Oxidant signals and oxidative stress

Current Opinion in Cell Biology

Volumn 15, Issue 2, 2003, Pages 247-254

  Finkel, Toren ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

REACTIVE OXYGEN METABOLITE;

AGING; BIODIVERSITY; CARCINOGENESIS; DESTRUCTION; HUMAN; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; REGULATORY MECHANISM; REVIEW; SIGNAL TRANSDUCTION;

EID: 0037376674     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(03)00002-4     Document Type: Review

References (54)

1. + flux. Nature. 416:2002;291-297.
2. Eiserich J.P., Baldus S., Brennan M.L., Ma W., Zhang C., Tousson A., Castro L., Lusis A.J., Nauseef W.M., White C.R.et al. Myeloperoxidase, a leukocyte-derived vascular NO oxidase. Science. 296:2002;2391-2394.
3. Suh Y.A., Arnold R.S., Lassegue B., Shi J., Xu X., Sorescu D., Chung A.B., Griendling K.K., Lambeth J.D. Cell transformation by the superoxide-generating oxidase Mox1. Nature. 401:1999;7982.
4. Arnold R.S., Shi J., Murad E., Whalen A.M., Sun C.Q., Polavarapu R., Parthasarathy S., Petros J.A., Lambeth J.D. Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1. Proc. Natl. Acad. Sci. USA. 98:2001;5550-5555 This study, and Suh et al. (1999) [3], demonstrate the existence of a family of oxidases similar to the classic neutrophil NADPH oxidase. Initial evidence suggests a role for the oxidants generated by this novel oxidase in regulating growth and cell transformation.
5. Arbiser J.L., Petros J., Klafter R., Govindajaran B., McLaughlin E.R., Brown L.F., Cohen C., Moses M., Kilroy S., Arnold R.S.et al. Reactive oxygen generated by Nox1 triggers the angiogenic switch. Proc. Natl. Acad. Sci. USA. 99:2002;715-720.
6. Terman J.R., Mao T., Pasterkamp R.J., Yu H.H., Kolodkin A.L. MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion. Cell. 109:2002;887-900.
7. Tobena-Santamaria R., Bliek M., Ljung K., Sandberg G., Mol J.N., Souer E., Koes R. FLOOZY of petunia is a flavin mono-oxygenase-like protein required for the specification of leaf and flower architecture. Genes Dev. 16:2002;753-763.
8. Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82:2002;47-95.
9. Mahadev K., Wu X., Zilbering A., Zhu L., Lawrence J.T., Goldstein B.J. Hydrogen peroxide generated during cellular insulin stimulation is integral to activation of the distal insulin signaling cascade in 3T3-L1 adipocytes. J. Biol. Chem. 276:2001;48662-48669.
10. Colavitti R., Pani G., Bedogni B., Anzevino R., Borrello S., Waltenberger J., Galeotti T. Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR. J. Biol. Chem. 277:2002;3101-3108.
11. Xu Y.C., Wu R.F., Gu Y., Yang Y.S., Yang M.C., Nwariaku F.E., Terada L.S. Involvement of TRAF4 in oxidative activation of c-Jun N-terminal kinase. J. Biol. Chem. 277:2002;28051-28057.
12. Kheradmand F., Werner E., Tremble P., Symons M., Werb Z. Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science. 280:1998;898-902.
13. Werner E., Werb Z. Integrins engage mitochondrial function for signal transduction by a mechanism dependent on Rho GTPases. J. Cell Biol. 158:2002;357-368 This study raises the intriguing possibility that oxidants released by the mitochondria might be tightly regulated, and that mitochondrial oxidants can elicit specific cellular responses. Although mitochondrial oxidants clearly play a role in the execution of cell death, limited information exists in other, nonapoptotic pathways.
14. Devadas S., Zaritskaya L., Rhee S.G., Oberley L., Williams M.S. Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and Fas ligand expression. J. Exp. Med. 195:2002;59-70 Although most attention has focused on hydrogen peroxide as a signal transducer, much less is known about what role, if any, superoxide plays. This study suggest that both reactive oxygen species can signal and that different pathways preferentially respond to one or the other oxidant species. This scenario is not unlike what exists in bacteria.
15. Zheng M., Storz G. Redox sensing by prokaryotic transcription factors. Biochem. Pharmacol. 59:2000;1-6.
16. ••].
17. ••].
18. Meng T.C., Fukada T., Tonks N.K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell. 9:2002;387-399 These studies that tyrosine phosphatases represent an important target of reactive oxygen species and that the activity of these enzymes is reversibly regulated by intracellular oxidants. Useful assays to detect these redox dependent activity changes are described by Meng et al.
19. 2. J. Biol. Chem. 277:2002;20336-20342.
20. Savitsky P.A., Finkel T. Redox regulation of Cdc25C. J. Biol. Chem. 277:2002;20535-20540.
21. Barrett W.C., DeGnore J.P., Konig S., Fales H.M., Keng Y.F., Zhang Z.Y., Yim M.B., Chock P.B. Regulation of PTP1B via glutathionylation of the active site cysteine 215. Biochemistry. 38:1999;6699-6705.
22. Wang J., Boja E.S., Tan W., Tekle E., Fales H.M., English S., Mieyal J.J., Chock P.B. Reversible glutathionylation regulates actin polymerization in A431 cells. J. Biol. Chem. 276:2001;47763-47766.
23. Sullivan D.M., Wehr N.B., Fergusson M.M., Levine R.L., Finkel T. Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation. Biochemistry. 39:2000;11121-11128.
24. Gu Z., Kaul M., Yan B., Kridel S.J., Cui J., Strongin A., Smith J.W., Liddington R.C., Lipton S.A. S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death. Science. 297:2002;1186-1190.
25. Finkel T., Holbrook N.J. Oxidants, oxidative stress and the biology of ageing. Nature. 408:2000;239-247.
26. Guarente L., Kenyon C. Genetic pathways that regulate ageing in model organisms. Nature. 408:2000;255-262.
27. •]) link three gene products involved in ageing, Forkhead transcription factors, p66shc and p53 to either the levels of intracellular reactive oxygen species or to the resistance to oxidative stress. Taken together, they strengthen the link between oxidants and ageing.
28. Furukawa-Hibi Y., Yoshida-Araki K., Ohta T., Ikeda K., Motoyama N. FOXO forkhead transcription factors induce G(2)-M checkpoint in response to oxidative stress. J. Biol. Chem. 277:2002;26729-26732.
29. •].
30. •].
31. Migliaccio E., Giorgio M., Mele S., Pelicci G., Reboldi P., Pandolfi P.P., Lanfrancone L., Pelicci P.G. The p66Shc adaptor protein controls oxidative stress response and life span in mammals. Nature. 402:1999;309-313.
32. •].
33. Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., Gu W. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell. 107:2001;137-148.
34. Vaziri H., Dessain S.K., Ng Eaton E., Imai S.I., Frye R.A., Pandita T.K., Guarente L., Weinberg R.A. hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell. 107:2001;149-159.
35. Langley E., Pearson M., Faretta M., Bauer U.M., Frye R.A., Minucci S., Pelicci P.G., Kouzarides T. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21:2002;2383-2396.
36. Packer L., Fuehr K. Low oxygen concentration extends the lifespan of cultured human diploid cells. Nature. 267:1977;423-425.
37. Macip S., Igarashi M., Fang L., Chen A., Pan Z.Q., Lee S.W., Aaronson S.A. Inhibition of p21-mediated ROS accumulation can rescue p21-induced senescence. EMBO J. 21:2002;2180-2188.
38. Lee A.C., Fenster B.E., Ito H., Takeda K., Bae N.S., Hirai T., Yu Z.X., Ferrans V.J., Howard B.H., Finkel T. Ras proteins induce senescence by altering the intracellular levels of reactive oxygen species. J. Biol. Chem. 274:1999;7936-7940.
39. Klein J.A., Longo-Guess C.M., Rossmann M.P., Seburn K.L., Hurd R.E., Frankel W.N., Bronson R.T., Ackerman S.L. The harlequin mouse mutation downregulates apoptosis-inducing factor. Nature. 419:2002;367-374 This work suggests that the physiological role of apoptosis-inducing factor is to scavenge mitochondrial oxidants. When levels of apoptosis-inducing factor are reduced, reactive oxygen species rise within specific neurons and there is subsequent neuronal degeneration and death. Thus, an antioxidant scavenger can both protect and participate in apoptosis.
40. Rosen D.R., Siddique T., Patterson D., Figlewicz D.A., Sapp P., Hentati A., Donaldson D., Goto J., O'Regan J.P., Deng H.X.et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 362:1993;59-62.
41. Cai J.Y., Jones D.P. Superoxide in apoptosis - mitochondrial generation triggered by cytochrome c loss. J. Biol. Chem. 273:1998;11401-11404.
42. Szatrowski T.P., Nathan C.F. Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res. 51:1991;794-798.
43. Karanjawala Z.E., Murphy N., Hinton D.R., Hsieh C.L., Lieber M.R. Oxygen metabolism causes chromosome breaks and is associated with the neuronal apoptosis observed in DNA double-strand break repair mutants. Curr. Biol. 12:2002;397-402.
44. Benhar M., Dalyot I., Engelberg D., Levitzki A. Enhanced ROS production in oncogenically transformed cells potentiates c-Jun N-terminal kinase and p38 mitogen-activated protein kinase activation and sensitization to genotoxic stress. Mol. Cell Biol. 21:2001;6913-6926.
45. Vafa O., Wade M., Kern S., Beeche M., Pandita T.K., Hampton G.M., Wahl G.M. c-Myc can induce DNA damage, increase reactive oxygen species, and mitigate p53 function: a mechanism for oncogene-induced genetic instability. Mol. Cell. 9:2002;1031-1044 This study links c-Myc expression with a rise in reactive oxygen species (ROS) and subsequent genetic instability. These results might have implications beyond a single oncogene, since other transforming genes also appear to increase ROS levels.
46. Tanaka H., Matsumura I., Ezoe S., Satoh Y., Sakamaki T., Albanese C., Machii T., Pestell R.G., Kanakura Y. E2F1 and c-Myc potentiate apoptosis through inhibition of NF-kappaB activity that facilitates MnSOD-mediated ROS elimination. Mol. Cell. 9:2002;1017-1029.
47. Wonsey D.R., Zeller K.I., Dang C.V. The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation. Proc. Natl. Acad. Sci. USA. 99:2002;6649-6654.
48. •].
49. •].
50. •]) suggest that antioxidant scavengers represent a network of interconnecting activities. These studies also suggest that metabolism and intracellular oxidants appear to regulate the activities of this scavenging network through a complex feedback circuit.
51. Koerkamp M.G., Rep M., Bussemaker H.J., Hardy G.P., Mul A., Piekarska K., Szigyarto C.A., De Mattos J.M., Tabak H.F. Dissection of transient oxidative stress response in Saccharomyces cerevisiae by using DNA microarrays. Mol. Biol. Cell. 13:2002;2783-2794.
52. Li J., Lee J.M., Johnson J.A. Microarray analysis reveals an antioxidant responsive element-driven gene set involved in conferring protection from an oxidative stress-induced apoptosis in IMR-32 cells. J. Biol. Chem. 277:2002;388-394.
53. Lin T.K., Hughes G., Muratovska A., Blaikie F.H., Brookes P.S., Darley-Usmar V., Smith R.A., Murphy M.P. Specific modification of mitochondrial protein thiols in response to oxidative stress: a proteomics approach. J. Biol. Chem. 277:2002;17048-17056.
54. Rabilloud T., Heller M., Gasnier F., Luche S., Rey C., Aebersold R., Benahmed M., Louisot P., Lunardi J. Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. J. Biol. Chem. 277:2002;19396-19401.