Chapter 19 Measuring Redox Changes to Mitochondrial Protein Thiols With Redox Difference Gel Electrophoresis (Redox-Dige)

Methods in Enzymology

Volumn 456, Issue A, 2009, Pages 343-361

  Hurd, Thomas R ^a   James, Andrew M ^a   Lilley, Kathryn S ^b   Murphy, Michael P ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE; MALEIMIDE DERIVATIVE; MITOCHONDRIAL PROTEIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; THIOL DERIVATIVE;

CELL LEVEL; GEL ELECTROPHORESIS; LIPID OXIDATION; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MODIFICATION; REVIEW; SIGNAL TRANSDUCTION;

ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; FLUORESCENT DYES; MITOCHONDRIA; OXIDATION-REDUCTION; PROTEINS; SULFHYDRYL COMPOUNDS;

EID: 63449092167     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)04419-4     Document Type: Review

References (47)

1. Alban A., David S.O., Bjorkesten L., Andersson C., Sloge E., Lewis S., and Currie I. A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 3 (2003) 36-44
2. Baty J.W., Hampton M.B., and Winterbourn C.C. Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells. Biochem. J. 389 (2005) 785-795
3. Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., and Murphy M.P. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: Implications for mitochondrial redox regulation and antioxidant defense. J. Biol. Chem. 279 (2004) 47939-47951
4. Beltran B., Orsi A., Clementi E., and Moncada S. Oxidative stress and S-nitrosylation of proteins in cells. Br. J. Pharmacol. 129 (2000) 953-960
5. Braun R.J., Kinkl N., Beer M., and Ueffing M. Two-dimensional electrophoresis of membrane proteins. Anal. Bioanal. Chem. 389 (2007) 1033-1045
6. Cadenas E., and Davies K.J. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic. Biol. Med. 29 (2000) 222-230
7. Carroll J., Altman M.C., Fearnley I.M., and Walker J.E. Identification of membrane proteins by tandem mass spectrometry of protein ions. Proc. Natl. Acad. Sci. USA 104 (2007) 14330-14335
8. Chan H.L., Gharbi S., Gaffney P.R., Cramer R., Waterfield M.D., and Timms J.F. Proteomic analysis of redox- and ErbB2-dependent changes in mammary luminal epithelial cells using cysteine- and lysine-labelling two-dimensional difference gel electrophoresis. Proteomics 5 (2005) 2908-2926
9. Chance B., Sies H., and Boveris A. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59 (1979) 527-605
10. Chang T.S., Cho C.S., Park S., Yu S., Kang S.W., and Rhee S.G. Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria. J. Biol. Chem. 279 (2004) 41975-41984
11. Chappell J.B., and Hansford R.G. In: Birnie G.D. (Ed). Subcellular components: Preparation and Fractionation (1972), Butterworths, London 77-91
12. Cochemé H.M., and Murphy M.P. Complex I is the major site of mitochondrial superoxide production by paraquat. J. Biol. Chem. 283 (2008) 1786-1798
13. Dahm C.C., Moore K., and Murphy M.P. Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite: Implications for the interaction of nitric oxide with mitochondria. J. Biol. Chem. 281 (2006) 10056-10065
14. Eaton P. Protein thiol oxidation in health and disease: Techniques for measuring disulfides and related modifications in complex protein mixtures. Free Radic. Biol. Med. 40 (2006) 1889-1899
15. Finkel T. Oxidant signals and oxidative stress. Curr. Opin. Cell Biol. 15 (2003) 247-254
16. Fu C., Hu J., Liu T., Ago T., Sadoshima J., and Li H. Quantitative analysis of redox-sensitive proteome with DIGE and ICAT. J. Proteome Res. 7 (2008) 3789-3802
17. Gharbi S., Gaffney P., Yang A., Zvelebil M.J., Cramer R., Waterfield M.D., and Timms J.F. Evaluation of two-dimensional differential gel electrophoresis for proteomic expression analysis of a model breast cancer cell system. Mol. Cell. Proteomics. 1 (2002) 91-98
18. Gitler C., Zarmi B., and Kalef E. General method to identify and enrich vicinal thiol proteins present in intact cells in the oxidized, disulfide state. Anal. Biochem. 252 (1997) 48-55
19. Gorg A., Weiss W., and Dunn M.J. Current two-dimensional electrophoresis technology for proteomics. Proteomics 4 (2004) 3665-3685
20. Gregory J.D. The stability of N-ethylmaleimide and its reaction with sulfhydryl groups. J. Am. Chem. Soc. 77 (1955) 3922-3923
21. Gygi S.P., Rist B., Gerber S.A., Turecek F., Gelb M.H., and Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17 (1999) 994-999
22. Henningsen R., Gale B.L., Straub K.M., and DeNagel D.C. Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2 (2002) 1479-1488
23. Hu Y., Wang G., Chen G.Y., Fu X., and Yao S.Q. Proteome analysis of Saccharomyces cerevisiae under metal stress by two-dimensional differential gel electrophoresis. Electrophoresis 24 (2003) 1458-1470
24. Hurd T.R., Costa N.J., Dahm C.C., Beer S.M., Brown S.E., Filipovska A., and Murphy M.P. Glutathionylation of mitochondrial proteins. Antioxid. Redox. Signal 7 (2005) 999-1010
25. Hurd T.R., Prime T.A., Harbour M.E., Lilley K.S., and Murphy M.P. Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: Implications for mitochondrial redox signaling. J. Biol. Chem. 282 (2007) 22040-22051
26. Hurd T.R., Raquejo R., Filipovska A., Brown S., Prime T.A., Robinson A.J., Fearnley I.M., and Murphy M.P. Complex I within oxidatively-stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: Potential role of Cys residues in decreasing oxidative damage. J. Biol. Chem. 283 (2008) 24801-24815
27. Issaq H., and Veenstra T. Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE): Advances and perspectives. Biotechniques 44 (2008) 697-700
28. Karp N.A., Kreil D.P., and Lilley K.S. Determining a significant change in protein expression with DeCyder during a pair-wise comparison using two-dimensional difference gel electrophoresis. Proteomics 4 (2004) 1421-1432
29. Kil I.S., and Park J.W. Regulation of mitochondrial NADP+-dependent isocitrate dehydrogenase activity by glutathionylation. J. Biol. Chem. 280 (2005) 10846-10854
30. Lilley K.S., and Friedman D.B. All about DIGE: Quantification technology for differential-display 2D-gel proteomics. Expert Rev. Proteomics 1 (2004) 401-409
31. Lin T.K., Hughes G., Muratovska A., Blaikie F.H., Brookes P.S., Darley-Usmar V., Smith R.A., and Murphy M.P. Specific modification of mitochondrial protein thiols in response to oxidative stress: A proteomics approach. J. Biol. Chem. 277 (2002) 17048-17056
32. Low F.M., Hampton M.B., Peskin A.V., and Winterbourn C.C. Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 109 (2007) 2611-2617
33. Murphy M.P. How mitochondria produce reactive oxygen species. Biochem. J. 417 (2009) 1-13
34. Perkins D.N., Pappin D.J., Creasy D.M., and Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
35. Poole L.B., Karplus P.A., and Claiborne A. Protein sulfenic acids in redox signaling. Annu. Rev. Pharmacol. Toxicol. 44 (2004) 325-347
36. 2, a necessary evil for cell signaling. Science 312 (2006) 1882-1883
37. Salmeen A., Andersen J.N., Myers M.P., Meng T.C., Hinks J.A., Tonks N.K., and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423 (2003) 769-773
38. Smyth D.G., Nagamatsu A., and Fruton J.S. Some Reactions of N-ethylmaleimide. Anal. Biochem. 82 (1960) 4600-4604
39. Stamler J.S. Redox signaling: Nitrosylation and related target interactions of nitric oxide. Cell 78 (1994) 931-936
40. Taylor E.R., Hurrell F., Shannon R.J., Lin T.K., Hirst J., and Murphy M.P. Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J. Biol. Chem. 278 (2003) 19603-19610
41. Thomas J.A., Poland B., and Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch. Biochem. Biophys. 319 (1995) 1-9
42. Unlu M., Morgan M.E., and Minden J.S. Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis 18 (1997) 2071-2077
43. Van den Bergh G., Clerens S., Vandesande F., and Arckens L. Reversed-phase high-performance liquid chromatography prefractionation prior to two-dimensional difference gel electrophoresis and mass spectrometry identifies new differentially expressed proteins between striate cortex of kitten and adult cat. Electrophoresis 24 (2003) 1471-1481
44. Wilm M., Shevchenko A., Houthaeve T., Breit S., Schweigerer L., Fotsis T., and Mann M. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379 (1996) 466-469
45. Winterbourn C.C., and Hampton M.B. Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med. 45 (2008) 549-561
46. Wittig I., and Schagger H. Features and applications of blue-native and clear-native electrophoresis. Proteomics 8 (2008) 3974-3990
47. Yan J.X., Devenish A.T., Wait R., Stone T., Lewis S., and Fowler S. Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics 2 (2002) 1682-1698