The redoxome. Proteomic analysis of cellular redox networks

Current Opinion in Chemical Biology

Volumn 15, Issue 1, 2011, Pages 113-119

  Thamsen, Maike ^a   Jakob, Ursula ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; PROTEIN; SULFENIC ACID DERIVATIVE; THIOL;

CONTROLLED STUDY; EUKARYOTE; HUMAN; IN VIVO STUDY; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PROKARYOTE; PROTEIN FUNCTION; PROTEOMICS; REDOXOME; REVIEW;

BIOTIN; HOMEOSTASIS; HUMANS; OXIDATION-REDUCTION; PROTEOME; PROTEOMICS; SULFENIC ACIDS;

EUKARYOTA; PROKARYOTA;

EID: 79851510399     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2010.11.013     Document Type: Review

References (56)

1. Halliwell B., Gutteridge J.M.C. Free Radicals in Biology and Medicine 2007, Oxford University Press, Oxford, New York. 4th edn.
2. Valko M., Leibfritz D., Moncol J., Cronin M.T., Mazur M., Telser J. Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 2007, 39:44-84.
3. Stadtman E.R. Protein oxidation in aging and age-related diseases. Ann N Y Acad Sci 2001, 928:22-38.
4. Paulsen C.E., Carroll K.S. Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem Biol 2010, 5:47-62.
5. Klomsiri C., Karplus P.A., Poole L.B. Cysteine-based redox switches in enzymes. Antioxid Redox Signal 2010.
6. Brandes N., Schmitt S., Jakob U. Thiol-based redox switches in eukaryotic proteins. Antioxid Redox Signal 2009, 11:997-1014.
7. Miller R.A., Britigan B.E. Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 1997, 10:1-18.
8. Allen C.L., Bayraktutan U. Oxidative stress and its role in the pathogenesis of ischaemic stroke. Int J Stroke 2009, 4:461-470.
9. Reuter S., Gupta S.C., Chaturvedi M.M., Aggarwal B.B. Oxidative stress, inflammation, and cancer: how are they linked?. Free Radic Biol Med 2010.
10. Antelmann H., Helmann J.D. Thiol-based redox switches and gene regulation. Antioxid Redox Signal 2010.
11. Winter J., Ilbert M., Graf P.C., Ozcelik D., Jakob U. Bleach activates a redox-regulated chaperone by oxidative protein unfolding. Cell 2008, 135:691-701.
12. Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R., Lee S.S., Moon J.C., Yun J.W., et al. Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell 2004, 117:625-635.
13. Veal E.A., Day A.M., Morgan B.A. Hydrogen peroxide sensing and signaling. Mol Cell 2007, 26:1-14.
14. Dalle-Donne I., Rossi R., Colombo G., Giustarini D., Milzani A. Protein S-glutathionylation: a regulatory device from bacteria to humans. Trends Biochem Sci 2009, 34:85-96.
15. Tonks N.K. Redox redux: revisiting PTPs and the control of cell signaling. Cell 2005, 121:667-670.
16. Burgoyne J.R., Eaton P. A rapid approach for the detection, quantification, and discovery of novel sulfenic acid or S-nitrosothiol modified proteins using a biotin-switch method. Methods Enzymol 2010, 473:281-303.
17. Yeh J.I., Claiborne A., Hol W.G. Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 A resolution. Biochemistry 1996, 35:9951-9957.
18. Dalle-Donne I., Scaloni A., Giustarini D., Cavarra E., Tell G., Lungarella G., Colombo R., Rossi R., Milzani A. Proteins as biomarkers of oxidative/nitrosative stress in diseases: the contribution of redox proteomics. Mass Spectrom Rev 2005, 24:55-99.
19. Foster M.W., Hess D.T., Stamler J.S. Protein S-nitrosylation in health and disease: a current perspective. Trends Mol Med 2009, 15:391-404.
20. Koharyova M., Kolarova M. Oxidative stress and thioredoxin system. Gen Physiol Biophys 2008, 27:71-84.
21. Gallogly M.M., Mieyal J.J. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr Opin Pharmacol 2007, 7:381-391.
22. Rhee S.G., Jeong W., Chang T.S., Woo H.A. Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: its discovery, mechanism of action, and biological significance. Kidney Int Suppl 2007, S3-8.
23. Findlay V.J., Townsend D.M., Morris T.E., Fraser J.P., He L., Tew K.D. A novel role for human sulfiredoxin in the reversal of glutathionylation. Cancer Res 2006, 66:6800-6806.
24. Chiappetta G., Ndiaye S., Igbaria A., Kumar C., Vinh J., Toledano M.B. Proteome screens for Cys residues oxidation: the redoxome. Methods Enzymol 2010, 473:199-216.
25. Kettenhofen N.J., Wood M.J. Formation, Reactivity, and Detection of Protein Sulfenic Acids. Chem Res Toxicol 2010.
26. Nelson K.J., Klomsiri C., Codreanu S.G., Soito L., Liebler D.C., Rogers L.C., Daniel L.W., Poole L.B. Use of dimedone-based chemical probes for sulfenic acid detection methods to visualize and identify labeled proteins. Methods Enzymol 2010, 473:95-115.
27. Leonard S.E., Reddie K.G., Carroll K.S. Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem Biol 2009, 4:783-799.
28. Takanishi C.L., Ma L.H., Wood M.J. A genetically encoded probe for cysteine sulfenic acid protein modification in vivo. Biochemistry 2007, 46:14725-14732.
29. Seo Y.H., Carroll K.S. Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies. Proc Natl Acad Sci U S A 2009, 106:16163-16168.
30. Jaffrey S.R., Snyder S.H. The biotin switch method for the detection of S-nitrosylated proteins. Sci STKE 2001, 2001:11.
31. Wang X., Kettenhofen N.J., Shiva S., Hogg N., Gladwin M.T. Copper dependence of the biotin switch assay: modified assay for measuring cellular and blood nitrosated proteins. Free Radic Biol Med 2008, 44:1362-1372.
32. Kallakunta V.M., Staruch A., Mutus B. Sinapinic acid can replace ascorbate in the biotin switch assay. Biochim Biophys Acta 2010, 1800:23-30.
33. Saurin A.T., Neubert H., Brennan J.P., Eaton P. Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc Natl Acad Sci U S A 2004, 101:17982-17987.
34. Shelton M.D., Chock P.B., Mieyal J.J. Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid Redox Signal 2005, 7:348-366.
35. Tello D., Tarin C., Ahicart P., Breton-Romero R., Lamas S., Martinez-Ruiz A. A " fluorescence switch" technique increases the sensitivity of proteomic detection and identification of S-nitrosylated proteins. Proteomics 2009, 9:5359-5370.
36. Huang B., Chen C. Detection of protein S-nitrosation using irreversible biotinylation procedures (IBP). Free Radic Biol Med 2005, 49:447-456.
37. Hao G., Derakhshan B., Shi L., Campagne F., Gross S.S. SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures. Proc Natl Acad Sci U S A 2006, 103:1012-1017.
38. Forrester M.T., Thompson J.W., Foster M.W., Nogueira L., Moseley M.A., Stamler J.S. Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture. Nat Biotechnol 2009, 27:557-559.
39. Sinha V., Wijewickrama G.T., Chandrasena R.E., Xu H., Edirisinghe P.D., Schiefer I.T., Thatcher G.R. Proteomic and mass spectroscopic quantitation of protein S-nitrosation differentiates NO-donors. ACS Chem Biol 2010, 5:667-680.
40. Giustarini D., Dalle-Donne I., Colombo R., Milzani A., Rossi R. Is ascorbate able to reduce disulfide bridges? A cautionary note. Nitric Oxide 2008, 19:252-258.
41. Karala A.R., Ruddock L.W. Does s-methyl methanethiosulfonate trap the thiol-disulfide state of proteins?. Antioxid Redox Signal 2007, 9:527-531.
42. Hansen R.E., Winther J.R. An introduction to methods for analyzing thiols and disulfides: reactions, reagents, and practical considerations. Anal Biochem 2009, 394:147-158.
43. Leichert L.I., Jakob U. Protein thiol modifications visualized in vivo. PLoS Biol 2004, 2:e333.
44. Riederer I.M., Riederer B.M. Differential protein labeling with thiol-reactive infrared DY-680 and DY-780 maleimides and analysis by two-dimensional gel electrophoresis. Proteomics 2007, 7:1753-1756.
45. Le Moan N., Clement G., Le Maout S., Tacnet F., Toledano M.B. The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways. J Biol Chem 2006, 281:10420-10430.
46. Perez V.I., Pierce A., de Waal E.M., Ward W.F., Bokov A., Chaudhuri A., Richardson A. Detection and quantification of protein disulfides in biological tissues a fluorescence-based proteomic approach. Methods Enzymol 2010, 473:161-177.
47. Marino S.M., Li Y., Fomenko D.E., Agisheva N., Cerny R.L., Gladyshev V.N. Characterization of surface-exposed reactive cysteine residues in Saccharomyces cerevisiae. Biochemistry 2010, 49:7709-7721.
48. Leichert L.I., Gehrke F., Gudiseva H.V., Blackwell T., Ilbert M., Walker A.K., Strahler J.R., Andrews P.C., Jakob U. Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proc Natl Acad Sci U S A 2008, 105:8197-8202.
49. Go Y.M, Pohl J., Jones D.P. Quantification of redox conditions in the nucleus. Methods Mol Biol 2009, 464:303-317.
50. Kumsta C., Thamsen M., Jakob U. Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans. Antioxid Redox Signal 2010.
51. Yi L., Jenkins P.M., Leichert L.I., Jakob U., Martens J.R., Ragsdale S.W. Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. J Biol Chem 2009, 284:20556-20561.
52. Sethuraman M., McComb M.E., Huang H., Huang S., Heibeck T., Costello C.E., Cohen R.A. Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J Proteome Res 2004, 3:1228-1233.
53. Hagglund P., Bunkenborg J., Maeda K., Svensson B. Identification of thioredoxin disulfide targets using a quantitative proteomics approach based on isotope-coded affinity tags. J Proteome Res 2008, 7:5270-5276.
54. Fu C., Hu J., Liu T., Ago T., Sadoshima J., Li H. Quantitative analysis of redox-sensitive proteome with DIGE and ICAT. J Proteome Res 2008, 7:3789-3802.
55. Leichert L.I., Jakob U. Global methods to monitor the thiol-disulfide state of proteins in vivo. Antioxid Redox Signal 2006, 8:763-772.
56. Sinha V., Wijewickrama G.T., Chandrasena R.E., Xu H., Edirisinghe P.D., Schiefer I.T., Thatcher G.R. Proteomic and mass spectroscopic quantitation of protein S-nitrosation differentiates NO-donors. ACS Chem Biol 2010, 5:667-680.