANSCRIPTION REGULATION;

EID: 0034668171     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(00)00371-3     Document Type: Article

References (84)

1. Darnell J.R. Variety in the level of gene control in eukaryotic cells. Nature. 297:1982;365-371.
2. Jones P.L., Wolffe A.P. Relationships between chromatin organization and DNA methylation in determining gene expression. Semin Cancer Biol. 9:1999;339-347.
3. Wallin J.J., Gackstetter E.R., Koshland M.E. Dependence of BSAP repressor and activator functions on BSAP concentration. Science. 279:1998;1961-1964.
4. Tjian R., Maniatis T. Transcriptional activation A complex puzzle with few easy pieces . Cell. 77:1994;5-8.
5. Epstein J., Glaser T., Cai J., Jepeal L., Walton D.S., Maas R.L. Two independent and interactive DNA-binding subdomains of the Pax6 paired domain are regulated by alternative splicing. Genes Dev. 8:1994;2022-2034.
6. Kozmik Z., Czerny T., Busslinger M. Alternatively spliced insertions in the paired domain restrict the DNA sequence specificity of Pax6 and Pax8. EMBO J. 16:1997;6793-6803.
7. Jackson S.P., Tjian R. O-glycosylation of eukaryotic transcription factors Implications for mechanisms of transcriptional regulation . Cell. 55:1988;125-133.
8. Boyes J., Byfield P., Nakatani Y., Ogryzko V. Regulation of activity of the transcription factor GATA-1 by acetylation. Nature. 396:1998;594-598.
9. Hunter T., Karin M. The regulation of transcription by phosphorylation. Cell. 70:1992;375-387.
10. Meplan C., Richard M.-J., Hainaut P. Redox signalling and transition metals in the control of the p53 pathway. Biochem Pharmacol. 59:2000;25-33.
11. Arrigo A.P. Gene expression and the thiol redox state. Free Radic Biol Med. 27:1999;936-944.
12. Nakamura H., Nakamura K., Yodoi J. Redox regulation of cellular activation. Annu Rev Immunol. 15:1997;351-369.
13. Zheng M., Storz G. Redox sensing by prokaryotic transcription factors. Biochem Pharmacol. 59:2000;1-6.
14. Morel Y., Barouki R. Down-regulation of cytochrome P450 1A1 gene promoter by oxidative stress. Critical contribution of nuclear factor 1. J Biol Chem. 273:1998;26969-26976.
15. 2 and NFI . Mol Cell Biol. 10:1999;6825-6832.
16. Wu X., Bishopric N., Disher D., Murphy B., Webster K. Physical and functional sensitivity of zinc finger transcription factors to redox change. Mol Cell Biol. 16:1996;1035-1046.
17. Pognonec P., Kato H., Roeder R.G. The helix-loop-helix/leucine repeat transcription factor USF can be functionally regulated in a redox-dependent manner. J Biol Chem. 267:1992;24563-24567.
18. Starovasnik M.A., Blackwell T.K., Laue T.M., Weintraub H., Klevit R.E. Folding topology of the disulfide-bonded dimeric DNA-binding domain of the myogenic determination factor MyoD. Biochemistry. 31:1992;9891-9903.
19. Semenza G. Expression of hypoxia-inducible factor 1 Mechanisms and consequences . Biochem Pharmacol. 59:2000;47-53.
20. 2 is mediated by xenobiotic-response element. Arch Biochem Biophys. 356:1998;142-150.
21. Rainwater R., Parks D., Anderson M., Tegtmeyer P., Mann K. Role of cysteine residues in regulation of p53 function. Mol Cell Biol. 15:1995;3892-3903.
22. Hainaut P., Milner J. Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res. 53:1993;4469-4473.
23. Parks D., Bolinger R., Mann K. Redox state regulates binding of p53 to sequence-specific DNA, but not to non-specific or mismatched DNA. Nucleic Acids Res. 25:1997;1289-1295.
24. Matthews J.R., Wakasugi N., Virelizier J.L., Yodoi J., Hay R.T. Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Nucleic Acids Res. 20:1992;3821-3830.
25. Mitomo K., Nakayama K., Fujimoto K., Sun X., Seki S., Yamamoto K. Two different cellular redox systems regulate the DNA-binding activity of the p50 subunit of NF-kappa B in vitro. Gene. 145:1994;197-203.
26. Toledano M.B., Leonard W.J. Modulation of transcription factor NF-kappaB binding activity by oxidation-reduction in vitro. Proc Natl Acad Sci USA. 88:1991;4328-4332.
27. Aslund F., Beckwith J. Bridge over troubled waters Sensing stress by disulfide bond formation . Cell. 96:1999;751-753.
28. Xanthoudakis S., Miao G., Wang F., Pan Y.C., Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11:1992;3323-3335.
29. Walker L.J., Robson C.N., Black E., Gillepsie D., Hickson I.D. Identification of residues in the human DNA repair enzyme HAP1 (Ref-1) that are essential for redox regulation of Jun DNA binding. Mol Cell Biol. 13:1993;5370-5376.
30. Huang L.H., Arany Z., Livingstone D.M., Bunn F.H. Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit. J Biol Chem. 271:1996;32253-32259.
31. Schenk H., Klein M., Erdbrugger W., Droge W., Schulze-Osthoff K. Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappa B and AP-1. Proc Natl Acad Sci USA. 91:1994;1672-1676.
32. Sen C.K., Packer L. Antioxidant and redox regulation of gene transcription. FASEB J. 10:1996;709-720.
33. Bowie A., O'Neill L.A. Oxidative stress and nuclear factor-kappa B activation. Biochem Pharmacol. 59:2000;13-23.
34. Guyton K., Xu K., Holbrook N. Induction of the mammalian stress response gene GADD153 by oxidative stress Role of AP-1 element . Biochem J. 314:1996;547-554.
35. Pinkus R., Weiner L.M., Daniel V. Role of oxidants and antioxidants in the induction of AP-1, NF-kappaB, and glutathione S-transferase gene expression. J Biol Chem. 271:1996;13422-13429.
36. Dröge W., Schulze-Osthoff K., Mihm S., Galter D., Schenk H., Eck H.P., Roth S., Gmunder H. Functions of glutathione and glutathione disulfide in immunology and immunopathology. FASEB J. 8:1994;1131-1138.
37. Herrlich P., Bohmer F.D. Redox regulation of signal transduction in mammalian cells. Biochem Pharmacol. 59:2000;35-41.
38. Herrlich A., Daub H., Knebel A., Herrlich P., Ullrich A., Schulz G., Gudermann T. Ligand-independent activation of platelet-derived growth factor is a necessary intermediate in lysophosphatidic acid-stimulated mitogenic activity. Proc Natl Acad Sci USA. 95:1998;8985-8990.
39. Schreck R., Rieber P., Baeuerle P.A. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J. 10:1991;2247-2258.
40. Sha W.C. Regulation of the immune responses by NF-kappa B/Rel transcription factors. J Exp Med. 187:1998;143-146.
41. Baeuerle P.A., Henkel T. Function and activation of NF-kappa B in the immune system. Annu Rev Immunol. 12:1994;141-179.
42. Baeuerle P.A., Baltimore D. NF-kappaB Ten years after . Cell. 87:1996;13-20.
43. Whiteside S.T., Israel A. IκB proteins Structure, function and regulation . Semin Cancer Biol. 8:1997;75-82.
44. Dejardin E., Bonizzi G., Bellachène A., Castronovo V., Merville M.P., Bours V. Highly-expressed p100/p52 (NFKB2) sequesters other NF-κB-related proteins in the cytoplasm of human breast cancer cells. Oncogene. 11:1995;1835-1841.
45. Traenckner E.B., Pahl H.L., Henkel T., Schmidt S., Wilk S., Baeuerle P.A. Phosphorylation of human IκBα on serines 32 and 36 controls IκBα proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14:1995;2876-2883.
46. Tran K., Merika M., Thanos D. Distinct functional properties of IkappaB alpha and IkappaB beta. Mol Cell Biol. 17:1997;5386-5399.
47. DiDonato J.A., Hayakawa M., Rothwarf D.M., Zandi E., Karin M. A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature. 388:1997;548-554.
48. Zandi E., Rothwarf D.M., Delhase M., Hayakawa M., Karin M. The IκB kinase complex (IKK) contains two kinase subunits, IKKα and IKKβ, necessary for IκBα phosphorylation and NF-κB activation. Cell. 91:1997;1231-1240.
49. Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F., Kirk H.E., Kay R.J., Israel A. Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation. Cell. 93:1998;1231-1240.
50. Rothwarf D.M., Zandi E., Natoli G., Karin M. IKKγ is an essential regulatory subunit of the IκB kinase complex. Nature. 395:1998;297-301.
51. Delhase M., Hayakawa M., Chen Y., Karin M. Positive and negative regulation of IkappaB kinase activity through IKKβ subunit phosphorylation. Science. 284:1999;309-313.
52. Karin M. The begining of the end IκB kinase (IKK) and NF-κB activation . J Biol Chem. 274:1999;27339-27342.
53. Mercurio F., Zhu H., Murray B.W., Shevchenko A., Bennett B.L., Li J., Young D.B., Barbosa M., Mann M., Manning A., Rao A. IKK-1 and IKK-2 Cytokine-activated IκB kinases essential for NF-κB activation . Science. 278:1997;860-866.
54. Regnier C.H., Song H.Y., Gao X., Goeddel D.V., Cao Z., Rothe M. Identification and characterization of an IκB kinase. Cell. 90:1997;373-383.
55. Lin X., Cunningham E.T., Mu Y., Geleziunas R., Greene W.C. The proto-oncogene Cot kinase participates in CD3/CD28 induction of NF-κB acting through the NF-κB-inducing kinase and IκB kinases. Immunity. 10:1999;271-280.
56. Nemoto S., DiDonato J.A., Lin A. Coordinate regulation of IκB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-κB-inducing kinase. Mol Cell Biol. 18:1998;7336-7343.
57. Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D. MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature. 385:1997;540-544.
58. Sylla B.S., Hung S.C., Davidson D.M., Hatzivassiliou E., Malinin N.L., Wallach D., Gilmore T.D., Kieff E., Mosialos G. Epstein-Barr virus-transforming protein latent infection membrane protein 1 activates transcription factor NF-κB through a pathway that includes the NF-κB-inducing kinase and the IκB kinases IKKα and IKKβ Proc Natl Acad Sci USA. 95:1998;10106-10111.
59. Zamanian-Daryoush M., Mogensen T.H., DiDonato J.A., Williams B.R. NF-κB activation by double-stranded-RNA-activated protein kinase (PRK) is mediated through NF-κB-inducing kinase and IκB kinase. Mol Cell Biol. 20:2000;1278-1290.
60. Yin M.J., Christerson L.B., Yamaoto Y., Kwak Y.T., Xu S., Mercurio F., Barbosa M., Cobb M.H., Gaynor R.B. HTLV-I Tax protein binds to MEKK-1 to stimulate IκB kinase activity and NF-κB activation. Cell. 93:1998;875-884.
61. Zhao Q., Lee F.S. Mitogen-activated protein kinase/ERK kinase kinases 2 and 3 activate nuclear factor-κB through IκB kinase-α and IκB kinase-β J Biol Chem. 274:1999;8355-8358.
62. Schreck R., Meier B., Mannel D.N., Droge W., Baeuerle P.A. Dithiocarbamates as potent inhibitors of NF-κB activation in intact cells. J Exp Med. 175:1992;1181-1194.
63. Bonizzi G., Dejardin E., Piret B., Piette J., Merville M.P., Bours V. Interleukin-1 β induces nuclear factor κB in epithelial cells independently of the production of reactive oxygen intermediates. Eur J Biochem. 242:1996;544-549.
64. Bonizzi G., Piette J., Merville M.P., Bours V. Distinct signal transduction pathways mediate nuclear factor-kappaB induction by IL-1β in epithelial and lymphoid cells. J Immunol. 159:1997;5264-5272.
65. Bonizzi G., Piette J., Schoonbroodt S., Greimers R., Havard L., Merville M.P., Bours V. Reactive oxygen intermediate-dependent NF-kappaB activation by interleukin-1β requires 5-lipoxygenase or NADPH oxidase activity. Mol Cell Biol. 19:1999;1950-1960.
66. 2 in NF-kappaB activation by either cytokine in both primary and transformed endothelial cells. J Biol Chem. 272:1997;25941-25950.
67. Rossi A., Kapahi P., Natoli G., Takahashi T., Chen Y., Karin M., Santoro G. Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IκB kinase. Nature. 403:2000;103-108.
68. Saitoh M., Nishitoh H., Fujii M., Takeda K., Tobiume K., Sawada Y., Kawabata M., Miyazono K., Ichijo H. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase 1 (ASK1). EMBO J. 17:1998;2596-2606.
69. Liu H., Nishitoh H., Ichijo H., Kyriakis J.M. 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. 20:2000;2198-2208.
70. Abe J.-I., Okuda M., Huang Q., Yoshizumi M., Berk B.C. Reactive oxygen species activate p90 ribosomal S6 kinase via Fyn and Ras. J Biol Chem. 275:2000;1739-1748.
71. rsk) phosphorylates the N-terminal regulatory domain of IκBα and stimulate its degradation in vitro. J Biol Chem. 272:1997;21281-21288.
72. Li N., Karin M. Ionizing radiation and short wavelength UV activate NF-κB through two distinct mechanisms. Proc Natl Acad Sci USA. 95:1998;13012-13017.
73. Bender K., Göttlicher M., Whiteside S., Rahmsdorf H.J., Herrlich P. Sequential DNA damage-independent and -dependent activation of NF-kappaB by UV. EMBO J. 17:1998;5171-5181.
74. Beraud C., Henzel W.J., Baeuerle P.A. Involvement of regulatory and catalytic subunits of phosphoinositide 3-kinase in NF-κB activation. Proc Natl Acad Sci USA. 96:1999;429-434.
75. Imbert V., Rupec R.A., Livolsi H., Pahl H.L., Traenckner E.B., Mueller-Dieckmann C., Farahifar D., Rossi B., Auberger P., Baeuerle P.A., Peyron J.F. Tyrosine phosphorylation of IκBα activates NF-κB without proteolytic degradation of IκBα Cell. 86:1996;787-798.
76. Mukhopadhyay A., Manna S.K., Aggarwal B.B. Pervanadate-induced nuclear factor-κB activation requires tyrosine phosphorylation and degradation of IκBα J Biol Chem. 275:2000;8549-8555.
77. Schoonbroodt S., Ferreira V., Best-Belpomme M., Boelaert J.R., Legrand-Poels S., Korner M., Piette J. Crucial role of the amino-terminal tyrosine residue 42 and the carboxy-terminal PEST domain of IκBα in NF-κB activation by an oxidative stress. J Immunol. 164:2000;4292-4300.
78. McKinsey T.A., Chu Z.L., Ballard D.W. Phosphorylation of the PEST domain of IkappaBbeta regulates the function of NF-kappaB/IkappaBbeta complexes. J Biol Chem. 272:1997;22377-22380.
79. Shumway S.D., Maki M., Miyamoto M. The PEST domain of IκBα is necessary and sufficient for in vitro degradation by μ-calpain. J Biol Chem. 274:1999;30874-30881.
80. Schmid E., Hotz-Wagenblatt A., Hacj V., Dröge W. Phosphorylation of the insulin receptor kinase by phosphocreatine in combination with hydrogen peroxide The structural basis of redox priming . FASEB J. 13:1999;1491-1500.
81. 2-induced T cell signal transduction. J Biol Chem. 269:1994;20718-20726.
82. Griffith C.E., Zhang W., Wanger R.L. ZAP-70-dependent and -independent activation of Erk in Jurkat T cells. J Biol Chem. 273:1997;10771-10776.
83. Aikawa R., Komuro I., Yamazaki T., Zou Y., Kudoh S., Tanaka M., Shiojima I., Hiroi Y., Yazaki Y. Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats. J Clin Invest. 100:1997;1813-1821.
84. Qin S., Ding J., Takano T., Yamamura H. Involvement of receptor aggregation and reactive oxygen species in osmotic stress-induced Syk activation in B cells. Biochem Biophys Res Commun. 262:1999;231-236.