Reactive oxygen species: Destroyers or messengers?

Biochemical Pharmacology

Volumn 77, Issue 8, 2009, Pages 1303-1315

  Bartosz, Grzegorz ^a,b  

^a UNIVERSITY OF LODZ   (Poland)

^b UNIVERSITY OF RZESZÓW   (Poland)

Author keywords

NADPH oxidase; Oxidative stress; Protein tyrosine phosphatases; Reactive oxygen species; Signaling

Indexed keywords

CYTOKINE; G PROTEIN COUPLED RECEPTOR; GROWTH FACTOR; INSULIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

ARTICLE; CELL ADHESION; CELL PH; CELL PROLIFERATION; CELL SPREADING; CYTOSKELETON; IMMUNE FUNCTION TEST; INSULIN RELEASE; OXIDATIVE STRESS; PRIORITY JOURNAL; SHEAR STRESS; WOUND HEALING;

EID: 62549102431     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2008.11.009     Document Type: Note

References (75)

1. Gerschman R., Gilbert D.L., Nye S.W., Dwyer P., and Fenn W.O. Oxygen poisoning and x-irradiation: a mechanism in common. Science 119 (1954) 623-626
2. Harman D. Aging: a theory based on free radical and radiation chemistry. Journal of Gerontology 11 (1956) 298-300
3. McCord J.M., and Fridovich I. Superoxide dismutase: an enzymatic function for erythrocuprein (hemocuprein). Journal of Biological Chemistry 244 (1969) 6049-6055
4. Barja G. Oxygen radicals, a failure or a success of evolution?. Free Radical Research Communications 18 (1993) 63-70
5. Sas K., Robotka H., Toldi J., and Vécsei L. Mitochondria, metabolic disturbances, oxidative stress and the kynurenine system, with focus on neurodegenerative disorders. Journal of Neurological Sciences 257 (2007) 221-239
6. Brand M.D., Buckingham J.A., Esteves T.C., Green K., Lambert A.J., Miwa S., et al. Mitochondrial superoxide and aging: uncoupling-protein activity and superoxide production. Biochemical Society Symposia 71 (2004) 203-213
7. Lambeth J.D., Krause K.H., and Clark R.A. NOX enzymes as novel targets for drug development. Seminars in Immunopathology 30 (2008) 339-363
8. Gertz M., Fischer F., Wolters D., and Steegborn C. Activation of the lifespan regulator p66Shc through reversible disulfide bond formation. Proceedings of the National Academy of Sciences of the USA 105 (2008) 5705-5709
9. Schrader M., and Fahimi H.D. Peroxisomes and oxidative stress. Biochimica et Biophysica Acta 1763 (2006) 1755-1766
10. Coatrieux C., Sanson M., Negre-Salvayre A., Parini A., Hannun Y., Itohara S., et al. MAO-A-induced mitogenic signaling is mediated by reactive oxygen species, MMP-2, and the sphingolipid pathway. Free Radical Biology and Medicine 43 (2007) 80-89
11. Bedard K., and Krause K.-H. The NOX family of ROS-generating NADPH oxidases; physiology and pathophysiology. Physiological Reviews 87 (2007) 245-313
12. Segal A.W. The function of the NADPH oxidase of phagocytes and its relationship to other Noxs in plants, invertebrates, and mammals. International Journal of Biochemistry and Cell Biology 40 (2008) 604-618
13. Thannickal V.J., and Fanburg B.L. Reactive oxygen species in cell signaling. American Journal of Physiology Lung Cellular Molecular Physiology 279 (2000) L1005-L1028
14. Townsend D.M. S-glutathionylation: indicator of cell stress and regulator of the unfolded protein response. Molecular Interventions 7 (2007) 313-324
15. Lei K., Townsend D.M., and Tew K.D. Protein cysteine sulfinic acid reductase (sulfiredoxin) as a regulator of cell proliferation and drug response. Oncogene 27 (2008) 4877-4887
16. Budanov A.V., Sablina A.A., Feinstein E., Koonin E.V., and Chumakov P.M. Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science 304 (2004) 596-600
17. Kim J.R., Yoon H.W., Kwon K.S., Lee S.R., and Rhee S.G. Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH. Analytical Biochemistry 283 (2000) 214-221
18. Bienert G.P., Møller A.L.B., Kristiansen K.A., Schulz A., Møller I.M., Schjoerring J.K., et al. Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes. Journal of Biological Chemistry 282 (2007) 1183-1192
19. Janssen-Heininger Y.M., Mossman B.T., Heintz N.H., Forman H.J., Kalyanaraman B., Finkel T., et al. Redox-based regulation of signal transduction: principles, pitfalls, and promises. Free Radical Biology and Medicine 45 (2008) 1-17
20. Bartosz G. The other face of oxygen. Free radicals in nature (2005), Polish Scientific Publishers, Warsaw
21. Wong C.M., Cheema A.K., Zhang L., and Suzuki Y.J. Protein carbonylation as a novel mechanism in redox signaling. Circulation Research 102 (2008) 310-318
22. Schafer F.Q., and Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radical Biology and Medicine 30 (2001) 1191-1212
23. Cao C., Leng Y., and Kufe D. Catalase activity is regulated by c-Abl and Arg in the oxidative stress response. Journal of Biological Chemistry 278 (2003) 29667-29675
24. Yano S., Arroyo N., and Yano N. Catalase binds Grb2 in tumor cells when stimulated with serum or ligands for integrin receptors. Free Radical Biology and Medicine 36 (2004) 1542-1554
25. Qu D., Rashidian J., Mount M.P., Aleyasin H., Parsanejad M., Lira A., et al. Role of Cdk5-mediated phosphorylation of Prx2 in MPTP toxicity and Parkinson's disease. Neuron 55 (2007) 37-52
26. Wood Z.A., Poole L.B., and Karplus P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300 (2003) 650-653
27. Lillig C.H., and Holmgren A. Thioredoxin and related molecules-from biology to health and disease. Antioxidants and Redox Signaling 9 (2007) 25-47
28. Lillig C.H., Berndt C., and Holmgren A. Glutaredoxin systems. Biochimica et Biophysica Acta 1780 (2008) 1304-1317
29. Nakayama M., Inoguchi T., Sonta T., Maeda Y., Sasaki S., Sawada F., et al. Increased expression of NAD(P)H oxidase in islets of animal models of Type 2 diabetes and its improvement by an AT1 receptor antagonist. Biochemical and Biophysical Research Communications 332 (2005) 927-933
30. Uchizono Y., Takeya R., Iwase M., Sasaki N., Oku M., Imoto H., et al. Expression of isoforms of NADPH oxidase components in rat pancreatic islets. Life Sciences 80 (2006) 133-139
31. Sandström M.E., Zhang S., Bruton J., Silva J.P., Reid M.B., Westerblad H., et al. Role of reactive oxygen species in contraction-mediated glucose transport in mouse skeletal muscle. Journal of Physiology 575 (2006) 251-262
32. Rhee S.G., Chang T.S., Bae Y.S., Lee S.R., and Kang S.W. Cellular regulation by hydrogen peroxide. Journal of the American Society of Nephrology 14 (2003) S211-S215
33. 2 for platelet-derived growth factor signal transduction. Science 270 (1995) 296-299
34. Bae Y.S., Kang S.W., Seo M.S., Baines I.C., Tekle E., Chock P.B., et al. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. Journal of Biological Chemistry 272 (1997) 217-221
35. Ushio-Fukai M., Alexander R.W., Akers M., Yin Q., Fujio Y., Walsh K., et al. Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells. Journal of Biological Chemistry 274 (1999) 22699-22704
36. Droge W. Free radicals in the physiological control of cell function. Physiological Reviews 82 (2002) 47-95
37. 2-linked cascade. Journal of Biological Chemistry 275 (2000) 32357-32362
38. Chiarugi P. From anchorage dependent proliferation to survival: lessons from redox signalling. IUBMB Life 60 (2008) 301-307
39. McCubrey J.A., Lahair M.M., and Franklin R.A. Reactive oxygen species-induced activation of the MAP kinase signaling pathways. Antioxidants and Redox Signaling 8 (2006) 1775-1789
40. Bubici C., Papa S., Dean K., and Franzoso G. Mutual cross-talk between reactive oxygen species and nuclear factor-kappa B: molecular basis and biological significance. Oncogene 25 (2006) 6731-6748
41. Copple I.M., Goldring C.E., Kitteringham N.R., and Park B.K. The Nrf2-Keap1 defence pathway: role in protection against drug-induced toxicity. Toxicology 246 (2008) 24-33
42. Funato Y., Miki H., and Nucleoredoxin. A novel thioredoxin family member involved in cell growth and differentiation. Antioxidants and Redox Signaling 9 (2007) 1035-1057
43. Tothova Z., Kollipara R., Huntly B.J., Lee B.H., Castrillon D.H., Cullen D.E., et al. FoxOs are critical mediators of hematopoietic stem cell resistance to physiologic oxidative stress. Cell 128 (2007) 325-339
44. Ahn S.G., and Thiele D.J. Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress. Genes and Development 17 (2003) 516-528
45. Liu B., Chen Y., and St. Clair D.K. ROS and p53: a versatile partnership. Free Radical Biology and Medicine 44 (2008) 1529-1535
46. Kietzmann T., and Görlach A. Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression. Seminars in Cell and Developmental Biology 16 (2005) 474-486
47. Adachi T., Weisbrod R.M., Pimentel D.R., Ying J., Sharov V.S., Schöneich C., et al. S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide. Nature Medicine 10 (2004) 1200-1207
48. Hool L.C., and Corry B. Redox control of calcium channels: from mechanisms to therapeutic opportunities. Antioxidants and Redox Signaling 9 (2007) 409-435
49. Juncos R., Hong N.J., and Garvin J.L. Differential effects of superoxide on luminal and basolateral Na+/H+ exchange in the thick ascending limb. American Journal of Physiology Regulatory and Integrative Comparative Physiology 290 (2006) R79-R83
50. Lee Y.J., and Shacter E. Hydrogen peroxide inhibits activation, not activity, of cellular caspase-3 in vivo. Free Radical Biology and Medicine 29 (2000) 684-692
51. Brennan M., Bhatti H., Nerusu K.C., Bhagavathula N., Kang S., Fisher G.J., et al. Matrix metalloproteinase-1 is the major collagenolytic enzyme responsible for collagen damage in UV-irradiated human skin. Photochemistry and Photobiology 78 (2003) 43-48
52. Shin M.H., Moon Y.J., Seo J.E., Lee Y., Kim K.H., and Chung J.H. Reactive oxygen species produced by NADPH oxidase, xanthine oxidase, and mitochondrial electron transport system mediate heat shock-induced MMP-1 and MMP-9 expression. Free Radical Biology and Medicine 44 (2008) 635-645
53. Ilbert M., Horst J., Ahrens S., Winter J., Graf P.C., Lilie H., et al. The redox-switch domain of Hsp33 functions as dual stress sensor. Nature Structural and Molecular Biology 14 (2007) 556-563
54. Fiaschi T., Cozzi G., Raugei G., Formigli L., Ramponi G., and Chiarugi P. Redox regulation of beta-actin during integrin-mediated cell adhesion. Journal of Biological Chemistry 281 (2006) 22983-22991
55. 2-induced PKB and ERK1/2 signaling. Cell Biochemistry and Biophysics 47 (2007) 1-10
56. Sorescu G.P., Song H., Tressel S.L., Hwang J., Dikalov S., Smith D.A., et al. Bone morphogenic protein 4 produced in endothelial cells by oscillatory shear stress induces monocyte adhesion by stimulating reactive oxygen species production from a nox1-based NADPH oxidase. Circulation Research 95 (2004) 773-779
57. Park H.S., Chun J.N., Jung H.Y., Choi C., and Bae Y.S. Role of NADPH oxidase 4 in lipopolysaccharide-induced proinflammatory responses by human aortic endothelial cells. Cardiovascular Research 72 (2006) 447-455
58. Parinandi N.L., Kleinberg M.A., Usatyuk P.V., Cummings R.J., Pennathur A., Cardounel A.J., et al. Hyperoxia-induced NAD(P)H oxidase activation and regulation by MAP kinases in human lung endothelial cells. American Journal of Physiology Lung Cellular and Molecular Physiology 284 (2003) L26-L38
59. Pervaiz S., and Clement M.V. Superoxide anion: oncogenic reactive oxygen species?. International Journal of Biochemistry and Cell Biology 39 (2007) 1297-1304
60. Tonks N.K. Redox redux: revisiting PTPs and the control of cell signaling. Cell 121 (2005) 667-670
61. Hehner S.P., Breitkreutz R., Shubinsky G., Unsoeld H., Schulze-Osthoff K., Schmitz M.L., et al. Enhancement of T cell receptor signaling by a mild oxidative shift in the intracellular thiol pool. Journal of Immunology 165 (2000) 4319-4328
62. Gelderman K.A., Hultqvist M., Pizzolla A., Zhao R., Nandakumar K.S., Mattsson R., et al. Macrophages suppress T cell responses and arthritis development in mice by producing reactive oxygen species. Journal of Clinical Investigations 117 (2007) 3020-3028
63. Toyokuni S., and Akatsuka S. Pathological investigation of oxidative stress in the post-genomic era. Pathology International 57 (2007) 461-473
64. Menon S.G., and Goswami P.C. A redox cycle within the cell cycle: ring in the old with the new. Oncogene 26 (2007) 1101-1109
65. Thomas S.R., Witting P.K., and Drummond G.R. Redox control of endothelial function and dysfunction: molecular mechanisms and therapeutic opportunities. Antioxidants and Redox Signaling 10 (2008) 1713-1765
66. Acker H. The oxygen sensing signal cascade under the influence of reactive oxygen species. Philosophical Transactions of the Royal Society of London Series B: Biological Sciences D 360 (2005) 2201-2210
67. Roy S., Khanna S., Nallu K., Hunt T.K., and Sen C.K. Dermal wound healing is subject to redox control. Molecular Therapy 13 (2006) 211-220
68. Sies H. Oxidative stress: introductory remarks. In: Sies H. (Ed). Oxidative stress (1985), Academic Press, London 1-8
69. Rybak L.P., Whitworth C.A., Mukherjea D., and Ramkumar V. Mechanisms of cisplatin-induced ototoxicity and prevention. Hear Research 226 (2007) 157-167
70. Lambeth J.D. Nox enzymes, ROS, and chronic disease: an example of antagonistic pleiotropy. Free Radical Biology and Medicine 43 (2007) 332-347
71. Yan S.F., Ramasamy R., and Schmidt A.M. Mechanisms of disease: advanced glycation end-products and their receptor in inflammation and diabetes complications. Nature Clinical Practice Endocrinology & Metabolism 4 (2008) 285-293
72. Wendt M.C., Daiber A., Kleschyov A.L., Mülsch A., Sydow K., Schulz E., et al. Differential effects of diabetes on the expression of the gp91phox homologues nox1 and nox4. Free Radical Biology and Medicine 39 (2005) 381-391
73. Matés J.M., Segura J.A., Alonso F.J., and Márquez J. Intracellular redox status and oxidative stress: implications for cell proliferation, apoptosis, and carcinogenesis. Archives of Toxicology 82 (2008) 273-299
74. Quinn M.T., Ammons M.C., and Deleo F.R. The expanding role of NADPH oxidases in health and disease: no longer just agents of death and destruction. Clinical Science 111 (2006) 1-20
75. Halliwell B. Oxidative stress and cancer: have we moved forward?. Biochemical Journal 401 (2007) 1-11