Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte

Blood

Volumn 109, Issue 6, 2007, Pages 2611-2617

  Low, Felicia M ^a   Hampton, Mark B ^a   Peskin, Alexander V ^a   Winterbourn, Christine C ^a  

^a UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; HYDROGEN PEROXIDE; PEROXIREDOXIN; PEROXIREDOXIN 2; SCAVENGER; SULFONIC ACID DERIVATIVE; THIOL; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

ARTICLE; AUTOOXIDATION; CATALYSIS; DIMERIZATION; ENZYME ACTIVITY; ENZYME SUBSTRATE; ERYTHROCYTE; HEMOLYSATE; HUMAN; HUMAN CELL; HUMAN EXPERIMENT; LEUKEMIA CELL LINE; NORMAL HUMAN; OXIDATION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; T LYMPHOCYTE;

EID: 33947204162     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2006-09-048728     Document Type: Article

References (46)

1. Wood ZA, Schroder E, Harris JR, Poole LB. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem Sci. 2003;28:32-40.
2. Chae H, Chung S, Rhee S. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem. 1994;269:27670-27678.
3. Yang KS, Kang SW, Woo HA, et al. 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. 2002;277:38029-38036.
4. Biteau B, Labarre J, Toledano MB.ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature. 2003;425:980-984.
5. Kang SW, Chae HZ, Seo MS, Kim K, Baines IC, Rhee SG. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem. 1998;273:6297-6302.
6. Kang SW, Rhee SG, Chang T-S, Jeong W, Choi MH. 2-Cys peroxiredoxin function in intracellular signal transduction: therapeutic implications. Trends Mol Med. 2005;11:571-578.
7. Halliwell B, Gutteridge JMC. Free radicals in biology and medicine. 3rd ed. Oxford, United Kingdom: Oxford University Press; 1999.
8. Alayash AI, Patel RP, Cashon RE. Redox reactions of hemoglobin and myoglobin: biological and toxicological implications. Antioxid Redox Signal. 2001;3:313-327.
9. Cohen G, Hochstein P. Glutathione peroxidase: primary agent for elimination of hydrogen peroxide in erythrocytes. Biochemistry. 1963;2:1420-1428.
10. Gaetani GF, Galiano S, Canepa L, Ferraris AM, Kirkman HN. Catalase and glutathione-peroxidase are equally active in detoxification of hydrogen-peroxide in human-erythrocytes. Blood. 1989;73:334-339.
11. Scott MD, Lubin BH, Zuo L, Kuypers FA. Erythrocyte defense against hydrogen peroxide: preeminent importance of catalase. J Lab Clin Med. 1991;118:7-16.
12. Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, Kirkman HN. Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood. 1996;87:1595-1599.
13. Johnson RM, Goyette G Jr, Ravindranath Y, Ho Y-S. Red cells from glutathione peroxidase-1-deficient mice have nearly normal defenses against exogenous peroxides. Blood. 2000;96:1985-1988.
14. Ho Y-S, Xiong Y, Ma W, Spector A, Ho DS. Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury. J Biol Chem. 2004;279:32804-32812.
15. Schroder E, Littlechild JA, Lebedev AA, Errington N, Vagin AA, Isupov MN. Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 angstrom resolution. Structure. 2000;8:605-615.
16. Moore R, Plishker G, Shriver S. Purification and measurement of calpromotin, the cytoplasmic protein which activates calcium-dependent potassium transport. Biochem Biophys Res Commun. 1990;166:146-153.
17. + transport in erythrocyte membrane vesicles requires a cytoplasmic protein. J Biol Chem. 1991;266:18964-18968.
18. Plishker GA, Chevalier D, Seinsoth L, Moore RB. Calcium-activated potassium transport and high molecular weight forms of calpromotin. J Biol Chem. 1992;267:21839-21843.
19. 2 levels in erythrocytes. Free Radic Biol Med. 2005;39:1407-1417.
20. Rabilloud T, Berthier R, Vincon M, Ferbus D, Goubin G, Lawrence J-J. Early events in erythroid differentiation: accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B). Biochem J. 1995;312:699-705.
21. Lim Y-S, Cha M-K, Yun C-H, Kim H-K, Kim K, Kim I-H. Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein. Biochem Biophys Res Commun. 1994;199:199-206.
22. Cha M-K, Yun C-H, Kim I-H. Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane. Biochemistry. 2000;39:6944-6950.
23. Lee T-H, Kim S-U, Yu S-L, et al. Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice. Blood. 2003;101:5033-5038.
24. Zijlstra WG, Buursma A, Meeuwsen-van der Roest WP. Absorption spectra of human fetal and adult oxyhemoglobin, de-oxyhemoglobin, carboxyhemoglobin, and methemoglobin. Clin Chem. 1991;37:1633-1638.
25. Wolff SP. Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Meth Enzymol. 1994;233:182-189.
26. Arnér ES, Zhong L, Holmgren A. Preparation and assay of mammalian thioredoxin and thioredoxin reductase. Meth Enzymol. 1999;300:226-239.
27. Riddles P, Blakeley R, Zerner B. Ellman's reagent: 5,5′- dithiobis(2-nitrobenzoic acid): a reexamination. Anal Biochem. 1979;94:75-81.
28. Beutler E. Red cell metabolism. 3rd ed. Orlando, FL: Grune & Stratton; 1984.
29. Baty JW, Hampton MB, Winterbourn CC. Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells. Biochem J. 2005;389:785-795.
30. Mitsumoto A, Takanezawa Y, Okawa K, Iwamatsu A, Nakagawa Y. Variants of peroxiredoxins expression in response to hydroperoxide stress. Free Radic Biol Med. 2001;30:625-635.
31. Holmgren A, Luthman M. Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay. Biochemistry. 1978;17:4071-4077.
32. Cha M-K, Kim IH. Thioredoxin-linked peroxidase from human red blood cells: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell. Biochem Biophys Res Commun. 1995;217:900-907.
33. Gromer S, Urig S, Becker K. The thioredoxin system: from science to clinic. Med Res Rev. 2004;24:40-89.
34. Mendiratta S, Qu Z-C, May JM. Enzyme-dependent ascorbate recycling in human erythrocytes: role of thioredoxin reductase. Free Radic Biol Med. 1998;25:221-228.
35. Carrell RW, Winterbourn CC, Rachmilewitz EA. Activated oxygen and haemolysis. Br J Haematol. 1975;30:259-264.
36. Winterbourn CC. Free-radical production and oxidative reactions of hemoglobin. Environ Health Perspect. 1985;64:321-330.
37. Hofmann B, Hecht H-J, Flohé L. Peroxiredoxins. Biol Chem. 2002;383:347-364.
38. Parsonage D, Youngblood DS, Sarma GN, Wood ZA, Karplus PA, Poole LB. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry. 2005;44:10583-10592.
39. Wagner E, Luche S, Penna L, et al. A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress. Biochem J. 2002;366:777-785.
40. Giulivi C, Hochstein P, Davies KJA. Hydrogen peroxide production by red blood cells. Free Radic Biol Med. 1994;16:123-129.
41. 2, a necessary evil for cell signaling. Science. 2006;312:1882-1883.
42. Georgiou G, Masip L. An overoxidation journey with a return ticket. Science. 2003;300:592-594.
43. Jang HH, Lee KO, Chi YH, 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.
44. Wood ZA, Poole LB, Hantgan RR, Karplus PA. Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins. Biochemistry. 2002;41:5493-5504.
45. Moon EY, Lee JH, Oh SY, et al. Reaction oxygen species augment B-cell-activating factor expression. Free Radic Biol Med. 2006;40:2103-2111.
46. Moon E-Y, Han Y-H, Lee D-S, Han Y-M, Yu D-Y. Reactive oxygen species induced by the deletion of peroxiredoxin II (Prx II) increases the number of thymocytes resulting in the enlargement of PrxII-null thymus. Eur J Immunol. 2004;34:2119-2128.