Direct evidence for catalase as the predominant H2O2-removing enzyme in human erythrocytes

Blood

Volumn 90, Issue 12, 1997, Pages 4973-4978

  Mueller, Sebastian ^a,b   Riedel, Hans Dieter ^a   Stremmel, Wolfgang ^a  

^a UNIVERSITY OF HEIDELBERG   (Germany)

^b UNIVERSITY OF SOUTHERN CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; HYPOCHLORITE SODIUM; LUMINOL; SODIUM NITRATE;

ARTICLE; CONTROLLED STUDY; DECOMPOSITION; ENZYME ACTIVITY; ERYTHROCYTE; HEMOLYSATE; HUMAN; HUMAN CELL; PRIORITY JOURNAL;

EID: 0031441273     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v90.12.4973     Document Type: Article

References (43)

1. Halliwell B, Gutteridge JMC: Free Radicals in Biology and Medicine (ed 2). Oxford, UK, Clarendon Press, 1989
2. Cadenas E: Biochemistry of oxygen toxicity. Annu Rev Biochem 58:79, 1989
3. 2 toxicity, in Pryor WA (ed): Free Radicals in Biology (vol 1). New York, NY, Academic Press, 1976, p 243
4. Halliwell B, Gutteridge JMC: Role of free radicals and catalyticmetal ions in human disease: An overview. Method Enzymol 186:1, 1990
5. Khan AU, Wilson T: Reactive oxygen species as cellular messengers. Chem Biol 2:437, 1995
6. Fridovich I: Superoxide radical and Superoxide dismutases. Annu Rev Biochem 64:97, 1995
7. Suzuki YJ, Forman HJ, Sevanian A: Oxidants as stimulators of signal transduction. Free Radic Biol Med 22:269, 1997
8. Pantopoulos K, Mueller S, Atzberger A, Ansorge W, Stremmel W, Hentze MW: Differences in the regulation of IRP-1 (iron regulatory protein-1 ) by extra-and intracellular oxidative stress. J Biol Chem 272:9802, 1997
9. Mills GC: Hemoglobin catabolism. 1. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J Biol Chem 229:189, 1957
10. Cohen G, Hochstein P: Glutathione peroxidase: The primary agent for the elimination of hydrogen peroxide in erythrocytes. Biochemistry 2:1420, 1963
11. Jacob HS, Ingbar SH, Jandl JH: Oxidative hemolysis and erythrocyte metabolism in hereditary acatalasia. J Clin Invest 44:1187, 1965
12. Kirkman HN, Gaetani GF: Catalase: A tetrameric enzyme with four tightly bound molecules of NADPH. Proc Natl Acad Sci USA 81:4343, 1984
13. Scott MD, Lubin BH, Zuo L, Kuypers FA: Erythrocyte defense against hydrogen peroxide: Preeminent importance of catalase. J Lab Clin Med 118:7, 1991
14. 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 87:1595, 1996
15. Agar NS, Sadrzadeh SM, Hallaway PE, Eaton JW: Erythrocyte catalase. A somatic oxidant defense? J Clin Invest 77:319, 1986
16. Scott MD, Zuo L, Lubin BH, Chiu DTY: NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes. Blood 77:2059, 1991
17. 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 73:334, 1989
18. Kirkman HN, Galiano S, Gaetani GF: The function of catalase-bound NADPH. J Biol Chem 262:660, 1987
19. Scott MD, Wagner TC, Chiu DT: Decreased catalase activity is the underlying mechanism of oxidant susceptibility in glucose-6-phosphate dehydrogenase-deficient erythrocytes. Biochim Biophys Acta 1181:163, 1993
20. Gaetani GF, Kirkman HN, Mangerini R, Ferraris AM: Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood 84:325, 1994
21. Arnhold J, Mueller S, Arnold K, Grimm E: Chemiluminescence intensities and spectra of luminol oxidation by sodium hypochlorite in the presence of hydrogen peroxide. J Biolumin Chemilumin 6:189, 1991
22. Arnhold J, Mueller S, Arnold K, Sonntag K: Mechanisms of inhibition of chemiluminescence in the oxidation of luminol by sodium hypochlorite. J Biolumin Chemilumin 8:307, 1993
23. 2 concentration in stimulated human neutrophils. J Biolumin Chemilumin 10:229, 1995
24. 2 concentrations, in Hastings JW, Kricka LJ, Stanley PE (eds): Bioluminescence and Chemiluminescence: Molecular Reporting With Photons. Baffins Lane, Chichester, UK, John Wiley & Sons Ltd, 1997, p 462
25. 2 concentrations. Anal Biochem 245:55, 1997
26. Mueller S, Pantopoulos K, Hentze MW, Stremmel W: A chemiluminescence approach to study the regulation of iron metabolism by oxidative stress, in Hastings JW, Kricka LJ, Stanley PE (eds): Bioluminescence and Chemiluminescence: Molecular Reporting With Photons. Baffins Lane, Chichester, UK, John Wiley & Sons Ltd, 1997, p 338
27. Morris JC: The acid ionization constant of HOCl from 5 to 35°. J Phys Chem 70:2798, 1966
28. Beers RF, Sizer IW: A spectrometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195:133, 1952
29. Giulivi C, Hochstein P, Davies KJ: Hydrogen peroxide production by red blood cells. Free Radic Biol Med 16:123, 1994
30. Aebi H: Catalase in vitro. Methods Enzymol 105:121, 1984
31. Flohé L, Günzler W: Assays of glutathione peroxidase. Methods Enzymol 105:114, 1984
32. Ursini F, Maiorino M, Gregolin C: The selenoenzyme phospholipid hydroperoxide gluthathione peroxidase. Biochim Biophys Acta 839:62, 1985
33. Flohé L, Loschen G, Günzler WA, Eichele E: Glutathione peroxidase, V. Hoppe Seylers Z Physiol Chem 353:987, 1972
34. Nicholls P: Activity of catalase in the red cell. Biochim Biophys Acta 99:286, 1965
35. Awasthi YC, Beutler E, Srivastava SK: Purification and properties of human erythrocyte glutathione peroxidase. J Biol Chem 250:5144, 1975
36. Eaton JW, Ma M: Acalasemia, in Scriver CR, Beaudet AL, Sly WS, Valle D (eds): The Metabolic and Molecular Bases of Inherited Disease (ed 7, vol 2). New York, NY, McGraw-Hill, 1995, p 2371
37. Deisseroth A, Dounce AL: Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role. Physiol Rev 50:319, 1970
38. Burdon RH: Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Radie Biol Med 18:775, 1995
39. Keilin D, Hartree EF: Properties of catalase. Catalysis of coupled oxidation of alcohols. Biochem J 39:293, 1945
40. Takahara S: Acatalasemia in Japan, in Beutler E (ed): Hereditary Disorders of Erythrocyte Metabolism. New York, NY, Grune and Stratton, 1968, p 21
41. Aebi H, Bossi E, Cantz M, Matsubara S, Suter H: Acatalasemia in Switzerland, in Beutler E (ed): Hereditary Disorders of Erythrocyte Metabolism. New York, NY, Grune and Stratton, 1968, p 41
42. Cadenas E, Boveris A: Enhancement of hydrogen peroxide formation by protophores and ionophores in antimycin-supplemented mitochondria. Biochem J 188:31, 1980
43. 2 removal in the liver: Different importance of catalase and glutathione peroxidase. Hepatology 24:186A, 1996 (abstr)