| Name | myeloperoxidase |
|---|---|
| Synonyms | 38 kDa MYELOPEROXIDASE; MPO; Myeloperoxidase; Myeloperoxidase precursor; Peroxidase (Myeloperoxidase); Myeloperoxidases; Myeloperoxidase precursors; Peroxidase (Myeloperoxidase)s |
| Name | amitrole |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 9721600 | Rastogi L, Patnaik GK, Dikshit M: Free radicals and antioxidant status following pylorus ligation induced gastric mucosal injury in rats. Pharmacol Res. 1998 Aug;38(2):125-32. MDA level, myeloperoxidase (a neutrophil maker) and catalase activity in the rat stomach homogenate were augmented 2, 4 and 19 h after pylorus ligation. |
1(0,0,0,1) | Details |
| 6833495 | Burger AG, Engler D, Buergi U, Weissel M, Steiger G, Ingbar SH, Rosin RE, Babior BM: Ether link cleavage is the major pathway of iodothyronine metabolism in the phagocytosing human leukocyte and also occurs in vivo in the rat. J Clin Invest. 1983 Apr;71(4):935-49. FROM THESE FINDINGS WE CONCLUDE THE FOLLOWING: (a) ELC is the major pathway for the degradation of T (4) during leukocyte phagocytosis, and accounts for 50% of the disposal of this iodothyronine; (b) the NEI and iodide formed by phagocytosing cells are derived from the degradation of the phenolic and tyrosyl rings of T (4), although ELC per se accounts for only a small fraction of these iodinated products; (c) the process by which ELC occurs is enzymic in nature, and its occurrence requires the presence of the respiratory burst that accompanies phagocytosis; (d) the enzyme responsible for ELC is likely to be a peroxidase, although a clear role for myeloperoxidase as the candidate enzyme remains to be established; (e) iodothyronines are also degraded by ELC in vivo, and the quantitative importance of this pathway in various pathophysiological states requires further investigation. |
1(0,0,0,1) | Details |
| 6301583 | Lane TA, Lamkin GE: Myeloperoxidase-mediated modulation of chemotactic peptide binding to human neutrophils. Blood. 1983 Jun;61(6):1203-7. |
5(0,0,0,5) | Details |
| 3015901 | Thomas EL, Fishman M: Oxidation of and by isolated leukocytes. . J Biol Chem. 1986 Jul 25;261(21):9694-702. Stimulated neutrophils produced H2O2 and secreted myeloperoxidase. |
4(0,0,0,4) | Details |
| 3010869 | Miyasaki KT, Wilson ME, Cohen E, Jones PC, Genco RJ: Evidence for and partial characterization of three major and three minor chromatographic forms of human neutrophil myeloperoxidase. Arch Biochem Biophys. 1986 May 1;246(2):751-64. |
2(0,0,0,2) | Details |
| 6325545 | Cramer R, Soranzo MR, Dri P, Menegazzi R, Pitotti A, Zabucchi G, Patriarca P: A simple reliable assay for myeloperoxidase activity in mixed neutrophil-eosinophil cell suspensions: application to detection of myeloperoxidase deficiency. J Immunol Methods. 1984 May 11;70(1):119-25. |
2(0,0,0,2) | Details |
| 3009503 | Frenkel K, Blum F, Troll W: ions and peroxide form from NaCl thereby mimicking myeloperoxidase. J Cell Biochem. 1986;30(3):181-93. |
2(0,0,0,2) | Details |
| 2154520 | Bozeman PM, Learn DB, Thomas EL: Assay of the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. J Immunol Methods. 1990 Jan 24;126(1):125-33. |
2(0,0,0,2) | Details |
| 3008887 | Dallegri F, Patrone F, Ballestrero A, Frumento G, Sacchetti C: Inhibition of neutrophil cytolysin production by target cells. Blood. 1986 May;67(5):1265-72. The lysis was inhibited by azide, catalase, -free medium and amino acids, suggesting the requirement for myeloperoxidase (MPO), peroxide (H2O2), ions (Cl-), and hypochlorous acid (HOC1), respectively. |
1(0,0,0,1) | Details |
| 6282623 | Pember SO, Fuhrer-Krusi SM, Barnes KC, Kinkade JM Jr: Isolation of three native forms of myeloperoxidase from human polymorphonuclear leukocytes. FEBS Lett. 1982 Apr 5;140(1):103-8. |
1(0,0,0,1) | Details |
| 232823 | Cramer R, Bisiacchi B, de Nicola G, Patriarca P: A comparative study of the biochemical properties of myeloperoxidase and eosinophil peroxidase. Adv Exp Med Biol. 1979;121(A):91-9. |
1(0,0,0,1) | Details |
| 2176263 | Duval DL, Howard D, McCalden TA, Billings RE: The determination of myeloperoxidase activity in liver. . Life Sci. 1990;47(24):PL145-50. |
1(0,0,0,1) | Details |
| 12421972 | Clark SR, Coffey MJ, Maclean RM, Collins PW, Lewis MJ, Cross AR, O'Donnell VB: Characterization of consumption pathways by normal, chronic granulomatous disease and myeloperoxidase-deficient human neutrophils. J Immunol. 2002 Nov 15;169(10):5889-96. |
1(0,0,0,1) | Details |
| 2824562 | Winterbourn CC, Stern A: Human red cells scavenge extracellular peroxide and inhibit formation of hypochlorous acid and J Clin Invest. 1987 Nov;80(5):1486-91. Red cells efficiently inhibited oxidation by generated from H2O2, O2- and Fe (EDTA), and myeloperoxidase-dependent oxidation of to by stimulated neutrophils. |
1(0,0,0,1) | Details |
| 6094369 | Muller-Peddinghaus R: In vitro determination of phagocyte activity by luminol- and lucigenin-amplified chemiluminescence. Int J Immunopharmacol. 1984;6(5):455-66. The dependence of luminol-amplified CL upon the generation of the chain reaction intermediate H2O2 and its three main catalysts catalase, myeloperoxidase and makes this reaction prone to different artifacts if cell activity is to be determined. |
1(0,0,0,1) | Details |
| 6428753 | Cardoni RL, Rimoldi MT, de Bracco MM: Antibody-dependent cytotoxicity of human and mouse mononuclear cells against Trypanosoma cruzi epimastigotes. Cell Immunol. 1984 Jul;86(2):518-24. When human mononuclear cells were incubated with amobarbital, azide, or aminotriazole, an inhibition of cytotoxicity against sensitized T. cruzi was observed, suggesting that reduction products and myeloperoxidase were involved in the destruction of sensitized T. cruzi epimastigotes by normal human mononuclear cells. |
1(0,0,0,1) | Details |
| 20032404 | Bechtel W, Bauer G: Modulation of intercellular ROS signaling of human tumor cells. . Anticancer Res. 2009 Nov;29(11):4559-70. These supraoptimal conditions can be brought back to the optimum through excess myeloperoxidase (MPO), partial removal of peroxide through the catalase mimetic EUK-134 or partial inhibition of oxidase. |
1(0,0,0,1) | Details |