| Name | myeloperoxidase |
|---|---|
| Synonyms | 38 kDa MYELOPEROXIDASE; MPO; Myeloperoxidase; Myeloperoxidase precursor; Peroxidase (Myeloperoxidase); Myeloperoxidases; Myeloperoxidase precursors; Peroxidase (Myeloperoxidase)s |
| Name | sodium azide |
|---|---|
| CAS | sodium azide |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 17900002 | Okai Y, Sato EF, Higashi-Okai K, Inoue M: Potentiating effect of an endocrine disruptor, paranonylphenol, on the generation of reactive species (ROS) in human venous blood -- association with the activation of signal transduction pathway. J UOEH. 2007 Sep 1;29(3):221-33. An -dependent oxidase inhibitor, diphenyl iodonium (DPI), and a myeloperoxidase inhibitor, sodium azide (NaN3), showed remarkable inhibitory effects on ROS generation induced by NP, but an inhibitor against mitochondrial respiratory function, (KCN), did not exhibit a significant effect. |
0(0,0,0,0) | Details |
| 9258608 | Torreilles J, Guerin MC, Roch P: Peroxidase-release associated with phagocytosis in Mytilus galloprovincialis haemocytes. Dev Comp Immunol. 1997 May-Jun;21(3):267-75. Lucigenine-enhanced chemiluminescence (CLluc) of M. galloprovincialis haemocytes stimulated by zymosan or by phorbol ester (PMA) was measured in the presence and absence of sodium azide, a peroxidase inhibitor. |
0(0,0,0,0) | Details |
| 15865436 | Palazzolo AM, Suquet C, Konkel ME, Hurst JK: Green fluorescent protein-expressing Escherichia coli as a selective probe for HOCl generation within neutrophils. Biochemistry. 2005 May 10;44(18):6910-9. Addition of sodium azide to the medium to inhibit MPO prevented neutrophil-mediated fluorescence quenching. |
0(0,0,0,0) | Details |
| 10369086 | Vento AE, Ramo OJ, Nemlander AT, Ahotupa M, Nissinen E, Holopainen A, Mattila SP: Nitecapone inhibits myeloperoxidase in vitro and enhances functional performance after 8 h of ischemia in experimental heart transplantation. Res Exp Med. 1999 Apr;198(6):299-306. In vitro studies were performed using sodium azide or nitecapone to inhibit myeloperoxidase (MPO) activity of isolated human leukocytes. |
84(1,1,1,4) | Details |
| 9065819 | Panousis C, Kettle AJ, Phillips DR: Neutrophil-mediated activation of mitoxantrone to metabolites which form adducts with DNA. Cancer Lett. 1997 Feb 26;113(1-2):173-8. The use of the myeloperoxidase inhibitor sodium azide confirmed that the activation and covalent binding of mitoxantrone to cellular DNA was due to its metabolism by the haem enzyme myeloperoxidase. |
82(1,1,1,2) | Details |
| 9558962 | Dima VF, Suzuki K, Liu Q, Koie T, Yamada M, Suzuki KJ, Nakaji S, Sugawara K: Laser and serum opsonic activity. Roum Arch Microbiol Immunol. 1996 Oct-Dec;55(4):277-83. We used both lucigenin-dependent CL (LgCL) for (O2-) detection and luminol-dependent CL (LmCL) which detects myeloperoxidase (MPO)-dependent formation of hypochlorous acid in combination with MPO inhibitor, sodium azide (NaN3). |
81(1,1,1,1) | Details |
| 8533604 | Mueller S, Arnhold J: Fast and sensitive chemiluminescence determination of H2O2 concentration in stimulated human neutrophils. J Biolumin Chemilumin. 1995 Jul-Aug;10(4):229-37. Concentrations of H2O2 were diminished by catalase and enhanced by sodium azide owing to inhibition of cellular catalase and myeloperoxidase. |
81(1,1,1,1) | Details |
| 12711275 | Vazzana M, Parrinello D, Cammarata M: Chemiluminescence response of beta-glucan stimulated leukocytes isolated from different tissues and peritoneal cavity of Dicentrarchus labrax. Fish Shellfish Immunol. 2003 May;14(5):423-34. Inhibition experiments by a myeloperoxidase inhibitor sodium azide, iodonium-diphenyl- which inhibits -oxidase, and exogenous superoxide dismutase, which catalyses O-2 dismutation to H (2) O (2), supported the correlation between CL and respiratory burst. |
31(0,1,1,1) | Details |
| 17512464 | Tintinger GR, Theron AJ, Potjo M, Anderson R: Reactive oxidants regulate membrane repolarization and store-operated uptake of by formyl peptide-activated human neutrophils. Free Radic Biol Med. 2007 Jun 15;42(12):1851-7. Epub 2007 Mar 24. In the current study, we have investigated the effects of superoxide dismutase (SOD), catalase, and the myeloperoxidase (MPO) inhibitors, sodium azide and 4-aminobenzoyl hydrazide (ABAH), as well as those of H (2) O (2) and HOCl (both at 100 microM) on the alterations in membrane potential which accompany activation of human neutrophils with the chemoattractant, FMLP (1 microM), and on store-operated uptake of Ca (2+). |
31(0,1,1,1) | Details |
| 8598491 | Hansson M, Asea A, Ersson U, Hermodsson S, Hellstrand K: Induction of apoptosis in NK cells by monocyte-derived reactive metabolites. J Immunol. 1996 Jan 1;156(1):42-7. Sodium azide, a myeloperoxidase inhibitor, substantially reduced the monocyte-induced apoptosis in NK cells. |
31(0,1,1,1) | Details |
| 10400460 | Panasenko OM, Arnhold J: hydroperoxide favours - and myeloperoxidase-induced lipid peroxidation. Free Radic Res. 1999 Jun;30(6):479-87. Lipid peroxidation was also prevented by sodium azide or free medium in the myeloperoxidase- peroxide-Cl- system. |
8(0,0,1,3) | Details |
| 10393704 | Anderson MM, Requena JR, Crowley JR, Thorpe SR, Heinecke JW: The myeloperoxidase system of human phagocytes generates Nepsilon-(carboxymethyl) on proteins: a mechanism for producing advanced glycation end products at sites of inflammation. J Clin Invest. 1999 Jul;104(1):103-13. |
7(0,0,0,7) | Details |
| 11559029 | Suzuki T, Masuda M, Friesen MD, Ohshima H: Formation of spiroiminodihydantoin nucleoside by reaction of 8-oxo-7,8-dihydro- with hypochlorous acid or a myeloperoxidase-H (2) O (2)-Cl (-) system. Chem Res Toxicol. 2001 Sep;14(9):1163-9. Since the presence of 50% D (2) O, 10 mM sodium azide, or 2% did not affect the yield of the products, involvement of singlet and in the formation of dSph from 8-oxodGuo with HOCl was ruled out. |
4(0,0,0,4) | Details |
| 9288889 | Culp SJ, Roberts DW, Talaska G, Lang NP, Fu PP, Lay JO Jr, Teitel CH, Snawder JE, Von Tungeln LS, Kadlubar FF: Immunochemical, 32P-postlabeling, and GC/MS detection of 4-aminobiphenyl-DNA adducts in human peripheral lung in relation to metabolic activation pathways involving pulmonary N-oxidation, conjugation, and peroxidation. Mutat Res. 1997 Aug 1;378(1-2):97-112. The preferred co-oxidant was peroxide and the reaction was strongly inhibited by sodium azide but not by indomethacin or eicosatetraynoic acid, which suggested the primary involvement of myeloperoxidase rather than prostaglandin H synthase or lipoxygenase. This was confirmed by immunoinhibition and immunoprecipitation studies using solubilized human lung microsomes and antisera specific for myeloperoxidase. |
3(0,0,0,3) | Details |
| 10193578 | Gutierrez-Correa J, Stoppani AO: Inactivation of myocardial dihydrolipoamide dehydrogenase by myeloperoxidase systems: effect of halides, and thiol compounds. Free Radic Res. 1999 Feb;30(2):105-17. The effect of the MPO/H2O2/NaNO2 system was prevented by MPO inhibitors (sodium azide, isoniazid, salicylhydroxamic acid) and also by and |
2(0,0,0,2) | Details |
| 11677044 | Arnhold J, Osipov AN, Spalteholz H, Panasenko OM, Schiller J: Effects of hypochlorous acid on unsaturated phosphatidylcholines. Free Radic Biol Med. 2001 Nov 1;31(9):1111-9. Effects of hypochlorous acid and of the myeloperoxidase- peroxide- system on mono- and polyunsaturated phosphatidylcholines were analyzed by means of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). These chlorohydrins were not observed in the absence of peroxide, or myeloperoxidase as well as in the presence of or sodium azide. |
3(0,0,0,3) | Details |
| 12614844 | Panasenko OM, Spalteholz H, Schiller J, Arnhold J: Myeloperoxidase-induced formation of chlorohydrins and lysophospholipids from unsaturated phosphatidylcholines. Free Radic Biol Med. 2003 Mar 1;34(5):553-62. No formation of these products was detected in the absence of one of the components of the MPO-H (2) O (2)-Cl (-) system or in the presence of MPO inhibitors (sodium azide) or scavengers of hypochlorous acid |
3(0,0,0,3) | Details |
| 15056492 | Razumovitch JA, Fuchs D, Semenkova GN, Cherenkevich SN: Influence of on generation of reactive species by myeloperoxidase in human neutrophils. Biochim Biophys Acta. 2004 Apr 7;1672(1):46-50. Comparing several scavengers, formation of reactive species was totally blocked by sodium azide (NaN (3)), both in the presence and in the absence of |
2(0,0,0,2) | Details |
| 8643080 | Li Y, Kuppusamy P, Zweir JL, Trush MA: Role of Cu/Zn-superoxide dismutase in xenobiotic activation. Mol Pharmacol. 1996 Mar;49(3):412-21. Addition of human myeloperoxidase to the HQ/Cu/Zn-SOD synergistically enhanced the formation of BQ from HQ. Similar to the HQ/Cu (II) and H202/Cu (II) systems, the DNA strand breaks mediated by HQ/Cu/Zn-SOD could not be effectively inhibited by the scavengers, including dimethylsulfoxide, and 5,5-dimethyl-1-pyrroline N-oxide, but could be protected by sodium azide. |
2(0,0,0,2) | Details |
| 10569638 | Goldman R, Claycamp GH, Sweetland MA, Sedlov AV, Tyurin VA, Kisin ER, Tyurina YY, Ritov VB, Wenger SL, Grant SG, Kagan VE: Myeloperoxidase-catalyzed redox-cycling of promotes lipid peroxidation and thiol oxidation in HL-60 cells. Free Radic Biol Med. 1999 Nov;27(9-10):1050-63. |
2(0,0,0,2) | Details |
| 11004581 | Jerlich A, Fritz G, Kharrazi H, Hammel M, Tschabuschnig S, Glatter O, Schaur RJ: Comparison of HOCl traps with myeloperoxidase inhibitors in prevention of low density lipoprotein oxidation. Biochim Biophys Acta. 2000 Aug 31;1481(1):109-18. The efficiency of MPO inhibitors to prevent LDL damage increased in the series benzohydroxamic acid < salicylhydroxamic acid < 3-amino-1,2,4-triazole < sodium azide < < hydrazide, while for the HOCl traps the protective efficiency increased in the series < < |
2(0,0,0,2) | Details |
| 19345674 | Tomono S, Miyoshi N, Sato K, Ohba Y, Ohshima H: Formation of ozonolysis products through an ozone-free mechanism mediated by the myeloperoxidase-H2O2- system. Biochem Biophys Res Commun. 2009 May 29;383(2):222-7. Epub 2009 Apr 5. The formation of atheronals by the MPO-H (2) O (2)-Cl (-) system was inhibited by an inhibitor of MPO and scavengers of reactive species such as sodium azide, and vinylbenzoic acid. |
2(0,0,0,2) | Details |
| 14687762 | Abdel-Naim AB, Mohamadin AM: Myeloperoxidase-catalyzed oxidation of chloroacetonitrile to . Toxicol Lett. 2004 Feb 2;146(3):249-57. Addition of the MPO inhibitors; sodium azide (NaN3), 4-amino hydrazine (ABAH) or indomethacin to the reaction mixtures resulted in a significant decrease in the rate of CAN oxidation. |
2(0,0,0,2) | Details |
| 12223088 | Panasenko OM, Osipov AN, Schiller J, Arnhold J: Interaction of exogenous or produced by myeloperoxidase + H2O2 + Cl- system with unsaturated phosphatidylcholines. Biochemistry. 2002 Aug;67(8):889-900. In the absence of the enzyme or either of its substrates (H2O2 or Cl-) or in the presence of the MPO inhibitor (sodium azide) or scavengers or monochlorohydrin formation was not observed. |
2(0,0,0,2) | Details |
| 9718094 | VanUffelen BE, Van der Zee J, de Koster BM, VanSteveninck J, Elferink JG: Sodium azide enhances neutrophil migration and exocytosis: involvement of cyclic GMP and Life Sci. 1998;63(8):645-57. Azide can be oxidized by catalase and myeloperoxidase in the presence of H2O2, resulting in the generation of (NO). |
2(0,0,0,2) | Details |
| 8055842 | Ishizaki T, Yano E, Urano N, Evans PH: Crocidolite-induced reactive metabolites generation from human polymorphonuclear leukocytes. Environ Res. 1994 Aug;66(2):208-16. Sodium azide, an inhibitor of myeloperoxidase (MPO) to produce OCl-, also inhibited CL production. Sodium azide, an inhibitor of myeloperoxidase (MPO) to produce OCl-, also inhibited CL production. |
1(0,0,0,1) | Details |
| 8747893 | Salman-Tabcheh S, Guerin MC, Torreilles J: Potential role of the peroxidase-dependent metabolism of in lowering the polymorphonuclear leukocyte bactericidal function. Free Radic Res. 1996 Jan;24(1):61-8. The addition of catalase or sodium azide substantially reduced this binding. The present results suggest that metabolism is mediated by H2O2 and myeloperoxidase (MPO) released by activated PMNs. |
1(0,0,0,1) | Details |
| 9502580 | Hasegawa H, Suzuki K, Nakaji S, Sugawara K: Analysis and assessment of the capacity of neutrophils to produce reactive species in a 96-well microplate format using lucigenin- and luminol-dependent chemiluminescence. J Immunol Methods. 1997 Dec 15;210(1):1-10. Furthermore, we studied the contribution of various ROS to LgCL and luminol-dependent CL (LmCL) using modulators of ROS metabolism including superoxide dismutase (SOD), catalase, deferoxamine and sodium azide (NaN3). Thus, it was demonstrated that LgCL detects the with high selectivity whereas the LmCL assay measures myeloperoxidase (MPO)-mediated formation of hypochlorous acid. |
1(0,0,0,1) | Details |
| 16732739 | Panasenko OM, Spalteholz H, Schiller J, Arnhold J: Leukocytic myeloperoxidase-mediated formation of bromohydrins and lysophospholipids from unsaturated phosphatidylcholines. Biochemistry. 2006 May;71(5):571-80. The formation of lysophospholipids as well as of bromohydrins was not observed when the enzyme or one of its substrates (H2O2 or Br-) was absent from the incubation medium, or if an inhibitor of MPO (sodium azide) or hypobromite scavengers or were added. |
1(0,0,0,1) | Details |
| 7861697 | Li JZ, Sharma R, Dileepan KN, Savin VJ: Polymorphonuclear leukocytes increase glomerular albumin permeability via hypohalous acid. Kidney Int. 1994 Oct;46(4):1025-30. This increase in Palbumin was inhibited by superoxide dismutase, catalase, or (Palbumin = 0.035 +/- 0.06, -0.39 +/- 0.10, 0.028 +/- 0.06, respectively) and ameliorated by sodium azide (Palbumin = 0.21 +/- 0.03). To determine the role of specific ROS in PMN mediated glomerular injury, isolated rat glomeruli were incubated for 30 minutes at 37 degrees C with H2O2, with H2O2 and myeloperoxidase, or with activated PMNs. |
1(0,0,0,1) | Details |
| 8409752 | Albrecht D, Jungi TW: Luminol-enhanced chemiluminescence induced in peripheral blood-derived human phagocytes: obligatory requirement of myeloperoxidase exocytosis by monocytes. J Leukoc Biol. 1993 Oct;54(4):300-6. |
1(0,0,0,1) | Details |
| 17346675 | Herraiz T, Guillen H, Galisteo J: N-methyltetrahydro-beta-carboline analogs of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) neurotoxin are oxidized to beta-carbolinium cations by heme peroxidases. Biochem Biophys Res Commun. 2007 Apr 27;356(1):118-23. Epub 2007 Feb 26. However, 2-Me-THbetaC and 2,9-diMe-THbetaC were efficiently oxidized by horseradish peroxidase (HRP), lactoperoxidase (LPO), and myeloperoxidase (MPO) to 2-methyl-3,4-dihydro-beta-carbolinium cations (2-Me-DHbetaC (+), 2,9-diMe-DHbetaC (+)) as the main products, and detectable amount of 2-methyl-beta-carbolinium cations (2-Me-betaC (+), 2,9-diMe-betaC (+)). Peroxidase inhibitors sodium azide, and highly reduced or abolished this oxidation. |
1(0,0,0,1) | Details |
| 12713825 | Suzuki T, Friesen MD, Ohshima H: Formation of a diimino- nucleoside from by singlet generated by methylene blue photooxidation. Bioorg Med Chem. 2003 May 15;11(10):2157-62. Its identification is based on identical chromatographic and spectroscopic data with an authentic compound, which we recently isolated and characterised from the reaction mixture of with reagent HOCl and a myeloperoxidase-H (2) O (2)-Cl (-) system. |
1(0,0,0,1) | Details |
| 17089362 | Alexandrova ML, Bochev PG, Markova VI: Inhibitory and enhancing effects of piroxicam on whole blood chemiluminescence. Luminescence. 2007 Mar-Apr;22(2):97-104. Piroxicam inhibited the first phase of extracellular LCL in a dose-dependent manner (p = 0.0001) and revealed itself as an enhancing agent of CL in later time intervals after the start of respiratory burst, in a model system containing horseradish peroxidase (HRP) and sodium azide. Piroxicam inhibited the total fMLP-stimulated LCL by 70% approximately and, only by about 30%, the first phase of fMLP-stimulated extracellular LCL, which presupposes an effect on myeloperoxidase-catalysed formation of hypochloric acid. |
1(0,0,0,1) | Details |
| 15064160 | Okai Y, Sato EF, Higashi-Okai K, Inoue M: Enhancing effect of the endocrine disruptor para-nonylphenol on the generation of reactive species in human blood neutrophils. Environ Health Perspect. 2004 Apr;112(5):553-6. -dependent oxidase inhibitor, diphenyl iodonium and the myeloperoxidase inhibitor sodium azide (NaN3) showed remarkable inhibitory effects on ROS generation induced by NP, but an inhibitor against mitochondrial respiratory function, (KCN), did not exhibit significant effect. |
0(0,0,0,0) | Details |
| 10660661 | Yamada M, Suzuki K, Kudo S, Totsuka M, Simoyama T, Nakaji S, Sugawara K: Effect of exhaustive exercise on human neutrophils in athletes. Luminescence. 2000 Jan-Feb;15(1):15-20. Just after exercise, the LgCL response was not affected, while the response of LmCL mixed with sodium azide, which inhibits catalase and myeloperoxidase (MPO) activity, was significantly enhanced (p < 0.05). |
0(0,0,0,0) | Details |
| 7753758 | Takeyama Y, Ogino K, Segawa H, Kobayashi H, Uda T, Houbara T: Effects of zinc on production of active species by rat neutrophils. . Pharmacol Toxicol. 1995 Jan;76(1):50-5. Homogenized neutrophils showed a bimodal pattern on induction by zinc, the second peak of which was inhibited slightly by catalase and completely by sodium azide, but was not inhibited by superoxide dismutase. |
0(0,0,0,0) | Details |
| 8929553 | Bednar MM, Balazy M, Murphy M, Booth C, Fuller SP, Barton A, Bingham J, Golding L, Gross CE: augments fMLP-stimulated chemiluminescence by neutrophils in human whole blood. J Leukoc Biol. 1996 Nov;60(5):619-24. Both sodium azide and significantly inhibited LDCL (93% inhibition with 100 microM azide, 52% inhibition with 10 mM |
0(0,0,0,0) | Details |
| 8397140 | Rathakrishnan C, Tiku ML: Lucigenin-dependent chemiluminescence in articular chondrocytes. . Free Radic Biol Med. 1993 Aug;15(2):143-9. Catalase and the metabolic inhibitor, sodium azide, which inhibits the enzyme myeloperoxidase, had no inhibitory effect on lucigenin-dependent chemiluminescence production. |
0(0,0,0,0) | Details |
| 9918136 | Williams JA, Stone EM, Millar BC, Gusterson BA, Grover PL, Phillips DH: Determination of the enzymes responsible for activation of the heterocyclic amine 2-amino-3-methylimidazo [4,5-f] quinoline in the human breast. Pharmacogenetics. 1998 Dec;8(6):519-28. Adduct formation in stimulated neutrophils was inhibited 80% by the myeloperoxidase inhibitor sodium azide (1 mM) but was not affected by proadifen (100 microM), indomethacin (100 microM), or eicosatetraynoic acid (100 microM), inhibitors of cytochrome P450, prostaglandin synthetase, and lipoxygenase, respectively. |
0(0,0,0,0) | Details |