Myeloperoxidase

Current Opinion in Hematology

Volumn 7, Issue 1, 2000, Pages 53-58

  Winterbourn, Christine C ^a   Vissers, Margret C M ^a   Kettle, Anthony J ^a  

^a UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

MYELOPEROXIDASE;

ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DEFICIENCY; ENZYME MECHANISM; GENETIC ASSOCIATION; GENETIC POLYMORPHISM; NEUTROPHIL; PHAGOSOME; PRIORITY JOURNAL; PROMOTER REGION; REVIEW;

HUMANS; IMMUNITY, NATURAL; INFLAMMATION; MUTATION; PEROXIDASE; POLYMORPHISM, GENETIC; PROMOTER REGIONS (GENETICS);

EID: 0033989953     PISSN: 10656251     EISSN: None     Source Type: Journal    
DOI: 10.1097/00062752-200001000-00010     Document Type: Review

References (92)

1. 1 Klebanoff SJ: Myeloperoxidase: occurrence and biological function. In Peroxidases in Chemistry and Biology. Edited by Everse J, Everse KE, Grisham MB. Boca Raton: CRC Press; 1991:1 -35.
2. 2 Klebanoff SJ: A peroxidase-mediated antimicrobial system in leukocytes. J Clin Invest 1967, 46:1078.
3. 3 Nauseef WM, McCormick SJ, Clark RA: Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J Biol Chem 1995, 270:4741-4747.
4. 4 Nauseef WM, McCormick SJ, Goedken M: Coordinated participation of calreticulin and calnexin in the biosynthesis of myeloperoxidase. J Biol Chem 1998, 273:7107-7111. This paper shows that calreticulin and calnexin play different roles in chaperoning myeloperoxidase through the endoplasmic reticulum and regulating the proteolytic and heme insertion steps required for protein maturation.
5. 5 Zeng J, Fenna RE: X-ray crystal structure of canine myeloperoxidase at 3 A resolution. J Mol Biol 1992, 226:185-207.
6. 6 Nauseef WM, Cogley M, McCormick S: Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase. J Biol Chem 1996, 271:9546-9549.
7. 7 Romano M, Dri P, Dadalt L, Patriarca P, Baralle FE: Biochemical and molecular characterization of hereditary myeloperoxidase deficiency. Blood 1997, 90:4126-4134.
8. 8 DeLeo FR, Goedken M, McCormick SJ, Nauseef WM: A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation. J Clin Invest 1998, 101:2900-2909. This paper describes a mutant form of myeloperoxidase that acquires heme but undergoes degradation rather than proteolytic processing to mature subunits or secretion. This mutant contrasts with the R569W mutant that does not get processed beyond the apopro form.
9. 9 Nauseef WM, Cogley M, Bock S, Petrides PE: Pattern of inheritance in hereditary myeloperoxidase deficiency associated with the R569W missense mutation. J Leukoc Biol 1998, 63:264-269. This study examined 16 individuals from five unrelated kindreds with the R569W mutation and found that most of the myeloperoxidase-deficient individuals were compound heterozygotes with variable phenotype.
10. 10 Piedrafita FJ, Molander RB, Vansant G, Orlova EA, Pfahl M, Reynolds WF: An Alu element in the myeloperoxidase promoter contains a composite SP1-thyroid hormone-retinoic acid response element. J Biol Chem 1996, 271:14412-14420.
11. 11 Kutter D: Prevalence of myeloperoxidase deficiency: population studies using Bayer-Technicon automated hematology. J Mol Med 1998, 76:669-675.
12. 12 Lanza F: Clinical manifestation of myeloperoxidase deficiency. J Mol Med 1998, 76:676-681.
13. 13 Aratani Y, Koyama H, Nyui S, Suzuki K, Kura F, Maeda N: Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase. Infect Immun 1999, 67:1828-1836. This is the first report describing the generation of myeloperoxidase-deficient mice and their response to infectious challenge. The mice were able to handle S. aureus administered intraperitoneally but showed increased susceptibility to intratracheal and intraperitoneal C. albicans.
14. 14 Kettle AJ, Winterbourn CC: Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Report 1997, 3:3-15.
15. -.
16. 16 Van Dalen CJ, Whitehouse M, Winterbourn CC, Kettle AJ: Oxidation of thiocyanate by myeloperoxidase in the presence of chloride. Biochem J 1997, 327:487-492.
17. 17 Harrison JE, Schultz J: Studies on the chlorinating activity of myeloperoxidase. J Biol Chem 1976, 251:1371-1374.
18. 18 Winterbourn CC: Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim Biophys Acta 1985, 840:204-210.
19. 19 Hazen SL, Hsu FF, Mueller DM, Crowley JR, Heinecke JW: Human neutrophils employ chlorine gas as an oxidant during phagocytosis. J Clin Invest 1996, 98:1283-1289.
20. 20 Marquez LA, Dunford HB: Chlorination of taurine by myeloperoxidase. J Biol Chem 1994, 269:7950-7956.
21. 21 Libby RD, Beachy TM, Phipps AK: Quantitating direct chlorine transfer from enzyme to substrate in chloroperoxidase-catalyzed reactions. J Biol Chem 1996, 271:21820-21827.
22. 2 Klebanoff SJ: A peroxidase-mediated antimicrobial system in leukocytes. J Clin Invest 1967, 46:1078.
23. 3 Nauseef WM, McCormick SJ, Clark RA: Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J Biol Chem 1995, 270:4741-4747.
24. 4 Nauseef WM, McCormick SJ, Goedken M: Coordinated participation of calreticulin and calnexin in the biosynthesis of myeloperoxidase. J Biol Chem 1998, 273:7107-7111. This paper shows that calreticulin and calnexin play different roles in chaperoning myeloperoxidase through the endoplasmic reticulum and regulating the proteolytic and heme insertion steps required for protein maturation.
25. 5 Zeng J, Fenna RE: X-ray crystal structure of canine myeloperoxidase at 3 A resolution. J Mol Biol 1992, 226:185-207.
26. 6 Nauseef WM, Cogley M, McCormick S: Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase. J Biol Chem 1996, 271:9546-9549.
27. 7 Romano M, Dri P, Dadalt L, Patriarca P, Baralle FE: Biochemical and molecular characterization of hereditary myeloperoxidase deficiency. Blood 1997, 90:4126-4134.
28. 8 DeLeo FR, Goedken M, McCormick SJ, Nauseef WM: A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation. J Clin Invest 1998, 101:2900-2909. This paper describes a mutant form of myeloperoxidase that acquires heme but undergoes degradation rather than proteolytic processing to mature subunits or secretion. This mutant contrasts with the R569W mutant that does not get processed beyond the apopro form.
29. 9 Nauseef WM, Cogley M, Bock S, Petrides PE: Pattern of inheritance in hereditary myeloperoxidase deficiency associated with the R569W missense mutation. J Leukoc Biol 1998, 63:264-269. This study examined 16 individuals from five unrelated kindreds with the R569W mutation and found that most of the myeloperoxidase-deficient individuals were compound heterozygotes with variable phenotype.
30. 10 Piedrafita FJ, Molander RB, Vansant G, Orlova EA, Pfahl M, Reynolds WF: An Alu element in the myeloperoxidase promoter contains a composite SP1-thyroid hormone-retinoic acid response element. J Biol Chem 1996, 271:14412-14420.
31. 11 Kutter D: Prevalence of myeloperoxidase deficiency: population studies using Bayer-Technicon automated hematology. J Mol Med 1998, 76:669-675.
32. 12 Lanza F: Clinical manifestation of myeloperoxidase deficiency. J Mol Med 1998, 76:676-681.
33. 13 Aratani Y, Koyama H, Nyui S, Suzuki K, Kura F, Maeda N: Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase. Infect Immun 1999, 67:1828-1836. This is the first report describing the generation of myeloperoxidase-deficient mice and their response to infectious challenge. The mice were able to handle S. aureus administered intraperitoneally but showed increased susceptibility to intratracheal and intraperitoneal C. albicans.
34. 14 Kettle AJ, Winterbourn CC: Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Report 1997, 3:3-15.
35. -.
36. 16 Van Dalen CJ, Whitehouse M, Winterbourn CC, Kettle AJ: Oxidation of thiocyanate by myeloperoxidase in the presence of chloride. Biochem J 1997, 327:487-492.
37. 17 Harrison JE, Schultz J: Studies on the chlorinating activity of myeloperoxidase. J Biol Chem 1976, 251:1371-1374.
38. 18 Winterbourn CC: Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim Biophys Acta 1985, 840:204-210.
39. 19 Hazen SL, Hsu FF, Mueller DM, Crowley JR, Heinecke JW: Human neutrophils employ chlorine gas as an oxidant during phagocytosis. J Clin Invest 1996, 98:1283-1289.
40. 20 Marquez LA, Dunford HB: Chlorination of taurine by myeloperoxidase. J Biol Chem 1994, 269:7950-7956.
41. 21 Libby RD, Beachy TM, Phipps AK: Quantitating direct chlorine transfer from enzyme to substrate in chloroperoxidase-catalyzed reactions. J Biol Chem 1996, 271:21820-21827.
42. 22 Marquez LA, Dunford HB: Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II. J Biol Chem 1996, 270:30434-30440.
43. 23 van der Vliet A, Eiserich JP, Halliwell B, Cross CE: Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite: a potential additional mechanism of nitric oxide-dependent toxicity. J Biol Chem 1997, 272:7617-7625.
44. 24 Eiserich JP, Hristova M, Cross CE, Jones AD, Freeman BA, Halliwell B, van der Vliet A: Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils. Nature 1998, 391:393-397. This important paper demonstrates for the first time that neutrophils promote nitration of tyrosyl residues by the myeloperoxidase-dependent oxidation of nitrite. Experimental data implicated both nitrogen dioxide and nitryl chloride in this process.
45. 25 Sampson JB, Ye YZ, Rosen H, Beckman JS: Myeloperoxidase and horse-radish peroxidase catalyze tyrosine nitration in proteins from nitrite and hydrogen peroxide. Arch Biochem Biophys 1998, 356:207-213.
46. 6 /M/s.
47. 3 /M/s.
48. 28 Kettle AJ, Gedye CA, Hampton MB, Winterbourn CC: Inhibition of myeloperoxidase by benzoic acid hydrazides. Biochem J 1995, 308:559-563.
49. 29 Hampton MB, Kettle AJ, Winterbourn CC: Inside the neutrophil phagosome: oxidants, myeloperoxidase and bacterial killing. Blood 1998, 92:3007-3017.
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53. 33 Hampton MB, Kettle AJ, Winterbourn CC: The involvement of Superoxide and myeloperoxidase in oxygen-dependent bacterial killing. Infect Immun 1996,64:3512-3517.
54. 34 Winterbourn CC, Brennan SO: Characterisation of the oxidation products of the reaction between reduced glutathione and hypochlorous acid. Biochem J 1997, 326:87-92.
55. 35 Anderson MM, Hazen SL, Hsu FF, Heinecke JW: Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycoaldehyde, 2-hydroxypropanol, and acrolein: a mechanism for the generation of highly reactive α-hydroxy and α,β-unsaturated aldehydes by phagocytes at sites of inflammation. J Clin Invest 1997, 99:424-432.
56. 36 Hazen SL, d'Avignon A, Anderson MM, Hsu FF, Heinecke JW: Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes: mechanistic studies identifying labile intermediates along the reaction pathway. J Biol Chem 1998, 273:4997-5005.
57. 37 Anderson MM, Requena JR, Crowley JR, Thorpe SR, Heinecke JW: The myeloperoxidase system of human phagocytes generates Nε-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation. J Clin Invest 1999, 104:103-113. This paper extends earlier work characterizing the breakdown of chloramines to aldehydes. They show that chloramines formed from α-amino acids are much less stable than taurine chloramine and have half-lives of about 8 minutes, α-Hydroxy-or α,β-unsaturated aldehydes produced from hydroxyaminoacids readily form addition products with proteins.
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66. 46 Savenkova ML, Mueller DM, Heinecke JW: Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid peroxidation in low density lipoprotein. J Biol Chem 1994, 269:20394-20400.
67. - system converted LDL into a species that was rapidly taken up by mouse or human macrophages, even in the presence of physiologic concentrations of chloride.
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84. 64 Schoonbroodt S, Legrand-Poels S, Best-Belpomme M, Piette J: Activation of the NF-κB transcription factor in a T-lymphocytic cell line by hypochlorous acid. Biochem J 1997, 321:777-785.
85. 65 Dukan S, Belkin S, Touati D: Reactive oxygen species are partially involved in the bacteriocidal action of hypochlorous acid. Arch Biochem Biophys 1999, 367:311-316. This paper shows that bacteria treated with low-dose hypochlorous acid have a lower survival when subsequently plated in air compared with under anaerobic conditions. Bacteria deficient in Superoxide dismutase or glucose-6-phosphate dehydrogenase were more susceptible, suggesting that hypochlorous acid compromises the cells' ability to withstand endogenously generated oxidants.
86. 66 Kallenberg CG: Autoantibodies to myeloperoxidase: clinical and patho-physiological significance. J Mol Med 1998, 76:682-687.
87. 67 Franssen C, Gans R, Kallenberg C, Hageluken C, Hoorntje S: Disease spectrum of patients with antineutrophil cytoplasmic autoantibodies of defined specificity: distinct differences between patients with anti-proteinase 3 and anti-myeloperoxidase autoantibodies. J Intern Med 1998, 244:209-216. This retrospective analysis of 92 patients provides a useful overview of the clinical profile associated with antineutrophil cytoplasmic autoantibodies.
88. 68 Reynolds WF, Chang E, Douer D, Ball ED, Kanda V: An allelic association implicates myeloperoxidase in the etiology of acute promyelocytic leukemia. Blood 1997, 90:2730-2737.
89. 69 Nagra RM, Becher B, Tourtellotte WW, Antel JP, Gold D, Paladino T, et al.: Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis. J Neuroimmunol 1997, 78:97-107.
90. 70 Reynolds WF, Rhees J, Maciejewski D, Paladino T, Sieburg H, Maki RA, Masliah E: Myeloperoxidase polymorphism is associated with gender specific risk for Alzheimer's disease. Exp Neurol 1999, 155:31 -41. The GG genotype in the SP1 promoter was found to be overrepresented in women (73%) but not in men (48%) with Alzheimer's disease. Their data also suggest that myeloperoxidase gene expression can be induced in microglia in the brain.
91. 71 London SJ, Lehman TA, Taylor JA: Myeloperoxidase genetic polymorphism and lung cancer risk. Cancer Res 1997, 57:5001-5003.
92. 72 Foster CB, Lehrnbecher T, Mol F, Steinberg SM, Venzon DJ, Walsh TJ, et al.: Host defense molecule polymorphisms influence the risk for immune-mediated complications in chronic granulomatous disease. J Clin Invest 1998, 102:2146-2155. Patients with chronic granulomatous disease who are homozygous for the G allele in the SP1 promoter of myeloperoxidase were found to have a 54% chance of one or more major gastrointestinal or genitourinary infectious complications compared with 27.5% of other patients.