Myeloperoxidase human

Allegra, M. et al.. Mechanism of interaction of betanin and indicaxanthin with human myeloperoxidase and hypochlorons acid, Biochem. Biophys. Res. Commun., 332, 837, 2005. 

The effect of gold compounds on human neutrophil myeloperoxidase, in Bioinorganic Chemistry of Gold Coordination Compounds (eds B.M. Sutton and R.G. Franz), SK F, Philadelphia, pp. 58-66. 

Cramer, E.M., Beesley, J.E., Pulford, K.A.F., Breton-Gorius, J., and Mason, D.Y. (1989) Colocalization of elastase and myeloperoxidase in human blood and bone marrow neutrophils using a monoclonal antibody and immunogold. Am. J. Pathol. 134, 1275-1284. 

Furthermore, it was found that stimulated human neutrophils are able to produce 5-chloro-2 -deoxycytidine and that the myeloperoxidase system generates just the same levels of 5-chlorocytosine in DNA and RNA in vitro (Reaction (4), Figure 28.3). It is possible that myeloperoxidase-generated chlorinated products may modify nuclear acids of pathogens and nuclear acids in host cells during inflammation. Hawkins et al. [48] suggested that DNA oxidation may be initiated by protein chloramines formed in the reaction of HOCl with histones in the nucleosome. 

The classic oxidizing systems of human myeloperoxidase and horseradish peroxidase were exploited for their well-known abilities to oxidize phenolic substrates. Under conditions of incubations, the following oxidation pathway was defined (155). Peroxidases are first converted to the oxidized... 

Histochemical studies of bone marrow samples show that peroxidase-containing granules are detectable in promyelocytes. The human promyelo-cytic leukaemia cell line HL-60 grows easily in culture, and the cells resemble promyelocytes both structurally and functionally. Furthermore, they can be induced to differentiate in vitro upon addition of various agents, such as retinoic acid and phorbol esters, and these differentiated cells resemble more mature forms of neutrophils. HL-60 cells possess almost the same amount of myeloperoxidase (4.4 fig per 106 cells) as mature neutrophils, and the enzyme purified from these cells has the same subunit structure. The cells thus actively synthesise the enzyme only until they are induced to differentiate. This cell line has been extensively used to study the molecular events controlling the expression of enzymes such as myeloperoxidase, and also to investigate the molecular controls that lead to a cessation of their expression. 

Morishita, K., Kubota, N., Asano, S., Kaziro, Y., Nagata, S. (1987). Molecular cloning and characterization of cDNA for human myeloperoxidase. J. Biol. Chem. 262, 3844-51. 

Nauseef, W. M. (1986). Myeloperoxidase biosynthesis by a human promyelocytic leukemia cell line Insight into myeloperoxidase deficiency. Blood 67,865-72. 

Nauseef, W. M. (1987). Posttranslational processing of a human myeloid lysosomal protein, myeloperoxidase. Blood 70,1143-50. 

Swanson, M. S. (1987). cDNA cloning of human myeloperoxidase Decrease in myeloperoxidase mRNA upon induction of HL-60 cells. Proc. Natl. Acad. Sci. USA 84,2057-61. 

C5a is inactivated by the myeloperoxidase-H202 system, which oxidises a methionine residue (Met 70) on the molecule group A streptococcal endo-proteinases also abolish chemotactic activity of C5a and related compounds. Neutrophil lysosomal enzymes (e.g. elastase and cathepsin G) also destroy C5a chemotactic activity, but as these proteases are inhibited by the serum antiproteinases, a -antiproteinase and a2-macroglobulin, the physiological role of neutrophilic proteases in the inactivation of C5a is questionable. Two chemotactic factor inactivators have been found in human serum an a-globulin that specifically and irreversibly inactivates C5-derived chemotactic factors, and a / -globulin that inactivates bacterial chemotactic factors. These activities are heat labile (destroyed by treatment at 56 °C for 30 min) and are distinct from those attributable to anaphylatoxin inactivator. An apparently specific inhibitor of C5-derived chemotactic activity has also been described in human synovial fluid and peritoneal fluid. This factor (molecular mass of 40 kDa) is heat stable and acts directly on C5a. 

Winterboum, C. C., Garcia, R. C., Segal, A. W. (1985). Production of the superoxide adduct of myeloperoxidase (compound HI) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride. Biochem. J. 228, 583-92. 

Eastmond DA, Smith MT, Ruzo LO, et al. 1986. Metabolic activation of phenol by human myeloperoxidase and horseradish peroxidase. Mol Pharmacol 30 674-679. 

Subrahmanyam VV, Kolachana P, Smith MT. 1990b. Effect of phenol and catechol on the kinetics of human myeloperoxidase-dependent hydroquinone metabolism. Adv Exp Med Biol 283 377-381. 

Subrahmanyam VV, Kolachana P, Smith MT. 1991. Hydroxylation of phenol to hydroquinone catalyzed by a human myeloperoxidase-superoxide complex Possible implications in benzene-induced myelotoxicity. Free Radic Res Comms 15 285-296. 

Myeloperoxidase [17-19] Human leukocytes H2O2 + Cl- + H3O+ HCIO + 2H2O Antimicrobial... 

D Alessandro T, Prasain J, Benton MR et al. Polyphenols, inflammatory response, and cancer prevention chlorination of isoflavones by human neutrophils. J. Nutr. 133, 3773S-3777S, 2003. Boersma BJ, D Alessandro T, Benton MR et al. Neutrophil myeloperoxidase chlorinates and nitrates soy isoflavones and enhances their antioxidant properties. Free Radical Biol. Med. 35, 1417-1430, 2003. 

Furthermore, it was found that stimulated human neutrophils are able to produce 5-chloro-2 -deoxycytidine and that the myeloperoxidase system generates just the same levels of... 

Incubation of butadiene with human myeloperoxidase (from polymorphonuclear leukocytes) in the presence of hydrogen peroxide (1 mmol/L) yielded epoxybutene and small amounts of crotonaldehyde by direct oxygen transfer (Duescher Elfarra, 1992 Maniglier-Poulet et al., 1995). Addition of chloride in the hundred millimolar range led to the formation of l-chloro-2-hvdroxy-3-butene as the major metabolite (Duescher Elfarra, 1992). 

Duescher, R.J. Elfarra, A.A. (1992) 1,3-Butadiene oxidation by human myeloperoxidase. Role of chloride ion catalysis of divergent pathways. J. biol. Chem.. 267, 19859-19865... 

On the other hand, hydroquinone (3 pmol/L) prevented the staurosporine-induced apoptosis of HL-60 and the IL-3-dependent murine myeloblastic (32D) cell line it also prevented apoptosis of the 32D cells observed in the absence of IL-3. The myeloperoxidase inhibitor indomethacin opposed the effect of hydroquinone on staurosporine-induced apoptosis of HL-60 cells (Hazel et al., 1995, 1996b). Pretreatment of human leukaemia cells ML-1 with buthionine sulfoximine (100 pmol/L for 24 h), in order to decrease their glutathione content, increased the susceptibility of these cells to hydroquinone-induced inhibition of differentiation caused by phorbol acetate pretreatment with l,2-dithiole-3-thione, which induces reduced glutathione synthesis, prevented the differentiation inhibition of hydroquinone. Treatment of DBA/2 mice with 1,2-dithiole-3-thione, which increased the activity of quinone reductase of bone-marrow stromal cells by 50%, decreased the susceptibility of these cells towards hydroquinone (Trush et al., 1996). 

Subrahmanyam, V.V., Kolachana, P. Smith, M.T. (1991) Metabolism of hydroquinone by human myeloperoxidase mechamsms of stimulation by other phenolic compounds. Arch. Biochem. Biophys., 286, 76-84... 

Human neutrophils use HOC1 formed by myeloperoxidase to oxidize a-amino acids such as tyrosine to reactive aldehydes that form adducts with -SH, -NH2, imidazole, and other nucleophilic groups.560 They also contain NO synthases, which form NO, peroxynitrite (Fig. 18-24), and nitrite.561562... 

As discussed in the earlier survey (1), a biogenic source of polychlorinated dibenzo-p-dioxins and dibenzofurans is peroxidase-catalyzed transformation of chlorophenols as first reported by Oberg and Rappe (2041-2044). More recent studies confirm these observations (2045-2048). In addition to lactoperoxidase and horseradish peroxidase, human leukocyte myeloperoxidase catalyzes in vitro formation of dioxins and dibenzofurans from chlorophenols (2046, 2047). Formation rates are in the pmol/mol range (Scheme 3.6) demonstrating that a human biosynthesis of dioxins and furans is not only possible but also likely. These observations are reinforced by the reported in vivo (rats) conversion of the pre-dioxin nona-chloro-2-phenoxyphenol to octachlorodibenzo-p-dioxin (OCDD) (2049), and the production of hepta- and octachlorodibenzo-p-dioxin in the feces of cows fed pentachlorophenol-treated wood (Scheme 3.7) (2050, 2051). 

Henderson JP, Heinecke JW (2003) Myeloperoxidase and Eosinophil Peroxidase Phagocyte Enzymes for Halogenation in Humans. In Gribble GW (ed) Natural Production of Organohalogen Compounds, The Handbook of Environmental Chemistry, vol 3, part P. Springer, Berlin, p 201... 

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