- Hampton MB, Kettle AJ, Winterbourn CC. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 1998; 92: 3007–3017.
- Klebanoff SJ. Myeloperoxidase. Proc Assoc Am Physicians 1999; 111: 383–389.
- Podrez EA, Schmitt D, Hoff HF, Hazen SL. Myeloperoxidase-generated reactive nitrogen species convert LDL into an atherogenic form in vitro. J Clin Invest 1999; 103: 1547-1560.
- Whitman SC, Hazen SL, Miller DB, Hegele RA, Heinecke JW, Huff MW. Modification of type ifi VLDL, their remnants, and VLDL from ApoE-knockout mice by p-hydroxyphenyl-acetaldehyde, a product of myeloperoxidase activity, causes marked cholesteryl ester accumulation in macrophages. Arterioscler Thromb Vasc Biol 1999; 19: 1238–1249.
- Heller JI, Crowley JR, Hazen SL, Salvay DM, Wagner P, Pennathur S. p-Hydroxyphenylacetaldehyde, an aldehyde generated by myloperoxidase, modified phospholipid amino groups of low density lipoprotein in human atherosclerotic J Biol Chem 2000; 275: 9957-9962.
- Reynolds WE The role of myeloperoxidase in myeloid leukemia and multiple sclerosis. In: Nauseef WM, Petrides PE, eds. The Peroxidase Multigene Family of Enzymes. Berlin: Springer, 2000; In press.
- Nagra R, Becher B, Tourtellotte WW, Antel JP, Gold D, Palidino T. Immunohistochemical and genetic evidence of myeloperoxidase involvement in multiple sclerosis. J Neuroimmunol 1997; 78: 97–107.
- Reynolds WF, Rhees J, Maciejewski D et al. Myeloperoxidase polymorphism is associated with gender specific risk for Alzheimer's disease. Exp Neurol 1999; 155: 31–41.
- Jolivalt C, Leininger-Muller B, Drozdz R, Naskalski JW, Siest G. Apolipoprotein E is highly susceptible to oxidation by myeloperoxidase, an enzyme present in the brain. Neurosci Lett 1996; 210: 61–64.
- Nauseef WM, Brigham S, Cogley M. Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan. J Biol Chem 1994; 269: 1212–1216.
- 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.
- Romano M, Dri P, Dadalt L, Patriarca P, Baralle FE. Biochemical and molecular characterization of hereditary myeloperoxidase deficiency. Blood 1997; 90: 4126–4134.
- Nauseef WM, Petrides PE. Peroxidases and human disease: a meeting of minds. Mol Med Today 1999; 5: 58–60.
- Fiedler TJ, Davey CA, Fenna RE. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J Biol Chem 2000; 275: 11964–11971.
- Henderson LM, Chappell JB. NADPH oxidase of neutrophils. Biochim Biophys Acta 1996; 1273: 87–107.
- Kettle AJ, Winterbourn CC. Superoxide enhances hypochlorous acid production by stimulated human neutrophils. Biochim Biophys Acta 1990; 1052: 379–385.
- 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.
- Zgliczynski JM, Stelmaszynska T, Domanski J, Ostrowski W. Chloramines as intermediates of oxidative reaction of amino acids by myeloperoxidase. Biochim Biophys Acta 1971; 235: 419–424.
- Strauss RR, Paul BB, Jacobs AA, Sbarra AJ. Role of the phagocyte in host-parasite interactions. VCVII Myeloperoxidase-11202-C1- mediated aldehyde formation and its relationship to antimicrobial activity. Infect Immun 1971; 3: 595–602.
- Moguilevsky N, Garcia-Quintana L, Jacquet A et al. Structural and biological properties of human recombinant myeloperoxidase produced by Chinese hamster ovary cell lines. Eur J Biochem 1991; 197: 605–614.
- DeGioia L, Ghibaudi EM, Laurenti E, Salmona M, Ferrari RP. A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scaffold of the myeloperoxidase X-ray structure. J Biol Inorg Chem 1996; 1: 476–485.
- Kooter IM, Pierik AJ, Merkx M et al. Difference Fourier transform infrared evidence for ester bonds linking the heme group in myeloperoxidase, lactoperoxidase, and eosinophil peroxidase. J Am Chem Soc 1997; 119: 11542–11543.
- Ferrari RP. Structure function relationships amongst members of the animal peroxidase family of proteins. In: Nauseef WM, Petrides PE, eds. The Peroxidase Multigene Family of Enzymes. Berlin: Springer, 2000.
- Kooter IM, Moguilevsky N, Bonen A et al. Characterization of the Asp94 and G1u242 mutants in myeloperoxidase, the residues linking the heme group via ester bonds. Eur J Biochem 1999; 264: 211–217.
- Kooter IM, Moguilevsky N, Bonen A et al. The sulfonium ion linkage in myeloperoxidase. J Biol Chem 1999; 274: 26794–26802.
- Johnson KR, Nauseef WM, Care A et al. Characterization of cDNA clones for human myeloperoxidase: Predicted amino acid sequence and evidence for multiple mRNA species. Nucleic Acids Res 1987; 15: 2013–2028.
- Nauseef WM. Aberrant restriction endonuclease digests of DNA from subjects with hereditary myeloperoxidase deficiency. Blood 1989; 73: 290–295.
- Nauseef WM, McCormick SJ, Clark RA. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J Biol Chem 1995; 270: 4741–4747.
- Nauseef WM, McCormick SJ, Goedken M. Co-ordinated participation of calreticulin and calnexin in the biosynthesis of myeloperoxidase. J Biol Chem 1998; 273: 7107–7111.
- Nauseef WM, Cogley M, McCormick S. Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase. J Biol Chem 1996; 271: 9546–9549.
- Nauseef WM. Insights into myeloperoxidase biosynthesis from its inherited deficiency. J Mol Med 1998; 76: 661–668.
- Nauseef WM. Myeloperoxidase biosynthesis by a human promyelocytic leukemia cell line: insight into myeloperoxidase deficiency. Blood 1986; 67: 865–872.
- Nauseef WM. Myeloperoxidase deficiency. Hematol Oncol Clin North Am 1988; 2: 135–158.
- Nauseef WM. Posttranslational processing of a human myeloid lysosomal protein, myeloperoxidase. Blood 1987; 70: 1143–1150.
- Nauseef WM. Quality control in the endoplasmic reticulum: lessons from hereditary myeloperoxidase deficiency. J Lab Clin Med 1999; 134: 215–221.
- Nauseef WM, McCormick S, Yi H. Roles of heme insertion and the mannose-6-phosphate receptor in processing of the human myeloid lysosomal enzyme, myeloperoxidase. Blood 1992; 80: 2622–2633.
- Gullberg U, Bengtsson N, Billow E, Garwicz D, Lindmark A, Olsson I. Processing and targeting of granule proteins in human neutrophils. J Immunol Methods 1999; 232: 201–210.
- Gullberg U, Andersson E, Garwicz D, Lindmark A, Olsson I. Biosynthesis, processing and sorting of neutrophil proteins: insight into neutrophil granule development. Eur J Haematol 1997; 58: 137–153.
- Dinauer MC, Nauseef WM, Newburger PE. Inherited disorders of phagocyte killing. In: Scriver CR, Beaudet AL, Sly WS, Valle D, Vogelstein B, Childs B, eds. The Metabolic and Molecular Bases of Inherited Diseases. New York, NY: McGraw-Hill, 2000; In press.
- Piedrafita FJ, Molander RB, Vansant G, Orlova EA, Pfahl M, Reynolds WE An Mu element in the myeloperoxidase promoter contains a composite SP1-thyroid hormone-retinoic acid response element. J Biol Chem 1996; 271: 14412–14420.
- 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.
- Cascorbi I, Henning S, Brockmoller J et al. Substantially reduced risk of cancer of the aerodigestive tract in subjects with variant-463A of the myeloperoxidase gene. Cancer Res 2000; 60: 644–649.
- Le Marchand L, Seifried A, Lum A, Wilkens LR. Association of the myeloperoxidase -463GA polymorphism with lung cancer risk. Cancer Epidemiol Biomarkers Prey 2000; 9: 181–184.
- Hashinaka K, Nishio C, Hur SJ, Sakiyama F, Tsunasawa S, Yamada M. Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation. Biochemistry 1988; 27: 5906–5914.
- Hur SJ, Toda H, Yamada M. Isolation and characterization of an unprocessed extracellular myeloperoxidase in HL-60 cell cultures. J Biol Chem 1989; 264: 8542–8548.
- Taylor KL, Guzman GS, Burgess CA, Kinkade JM. Jr Assembly of dimeric myeloperoxidase during posttranslational maturation in human leukemic HL-60 cells. Biochemistry 1990; 29: 1533–1539.
- Van Leeuwen JEM, Kearse KP. Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes. Proc Natl Acad Sci USA 1996; 93: 13997–14001.
- Benoist F, Grand-Perret T. Co-translational degradation of apolipoprotein B100 by the proteasome is prevented by microsomal triglyceride transfer protein. J Biol Chem 1997; 272: 20435–20442.
- DeLeo FR, Burritt JB, Yu L, Jesaitis AJ, Dinauer MC, Nauseef WM. Processing and maturation of fiavocytochrome b558 includes incorporation of heme as a prerequisite for heterodimer assembly. J Biol Chem 2000; 275: 13986–13993.
- Nauseef WM, Cogley M, Bock S, Petrides PE. Pattern of inherit-ance in hereditary myeloperoxidase deficiency associated with the R569W missense mutation. J Leukoc Biol 1998; 63: 264–269.
- Van Dalen CJ, Whitehouse MW, Winterbourn CC, Kettle AJ. Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem J 1997; 327: 487–492.
- Arnljots K, Olsson I. Myeloperoxidase precursors incorporate heme. J Biol Chem 1987; 262: 10430–10434.
- Zeng J, Fenna RE. X-ray crystal structure of canine myeloperoxidase at 3 A resolution. J Mol Biol 1992; 226: 185–207.
- Lee DH, Goldberg AL. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol 1998; 8: 397–403.
- Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, Riordan JR. Multiple proteolytic systems, including the proteasome, contribute to CF IR processing. Cell 1995; 83: 129–135.
- Andrews PC, Parnes C, Krinsky NI. Comparison of myeloperoxidase and hemi-myeloperoxidase with respect to catalysis, regulation, and bactericidal activity. Arch Biochem Biophys 1984; 228: 439–442.
- Fenteany G, Schreiber SL. Lactacystin, proteasome function, and cell fate. J Biol Chem 1998; 273: 8545–8548.
- Williams DB. The Merck Frosst Award Lecture 1994. Calnexin: a molecular chaperone with a taste for carbohydrate. Biochem Cell Biol 1995; 73: 123–132.
- Bergeron JJM, Brenner MB, Thomas DY, Williams DB. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends Biochem Sci 1994; 19: 124–128.
- Hebert DN, Simons JF, Peterson JR, Helenius A. Calnexin, calreticulin, and Bip/Kar2p in protein folding. Cold Spring Harbor Symp Quant Biol 1995; 60: 405–415.
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Impact of missense mutations on biosynthesis of myeloperoxidase
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