PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10359564-3 1999 We now report that reactive nitrogen species generated by the MPO-H2O2-NO2- system of monocytes convert LDL into a form (NO2-LDL) that is avidly taken up and degraded by macrophages, leading to massive cholesterol deposition and foam cell formation, essential steps in lesion development. Nitrogen Dioxide 71-74 myeloperoxidase Homo sapiens 62-65 10894808-3 2000 Myeloperoxidase generates a number of reactive species, including hypochlorous acid, chloramines, tyrosyl radicals, and nitrogen dioxide. Nitrogen Dioxide 120-136 myeloperoxidase Homo sapiens 0-15 10437781-3 1999 We found that myeloperoxidase, an H2O2-generating system and nitrite (NO2-) peroxidized LDL lipids. Nitrogen Dioxide 70-73 myeloperoxidase Homo sapiens 14-29 11054430-2 2001 Recent studies have shown that myeloperoxidase (MPO), an abundant heme protein released by activated leukocytes, can oxidize nitrite (NO(2-)) to a radical species, most likely nitrogen dioxide. Nitrogen Dioxide 176-192 myeloperoxidase Homo sapiens 31-46 11054430-2 2001 Recent studies have shown that myeloperoxidase (MPO), an abundant heme protein released by activated leukocytes, can oxidize nitrite (NO(2-)) to a radical species, most likely nitrogen dioxide. Nitrogen Dioxide 176-192 myeloperoxidase Homo sapiens 48-51 10359564-3 1999 We now report that reactive nitrogen species generated by the MPO-H2O2-NO2- system of monocytes convert LDL into a form (NO2-LDL) that is avidly taken up and degraded by macrophages, leading to massive cholesterol deposition and foam cell formation, essential steps in lesion development. Nitrogen Dioxide 121-124 myeloperoxidase Homo sapiens 62-65 9686606-3 1998 We describe the effects of the interaction of NO and its decay product, NO2, with H2O2 and MPO on IC cross-linking. Nitrogen Dioxide 72-75 myeloperoxidase Homo sapiens 91-94 10029554-7 1999 However, it was independent of chloride ion and little affected by scavengers of hypochlorous acid, suggesting that the reactive agent is a nitrogen dioxide-like species that results from the one-electron oxidation of NO2- by myeloperoxidase. Nitrogen Dioxide 140-156 myeloperoxidase Homo sapiens 226-241 10029554-7 1999 However, it was independent of chloride ion and little affected by scavengers of hypochlorous acid, suggesting that the reactive agent is a nitrogen dioxide-like species that results from the one-electron oxidation of NO2- by myeloperoxidase. Nitrogen Dioxide 218-221 myeloperoxidase Homo sapiens 226-241 10029554-10 1999 The reaction required NO2- and was inhibited by catalase and heme poisons, implicating myeloperoxidase in the cell-mediated pathway. Nitrogen Dioxide 22-25 myeloperoxidase Homo sapiens 87-102 10029554-11 1999 These results indicate that human neutrophils use the myeloperoxidase-H2O2-NO2- system to generate reactive species that can nitrate the C-8 position of 2"-deoxyguanosine. Nitrogen Dioxide 75-78 myeloperoxidase Homo sapiens 54-69 9686606-9 1998 These results indicated that the product of interaction of H2O2 and NO2 mediated by MPO may be responsible for the increase in cross-linking. Nitrogen Dioxide 68-71 myeloperoxidase Homo sapiens 84-87 9450756-4 1998 We have recently demonstrated that nitrite (NO2-), a major end-product of .NO metabolism, readily promotes tyrosine nitration through formation of nitryl chloride (NO2Cl) and nitrogen dioxide (.NO2) by reaction with the inflammatory mediators hypochlorous acid (HOCl) or myeloperoxidase. Nitrogen Dioxide 44-47 myeloperoxidase Homo sapiens 271-286 9450756-4 1998 We have recently demonstrated that nitrite (NO2-), a major end-product of .NO metabolism, readily promotes tyrosine nitration through formation of nitryl chloride (NO2Cl) and nitrogen dioxide (.NO2) by reaction with the inflammatory mediators hypochlorous acid (HOCl) or myeloperoxidase. Nitrogen Dioxide 175-191 myeloperoxidase Homo sapiens 271-286 9450756-4 1998 We have recently demonstrated that nitrite (NO2-), a major end-product of .NO metabolism, readily promotes tyrosine nitration through formation of nitryl chloride (NO2Cl) and nitrogen dioxide (.NO2) by reaction with the inflammatory mediators hypochlorous acid (HOCl) or myeloperoxidase. Nitrogen Dioxide 164-167 myeloperoxidase Homo sapiens 271-286 9450756-5 1998 We now show that activated human polymorphonuclear neutrophils convert NO2- into NO2Cl and .NO2 through myeloperoxidase-dependent pathways. Nitrogen Dioxide 71-74 myeloperoxidase Homo sapiens 104-119 9450756-5 1998 We now show that activated human polymorphonuclear neutrophils convert NO2- into NO2Cl and .NO2 through myeloperoxidase-dependent pathways. Nitrogen Dioxide 81-84 myeloperoxidase Homo sapiens 104-119 27020551-3 2016 Since NO2(-) and MPO (and/or HOCl) were important mediators in brain function and disease, we investigated the effects of NO2(-) on MPO-mediated damage to human neuroblastoma SH-SY5Y cells. Nitrogen Dioxide 122-125 myeloperoxidase Homo sapiens 132-135 9065416-5 1997 Phenolic nitration by MPO-catalyzed NO2- oxidation is only partially inhibited by chloride (Cl-), the presumed major physiological substrate for MPO. Nitrogen Dioxide 36-39 myeloperoxidase Homo sapiens 22-25 9065416-5 1997 Phenolic nitration by MPO-catalyzed NO2- oxidation is only partially inhibited by chloride (Cl-), the presumed major physiological substrate for MPO. Nitrogen Dioxide 36-39 myeloperoxidase Homo sapiens 145-148 9065416-6 1997 In fact, low concentrations of NO2- (2-10 microM) catalyze MPO-mediated oxidation of Cl-, indicated by increased chlorination of monochlorodimedon or 4-hydroxyphenylacetic acid, most likely via reduction of MPO compound II. Nitrogen Dioxide 31-34 myeloperoxidase Homo sapiens 59-62 9065416-6 1997 In fact, low concentrations of NO2- (2-10 microM) catalyze MPO-mediated oxidation of Cl-, indicated by increased chlorination of monochlorodimedon or 4-hydroxyphenylacetic acid, most likely via reduction of MPO compound II. Nitrogen Dioxide 31-34 myeloperoxidase Homo sapiens 207-210 9065416-8 1997 Collectively, our results suggest that NO2-, at physiological or pathological levels, is a substrate for the mammalian peroxidases MPO and lactoperoxidase and that formation of NO2. Nitrogen Dioxide 39-42 myeloperoxidase Homo sapiens 131-134 7499684-6 1995 Allergen challenge after exposure to both air and NO2 significantly (p < 0.05) increased levels of MCT, but not MPO and IL-8 in the nasal lavage fluid. Nitrogen Dioxide 50-53 myeloperoxidase Homo sapiens 115-118 34085520-3 2021 At this site, MPO mediates endothelial dysfunction by catalytically consuming nitric oxide (NO) and producing reactive oxidants, hypochlorous acid (HOCl) and the nitrogen dioxide radical ( NO2). Nitrogen Dioxide 189-192 myeloperoxidase Homo sapiens 14-17 34085520-8 2021 Nitroxides also differentially inhibited protein nitration catalyzed by both purified and endothelial-localized MPO, which was dependent on NO2 scavenging rather than MPO inhibition. Nitrogen Dioxide 141-144 myeloperoxidase Homo sapiens 112-115 27020551-4 2016 Here, we showed that exposure of SH-SY5Y cells to MPO (or HOCl) resulted in a significant loss in viability, ATP and glutathione levels, and treatment of neuronal cells with NO2(-) substantially attenuated MPO (or HOCl)-dependent cellular toxicity. Nitrogen Dioxide 174-177 myeloperoxidase Homo sapiens 50-53 27020551-4 2016 Here, we showed that exposure of SH-SY5Y cells to MPO (or HOCl) resulted in a significant loss in viability, ATP and glutathione levels, and treatment of neuronal cells with NO2(-) substantially attenuated MPO (or HOCl)-dependent cellular toxicity. Nitrogen Dioxide 174-177 myeloperoxidase Homo sapiens 206-209 27020551-5 2016 The protective effects of NO2(-) on MPO (or HOCl)-induced cytotoxicity were because that (1) NO2(-) at high concentrations competed effectively with Cl(-) for MPO, thus limiting OCl(-) production by the enzyme; (2) HOCl was removed by reacting with NO2(-), forming less damaging compound; (3) NO2(-) significantly inhibited MPO-mediated inactivation of brain protein (enolase) and protein oxidation. Nitrogen Dioxide 26-29 myeloperoxidase Homo sapiens 36-39 27020551-5 2016 The protective effects of NO2(-) on MPO (or HOCl)-induced cytotoxicity were because that (1) NO2(-) at high concentrations competed effectively with Cl(-) for MPO, thus limiting OCl(-) production by the enzyme; (2) HOCl was removed by reacting with NO2(-), forming less damaging compound; (3) NO2(-) significantly inhibited MPO-mediated inactivation of brain protein (enolase) and protein oxidation. Nitrogen Dioxide 26-29 myeloperoxidase Homo sapiens 159-162 27020551-5 2016 The protective effects of NO2(-) on MPO (or HOCl)-induced cytotoxicity were because that (1) NO2(-) at high concentrations competed effectively with Cl(-) for MPO, thus limiting OCl(-) production by the enzyme; (2) HOCl was removed by reacting with NO2(-), forming less damaging compound; (3) NO2(-) significantly inhibited MPO-mediated inactivation of brain protein (enolase) and protein oxidation. Nitrogen Dioxide 26-29 myeloperoxidase Homo sapiens 159-162 27020551-5 2016 The protective effects of NO2(-) on MPO (or HOCl)-induced cytotoxicity were because that (1) NO2(-) at high concentrations competed effectively with Cl(-) for MPO, thus limiting OCl(-) production by the enzyme; (2) HOCl was removed by reacting with NO2(-), forming less damaging compound; (3) NO2(-) significantly inhibited MPO-mediated inactivation of brain protein (enolase) and protein oxidation. Nitrogen Dioxide 93-96 myeloperoxidase Homo sapiens 36-39 27020551-5 2016 The protective effects of NO2(-) on MPO (or HOCl)-induced cytotoxicity were because that (1) NO2(-) at high concentrations competed effectively with Cl(-) for MPO, thus limiting OCl(-) production by the enzyme; (2) HOCl was removed by reacting with NO2(-), forming less damaging compound; (3) NO2(-) significantly inhibited MPO-mediated inactivation of brain protein (enolase) and protein oxidation. Nitrogen Dioxide 93-96 myeloperoxidase Homo sapiens 36-39 27020551-5 2016 The protective effects of NO2(-) on MPO (or HOCl)-induced cytotoxicity were because that (1) NO2(-) at high concentrations competed effectively with Cl(-) for MPO, thus limiting OCl(-) production by the enzyme; (2) HOCl was removed by reacting with NO2(-), forming less damaging compound; (3) NO2(-) significantly inhibited MPO-mediated inactivation of brain protein (enolase) and protein oxidation. Nitrogen Dioxide 93-96 myeloperoxidase Homo sapiens 36-39 27020551-6 2016 Therefore, NO2(-) could show novel protective effects in some neurodegenerative diseases by preventing MPO-mediated oxidative damage. Nitrogen Dioxide 11-14 myeloperoxidase Homo sapiens 103-106 9407050-4 1997 Myeloperoxidase (MPO) also catalyzed nitration and chlorination of fluorescein and the fluorescein-conjugated particles in cell-free solutions; the relative nitration yields increased with increasing [NO2-]/[Cl-] ratios. Nitrogen Dioxide 201-205 myeloperoxidase Homo sapiens 0-15 9407050-4 1997 Myeloperoxidase (MPO) also catalyzed nitration and chlorination of fluorescein and the fluorescein-conjugated particles in cell-free solutions; the relative nitration yields increased with increasing [NO2-]/[Cl-] ratios. Nitrogen Dioxide 201-205 myeloperoxidase Homo sapiens 17-20 9407050-7 1997 These data indicate that intraphagosomal aromatic nitration in neutrophils is negligible, although extracellular nitration of phenolic compounds by secreted MPO could occur at physiological concentration levels of NO2-. Nitrogen Dioxide 214-217 myeloperoxidase Homo sapiens 157-160 16647868-7 2006 We also show that NO2* radicals, generated by a myeloperoxidase/H2O2/nitrite system, also degrade DMPO/HO*. Nitrogen Dioxide 18-22 myeloperoxidase Homo sapiens 48-63 26854590-8 2016 Moreover, the reduced effect of NO2(-) on OCl(-) production was attributed to that NO2(-) reduced H2O2 production in activated neutrophils without influencing the release of myeloperoxidase (MPO), thus limiting OCl(-) production by MPO/H2O2 system. Nitrogen Dioxide 32-35 myeloperoxidase Homo sapiens 191-194 26854590-8 2016 Moreover, the reduced effect of NO2(-) on OCl(-) production was attributed to that NO2(-) reduced H2O2 production in activated neutrophils without influencing the release of myeloperoxidase (MPO), thus limiting OCl(-) production by MPO/H2O2 system. Nitrogen Dioxide 32-35 myeloperoxidase Homo sapiens 232-235 26854590-8 2016 Moreover, the reduced effect of NO2(-) on OCl(-) production was attributed to that NO2(-) reduced H2O2 production in activated neutrophils without influencing the release of myeloperoxidase (MPO), thus limiting OCl(-) production by MPO/H2O2 system. Nitrogen Dioxide 83-86 myeloperoxidase Homo sapiens 232-235 17364963-1 2007 Production of nitrogen dioxide by the activity of myeloperoxidase (MPO) in the presence of nitrite is now considered a key step in the pathophysiology of low-density lipoprotein (LDL) oxidation. Nitrogen Dioxide 14-30 myeloperoxidase Homo sapiens 50-65 17364963-1 2007 Production of nitrogen dioxide by the activity of myeloperoxidase (MPO) in the presence of nitrite is now considered a key step in the pathophysiology of low-density lipoprotein (LDL) oxidation. Nitrogen Dioxide 14-30 myeloperoxidase Homo sapiens 67-70 12361810-3 2002 While NO(2)Tyr has been considered a marker of peroxynitrite (ONOO(-)) formation previously, there is growing evidence that heme-protein peroxidase activity, in particular neutrophil-derived myeloperoxidase (MPO), significantly contributes to NO(2)Tyr formation in vivo via the oxidation of nitrite (NO(2)(-)) to nitrogen dioxide (.NO(2)). Nitrogen Dioxide 313-329 myeloperoxidase Homo sapiens 191-206 15354951-0 2004 [Oxides of nitrogen (NO* and NO2-) as cofactors of the myeloperoxidase system]. Nitrogen Dioxide 29-32 myeloperoxidase Homo sapiens 55-70 15354951-9 2004 Nitrogen dioxide is formed after nitrite oxidation by myeloperoxidase. Nitrogen Dioxide 0-16 myeloperoxidase Homo sapiens 54-69