A colorimetric assay for sulfiredoxin activity using inorganic phosphate measurement

Analytical Biochemistry

Volumn 393, Issue 1, 2009, Pages 36-40

  Kim, Hojin ^a   Kim, Hyeryeon ^a   Hong, Sohyun ^a   Rhee, Sue Goo ^a   Jeong, Woojin ^a  

^a Ewha Womans University   (South Korea)

Author keywords

2 Cys peroxiredoxin; Hyperoxidation; Malachite green; Phosphate assay; Sulfiredoxin

Indexed keywords

AMINO ACIDS; CARBONATE MINERALS; CHEMICAL DETECTION; COLOR; ENZYMES; OXIDATION; PEROXIDES;

2-CYS PEROXIREDOXIN; HYPEROXIDATION; MALACHITE GREEN; PHOSPHATE ASSAY; SULFIREDOXIN;

COLORIMETRY;

ENZYME INHIBITOR; MALACHITE GREEN; PEROXIREDOXIN; PHOSPHATE; SULFINIC ACID DERIVATIVE; SULFIREDOXIN; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; CATALYSIS; COLORIMETRY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME METABOLISM; ENZYME SYNTHESIS; HIGH THROUGHPUT SCREENING; HUMAN; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS;

EID: 67650976330     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.06.030     Document Type: Article

References (40)

1. Rhee S.G., Kang S.W., Chang T.S., Jeong W., and Kim K. Peroxiredoxin, a novel family of peroxidases. IUBMB Life 52 (2001) 35-41
2. Hofmann B., Hecht H.J., and Flohe L. Peroxiredoxins. Biol. Chem. 383 (2002) 347-364
3. Wood Z.A., Schroder E., Robin Harris J., and Poole L.B. Structure, mechanism, and regulation of peroxiredoxins. Trends Biochem. Sci. 28 (2003) 32-40
4. Rhee S.G., Chae H.Z., and Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 38 (2005) 1543-1552
5. Rhee S.G., Kang S.W., Jeong W., Chang T.S., Yang K.S., and Woo H.A. Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17 (2005) 183-189
6. Chae H.Z., Chung S.J., and Rhee S.G. Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269 (1994) 27670-27678
7. Chae H.Z., Uhm T.B., and Rhee S.G. Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc. Natl. Acad. Sci. USA 91 (1994) 7022-7026
8. Yang K.S., Kang S.W., Woo H.A., Hwang S.C., Chae H.Z., Kim K., and Rhee S.G. Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J. Biol. Chem. 277 (2002) 38029-38036
9. Rabilloud T., Heller M., Gasnier F., Luche S., Rey C., Aebersold R., Benahmed M., Louisot P., and 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
10. Woo H.A., Chae H.Z., Hwang S.C., Yang K.S., Kang S.W., Kim K., and Rhee S.G. Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 300 (2003) 653-656
11. Woo H.A., Kang S.W., Kim H.K., Yang K.S., Chae H.Z., and Rhee S.G. Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulfinic acid: immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence. J. Biol. Chem. 278 (2003) 47361-47364
12. Biteau B., Labarre J., and Toledano M.B. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425 (2003) 980-984
13. Chang T.S., Jeong W., Woo H.A., Lee S.M., Park S., and Rhee S.G. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J. Biol. Chem. 279 (2004) 50994-51001
14. Woo H.A., Jeong W., Chang T.S., Park K.J., Park S.J., Yang J.S., and Rhee S.G. Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins. J. Biol. Chem. 280 (2005) 3125-3128
15. Jeong W., Park S.J., Chang T.S., Lee D.Y., and Rhee S.G. Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin. J. Biol. Chem. 281 (2006) 14400-14407
16. Jonsson T.J., Murray M.S., Johnson L.C., and Lowther W.T. Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate. J. Biol. Chem. 283 (2008) 23846-23851
17. Roussel X., Bechade G., Kriznik A., Van Dorsselaer A., Sanglier-Cianferani S., Branlant G., and Rahuel-Clermont S. Evidence for the formation of a covalent thiosulfinate intermediate with peroxiredoxin in the catalytic mechanism of sulfiredoxin. J. Biol. Chem. 283 (2008) 22371-22382
18. Van Veldhoven P.P., and Mannaerts G.P. Inorganic and organic phosphate measurements in the nanomolar range. Anal. Biochem. 161 (1987) 45-48
19. D'Angelo E., Crutchfield J., and Vandiviere M. Rapid, sensitive, microscale determination of phosphate in water and soil. J. Environ. Qual. 30 (2001) 2206-2209
20. Kang S.W., Baines I.C., and Rhee S.G. Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273 (1998) 6303-6311
21. Van Belle H. New and sensitive reaction for automatic determination of inorganic phosphate and its application to serum. Anal. Biochem. 33 (1970) 132-142
22. Debruyne I. Inorganic phosphate determination: colorimetric assay based on the formation of a rhodamine B-phosphomolybdate complex. Anal. Biochem. 130 (1983) 454-460
23. Burns D.T., Chimpalee D., Chimpalee N., and Ittipornkul S. Flow-injection spectrophotometric determination of phosphate using crystal violet. Anal. Chim. Acta 254 (1991) 197-200
24. Soyenkoff B.C. An improved micromethod of phosphate determination. J. Biol. Chem. 198 (1952) 221-227
25. Murphy J., and Riley J.P. A modified single solution method for the determination of phosphate in natural waters. Anal. Chim. Acta 27 (1962) 31-36
26. Tobey S.L., and Anslyn E.V. Determination of inorganic phosphate in serum and saliva using a synthetic receptor. Org. Lett. 5 (2003) 2029-2031
27. Webb M.R. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl. Acad. Sci. USA 89 (1992) 4884-4887
28. Zhou M., Diwu Z., Panchuk-Voloshina N., and Haugland R.P. A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal. Biochem. 253 (1997) 162-168
29. Cogan E.B., Birrell G.B., and Griffith O.H. A robotics-based automated assay for inorganic and organic phosphates. Anal. Biochem. 271 (1999) 29-35
30. Finkel T. Oxygen radicals and signaling. Curr. Opin. Cell Biol. 10 (1998) 248-253
31. Finkel T. Oxidant signals and oxidative stress. Curr. Opin. Cell Biol. 15 (2003) 247-254
32. Rhee S.G., Bae Y.S., Lee S.-R., and Kwon J. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE 53 (2000) 10.1126/stke.2000.53.pe1
33. Rhee S.G., Chang T.S., Bae Y.S., Lee S.R., and Kang S.W. Cellular regulation by hydrogen peroxide. J. Am. Soc. Nephrol. 14 (2003) S211-S215
34. Finkel T., and Holbrook N.J. Oxidants, oxidative stress, and the biology of ageing. Nature 408 (2000) 239-247
35. Klaunig J.E., and Kamendulis L.M. The role of oxidative stress in carcinogenesis. Annu. Rev. Pharmacol. Toxicol. 44 (2004) 239-267
36. Choi M.H., Lee I.K., Kim G.W., Kim B.U., Han Y.H., Yu D.Y., Park H.S., Kim K.Y., Lee J.S., Choi C., Bae Y.S., Lee B.I., Rhee S.G., and Kang S.W. Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II. Nature 435 (2005) 347-353
37. Kang S.W., Rhee S.G., Chang T.S., Jeong W., and Choi M.H. 2-Cys peroxiredoxin function in intracellular signal transduction: therapeutic implications. Trends Mol. Med. 11 (2005) 571-578
38. 2, a necessary evil for cell signaling. Science 312 (2006) 1882-1883
39. Rhee S.G., Jeong W., Chang T.S., and Woo H.A. Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: its discovery, mechanism of action, and biological significance. Kidney Intl. Suppl. (2007) S3-S8
40. Wei Q., Jiang H., Matthews C.P., and Colburn N.H. Sulfiredoxin is an AP-1 target gene that is required for transformation and shows elevated expression in human skin malignancies. Proc. Natl. Acad. Sci. USA 105 (2008) 19738-19743