PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26579678-3 2015 MPO is the antigen against which anti-MPO ANCAs are directed, the antigen to which pathogenic T cells that can induce antibody-independent AAV are directed, and MPO can induce glomerular injury directly by interacting with H2O2 and a halide to halogenate glomerular structures. halide 234-240 myeloperoxidase Homo sapiens 0-3 26898502-1 2016 Myeloperoxidase (MPO) released at sites of inflammation catalyzes the formation of the oxidants hypochlorous acid (HOCl) and hypothiocyanous acid (HOSCN) from H2O2 and halide and pseudo-halide ions. halide 168-174 myeloperoxidase Homo sapiens 0-15 26898502-1 2016 Myeloperoxidase (MPO) released at sites of inflammation catalyzes the formation of the oxidants hypochlorous acid (HOCl) and hypothiocyanous acid (HOSCN) from H2O2 and halide and pseudo-halide ions. halide 168-174 myeloperoxidase Homo sapiens 17-20 22810731-5 2014 Indeed, at the site of inflammation, taurine is known to react with and detoxify hypochlorous acid generated by the neutrophil myeloperoxidase (MPO)-halide system. halide 149-155 myeloperoxidase Homo sapiens 127-142 26279325-4 2015 The microbicidal activity of MPO exists due to its capability to oxidize halide and pseudohalide ions (CI(-), Br(-), I(-) and SCN(-)) by H2O2, thereby producing respective hypohalous acids (HOX). halide 73-79 myeloperoxidase Homo sapiens 29-32 24632382-1 2014 Myeloperoxidase is an important heme enzyme released by activated leukocytes that catalyzes the reaction of hydrogen peroxide with halide and pseudo-halide ions to form various hypohalous acids. halide 131-137 myeloperoxidase Homo sapiens 0-15 22810731-5 2014 Indeed, at the site of inflammation, taurine is known to react with and detoxify hypochlorous acid generated by the neutrophil myeloperoxidase (MPO)-halide system. halide 149-155 myeloperoxidase Homo sapiens 144-147 22348603-2 2012 MPO is released by activated neutrophils, monocytes and some tissue macrophages, where it catalyses the conversion of hydrogen peroxide to hypohalous acids (HOX; X = Cl, Br, SCN) in the presence of halide and pseudo-halide ions. halide 198-204 myeloperoxidase Homo sapiens 0-3 24504973-3 2014 The inhibition or the absence of the MPO-H2O2-halide system results in marked reduction in PMN killing of a variety of microbes, implicating its relative prominence in the hierarchy of PMN antimicrobial systems. halide 46-52 myeloperoxidase Homo sapiens 37-40 24194519-10 2013 HX1 was a mixed-type inhibitor of the halogenation activity of MPO with respect to both hydrogen peroxide and halide. halide 110-116 myeloperoxidase Homo sapiens 63-66 19968966-1 2010 The heme peroxidase enzyme myeloperoxidase (MPO) is released by activated neutrophils and monocytes, where it uses hydrogen peroxide (H(2)O(2)) to catalyze the production of the potent oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) from halide and pseudohalide (SCN(-)) ions. halide 282-288 myeloperoxidase Homo sapiens 27-42 22039673-1 2011 Taurine chloramine (TauCl) is generated at the site of inflammation as a result of reaction of taurine with hypochlorous acid (HOCl), the product of myeloperoxidase-halide system of neutrophils. halide 165-171 myeloperoxidase Homo sapiens 149-164 19968966-1 2010 The heme peroxidase enzyme myeloperoxidase (MPO) is released by activated neutrophils and monocytes, where it uses hydrogen peroxide (H(2)O(2)) to catalyze the production of the potent oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) from halide and pseudohalide (SCN(-)) ions. halide 282-288 myeloperoxidase Homo sapiens 44-47 19968966-3 2010 It is shown here that acetaminophen (paracetamol), a phenol-based drug with analgesic and antipyretic actions, is an efficient inhibitor of HOCl and HOBr generation by isolated MPO-H(2)O(2)-halide systems. halide 190-196 myeloperoxidase Homo sapiens 177-180 20369749-4 2010 Oxidative stress (OS) is the main element in this modification and the most significant is the myeloperoxidase/H2O2/halide system. halide 116-122 myeloperoxidase Homo sapiens 95-110 18652572-1 2008 Myeloperoxidase, released by activated phagocytes, forms reactive oxidants by catalysing the reaction of halide and pseudo-halide ions with H(2)O(2). halide 105-111 myeloperoxidase Homo sapiens 0-15 18652572-1 2008 Myeloperoxidase, released by activated phagocytes, forms reactive oxidants by catalysing the reaction of halide and pseudo-halide ions with H(2)O(2). halide 123-129 myeloperoxidase Homo sapiens 0-15 18652572-3 2008 With physiological levels of halide and pseudo-halide ions, similar amounts of HOCl (hypochlorous acid) and HOSCN (hypothiocyanous acid) are produced by myeloperoxidase. halide 29-35 myeloperoxidase Homo sapiens 153-168 18047295-1 2007 Hypohalous acids are generated from the oxidation of halide ions by myeloperoxidase and eosinophil peroxidase in the presence of H2O2. halide 53-59 myeloperoxidase Homo sapiens 68-83 17141727-0 2007 Differential effects of flavonols on inactivation of alpha1-antitrypsin induced by hypohalous acids and the myeloperoxidase-hydrogen peroxide-halide system. halide 142-148 myeloperoxidase Homo sapiens 108-123 17875773-11 2007 CONCLUSIONS: These results indicated that highly toxic ROS such as .OH generated via the hydrogen peroxide/MPO/halide system induce apoptosis and that ROS may be the direct mediators of EGCG-induced apoptosis in MPO-positive leukemic cells. halide 111-117 myeloperoxidase Homo sapiens 107-110 17875773-11 2007 CONCLUSIONS: These results indicated that highly toxic ROS such as .OH generated via the hydrogen peroxide/MPO/halide system induce apoptosis and that ROS may be the direct mediators of EGCG-induced apoptosis in MPO-positive leukemic cells. halide 111-117 myeloperoxidase Homo sapiens 212-215 17209550-0 2007 Kinetic evidence supports the existence of two halide binding sites that have a distinct impact on the heme iron microenvironment in myeloperoxidase. halide 47-53 myeloperoxidase Homo sapiens 133-148 17209550-8 2007 Our results are consistent with two halide binding sites that could be populated by two halides in which both display distinct effects on the MPO heme iron microenvironment. halide 36-42 myeloperoxidase Homo sapiens 142-145 16111649-4 2006 The comparison of experimentally derived and calculated data revealed that Cl(2), Br(2), or BrCl will primarily be formed by the myeloperoxidase-H(2)O(2)-halide system. halide 154-160 myeloperoxidase Homo sapiens 129-144 18453132-3 2007 The inhibition or absence of the MPO-H2O2-halide system results in marked reduction in PMN killing of a variety of microbes, implicating its relative prominence in the hierarchy of PMN antimicrobial systems. halide 42-48 myeloperoxidase Homo sapiens 33-36 17076648-7 2006 Recently, we found that a highly toxic reactive oxygen species (ROS) generated via the hydrogen peroxide/myeloperoxidase [H(2)O(2)/MPO/halide] system by natural compounds induces apoptosis in MPO-positive leukemic cells. halide 135-141 myeloperoxidase Homo sapiens 105-120 17076648-7 2006 Recently, we found that a highly toxic reactive oxygen species (ROS) generated via the hydrogen peroxide/myeloperoxidase [H(2)O(2)/MPO/halide] system by natural compounds induces apoptosis in MPO-positive leukemic cells. halide 135-141 myeloperoxidase Homo sapiens 131-134 17076648-7 2006 Recently, we found that a highly toxic reactive oxygen species (ROS) generated via the hydrogen peroxide/myeloperoxidase [H(2)O(2)/MPO/halide] system by natural compounds induces apoptosis in MPO-positive leukemic cells. halide 135-141 myeloperoxidase Homo sapiens 192-195 15161651-1 2004 Inflammatory infiltrates can modify (lipo)proteins via hypochlorous acid/hypochlorite (HOCl/OCl(-)) an oxidant formed by the myeloperoxidase-H(2)O(2)-halide system. halide 150-156 myeloperoxidase Homo sapiens 125-140 15689384-5 2005 Among the antimicrobial systems formed in the phagosome is one consisting of myeloperoxidase (MPO), released into the phagosome during the degranulation process, hydrogen peroxide (H2O2), formed by the respiratory burst and a halide, particularly chloride. halide 226-232 myeloperoxidase Homo sapiens 77-92 15689384-5 2005 Among the antimicrobial systems formed in the phagosome is one consisting of myeloperoxidase (MPO), released into the phagosome during the degranulation process, hydrogen peroxide (H2O2), formed by the respiratory burst and a halide, particularly chloride. halide 226-232 myeloperoxidase Homo sapiens 94-97 15689384-8 2005 This review will consider the potential sources of H2O2 for the MPO-H2O2-halide system; the toxic products of the MPO system; the evidence for MPO involvement in the microbicidal activity of neutrophils; the involvement of MPO-independent antimicrobial systems; and the role of the MPO system in tissue injury. halide 73-79 myeloperoxidase Homo sapiens 64-67 15161651-9 2004 The demonstration of selective up-regulation of a subgroup of genes if proteinuria is accompanied by the presence of HOCl-modified (lipo)proteins support the potential pathophysiological role of the myeloperoxidase-H(2)O(2)-halide system and HOCl-LDL in renal disease. halide 224-230 myeloperoxidase Homo sapiens 199-214 14556977-0 2003 Prostanoids and MPO-halide system products as a link between innate and adaptive immunity. halide 20-26 myeloperoxidase Homo sapiens 16-19 14556977-7 2003 In this paper we have focused on the role of taurine chloramine (TauCl), the physiological product of neutrophil MPO-halide system, in the regulation of immune system. halide 117-123 myeloperoxidase Homo sapiens 113-116 12953846-1 2003 The microbicidal activity of the myeloperoxidase (MPO)-hydrogen peroxide-halide system has been implicated as the most efficient, oxygen-dependent antimicrobial component of neutrophil host defense. halide 73-79 myeloperoxidase Homo sapiens 33-48 12707270-9 2003 In contrast, previous studies have demonstrated that 5-bromouracil could be generated by either eosinophil peroxidase or myeloperoxidase, which preferentially brominates uracil at plasma concentrations of halide and under moderately acidic conditions. halide 205-211 myeloperoxidase Homo sapiens 121-136 12953846-1 2003 The microbicidal activity of the myeloperoxidase (MPO)-hydrogen peroxide-halide system has been implicated as the most efficient, oxygen-dependent antimicrobial component of neutrophil host defense. halide 73-79 myeloperoxidase Homo sapiens 50-53 12060654-2 2002 One important pathway may involve the production of potent halogenating agents such as hypochlorous acid (HOCl) by the myeloperoxidase-hydrogen peroxide-halide system. halide 153-159 myeloperoxidase Homo sapiens 119-134 12070141-8 2002 The colocalization of immunoreactive HOCl-modified epitopes with apolipoprotein A-I along with deposits of lipids in serial sections of human atheroma shown here indicates that the myeloperoxidase-H(2)O(2)-halide system contributes to oxidative damage of HDL in vivo. halide 206-212 myeloperoxidase Homo sapiens 181-196 11594511-1 2001 Optimal oxygen-dependent antimicrobial activity of circulating polymorphonuclear leukocytes reflects the synergistic effects of the myeloperoxidase (MPO)-hydrogen peroxide-halide system. halide 172-178 myeloperoxidase Homo sapiens 132-147 11796821-2 2002 Although the nature of the in vivo oxidants has not been clearly identified, increasing evidence suggested the myeloperoxidase (MPO)-H(2)O(2)-halide system to be responsible for the damage observed in leukocyte-dependent glomerulonephritis. halide 142-148 myeloperoxidase Homo sapiens 111-126 11796821-2 2002 Although the nature of the in vivo oxidants has not been clearly identified, increasing evidence suggested the myeloperoxidase (MPO)-H(2)O(2)-halide system to be responsible for the damage observed in leukocyte-dependent glomerulonephritis. halide 142-148 myeloperoxidase Homo sapiens 128-131 11796821-13 2002 The observed colocalization of HOCl-modified proteins and MPO in podocytes and adjacent basement membranes strengthens the assumption that the MPO-H(2)O(2)-halide system contributes to glomerular dysfunction in patients with membranous glomerulonephritis. halide 156-162 myeloperoxidase Homo sapiens 58-61 11796821-13 2002 The observed colocalization of HOCl-modified proteins and MPO in podocytes and adjacent basement membranes strengthens the assumption that the MPO-H(2)O(2)-halide system contributes to glomerular dysfunction in patients with membranous glomerulonephritis. halide 156-162 myeloperoxidase Homo sapiens 143-146 11594511-1 2001 Optimal oxygen-dependent antimicrobial activity of circulating polymorphonuclear leukocytes reflects the synergistic effects of the myeloperoxidase (MPO)-hydrogen peroxide-halide system. halide 172-178 myeloperoxidase Homo sapiens 149-152 11422382-3 2001 At plasma concentrations of halide ion, hypochlorous acid is a major product of the myeloperoxidase-hydrogen peroxide-chloride system. halide 28-34 myeloperoxidase Homo sapiens 84-99 10766826-0 2000 X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. halide 48-54 myeloperoxidase Homo sapiens 78-93 11278358-1 2001 Hypochlorous acid/hypochlorite, generated by the myeloperoxidase/H(2)O(2)/halide system of activated phagocytes, has been shown to oxidize/modify low density lipoprotein (LDL) in vitro and may be involved in the formation of atherogenic lipoproteins in vivo. halide 74-80 myeloperoxidase Homo sapiens 49-64 10880973-0 2000 Immunohistochemical evidence for the myeloperoxidase/H2O2/halide system in human atherosclerotic lesions: colocalization of myeloperoxidase and hypochlorite-modified proteins. halide 58-64 myeloperoxidase Homo sapiens 37-52 10880973-5 2000 The antibodies recognized a specific epitope present on various proteins after treatment with OCl- added as reagent or generated by the MPO/H2O2/halide system. halide 145-151 myeloperoxidase Homo sapiens 136-139 10880973-10 2000 The colocalization of immunoreactive MPO and HOCl-modified-epitopes in serial sections of human atheroma (type IV), fibroatheroma (type V) and complicated (type VI) lesions provides further convincing evidence for MPO/H2O2/halide system-mediated oxidation of (lipo)proteins under in vivo conditions. halide 223-229 myeloperoxidase Homo sapiens 37-40 10880973-10 2000 The colocalization of immunoreactive MPO and HOCl-modified-epitopes in serial sections of human atheroma (type IV), fibroatheroma (type V) and complicated (type VI) lesions provides further convincing evidence for MPO/H2O2/halide system-mediated oxidation of (lipo)proteins under in vivo conditions. halide 223-229 myeloperoxidase Homo sapiens 214-217 10766826-6 2000 The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase. halide 64-70 myeloperoxidase Homo sapiens 155-170 9766843-3 1998 During concomitant activation of the NADPH-dependent oxidase, the stimulated neutrophil also generates hydrogen peroxide, and in this way the MPO-hydrogen peroxide-halide system exerts its potent microbicidal activity. halide 164-170 myeloperoxidase Homo sapiens 142-145 10699463-2 2000 Myeloperoxidase (MPO), a heme-containing glycoprotein located in the primary granules of polymorphonuclear leukocytes and monocytes, reacts with H(2)O(2) and halide ion and produces a more potent microbicidal oxidant, hypochlorous acid (HOCl). halide 158-164 myeloperoxidase Homo sapiens 0-15 10699463-2 2000 Myeloperoxidase (MPO), a heme-containing glycoprotein located in the primary granules of polymorphonuclear leukocytes and monocytes, reacts with H(2)O(2) and halide ion and produces a more potent microbicidal oxidant, hypochlorous acid (HOCl). halide 158-164 myeloperoxidase Homo sapiens 17-20 9261850-11 1997 We conclude that proteinase-free myeloperoxidase, in the presence of non-toxic concentrations of its substrates, hydrogen peroxide and halide, produced increases in permeability to non-ionic molecules in the rat trachea within 15 minutes. halide 135-141 myeloperoxidase Homo sapiens 33-48 9706251-9 1998 The MPO/NADH/halide systems, where NADH replaced H2O2, also inactivated LADH. halide 13-19 myeloperoxidase Homo sapiens 4-7 9425735-3 1997 Here, Janusz Marcinkiewicz examines recent data indicating that chloramines, the neutrophil-specific products of the myeloperoxidase--hydrogen-peroxide--halide system, may provide a bridge between the afferent branches of the innate and acquired immune response. halide 153-159 myeloperoxidase Homo sapiens 117-132 9033274-3 1997 Although the nature of the in vivo oxidants remains unknown, recent findings indicated that the myeloperoxidase (MPO)-H2O2-halide system could play an important role in modification of (lipo)proteins in human tissues. halide 123-129 myeloperoxidase Homo sapiens 96-111 9151778-3 1997 Myeloperoxidase is the only human enzyme known to generate hypochlorous acid (HOCl), a potent oxidizing agent, at physiological halide concentrations. halide 128-134 myeloperoxidase Homo sapiens 0-15 9033274-3 1997 Although the nature of the in vivo oxidants remains unknown, recent findings indicated that the myeloperoxidase (MPO)-H2O2-halide system could play an important role in modification of (lipo)proteins in human tissues. halide 123-129 myeloperoxidase Homo sapiens 113-116 1329616-4 1992 The antimicrobial agents also inhibited the generation of reactive oxidants by the MPO-H2O2-halide system during activation of both untreated and 1-hp-treated neutrophils by FMLP. halide 92-98 myeloperoxidase Homo sapiens 83-86 7750983-0 1994 Oxidants generated by the myeloperoxidase-halide system activate the fifth component of human complement, C5. halide 42-48 myeloperoxidase Homo sapiens 26-41 7750983-7 1994 Since hypochlorite and T-NCl are biological products generated by the myeloperoxidase-halide system of stimulated leukocytes, the activation of C5 by these agents may be one way to complement activation during inflammation and tissue injury. halide 86-92 myeloperoxidase Homo sapiens 70-85 7814266-4 1994 The H2O2-MPO-halide system in phagocytosing cells was localized at the fine structural level by our development of 3,3"-diaminobenzidine (DAB) as a cytochemical probe for detecting peroxidase activities. halide 13-19 myeloperoxidase Homo sapiens 9-12 8177196-4 1994 Measurement of O2- production capacity was used as a reflection of the activity of NADPH oxidase, and the activity of myeloperoxidase-H2O2-halide system was evaluated using luminol-dependent chemiluminescence. halide 139-145 myeloperoxidase Homo sapiens 118-133 8177196-8 1994 These results suggest that postoperative PMN signal transduction mechanisms, mediated by protein kinase C, may activate myeloperoxidase-H2-O2-halide system but suppress NADPH oxidase system dependently of the degree of surgical stress, revealing a differential effect of protein kinase C activation on PMN microbicidal activity. halide 142-148 myeloperoxidase Homo sapiens 120-135 8145684-4 1993 As chemiluminogenic probes we have employed lucigenin and luminon that are know to be sensitive to the superoxide anion and the H2O2-myeloperoxidase-halide system of PMNs, respectively. halide 149-155 myeloperoxidase Homo sapiens 133-148 8145684-5 1993 Activated PMNs from children with trisomy 21 exhibited a low level of superoxide and a reduced activity of H2O2-myeloperoxidase-halide system compared to the control group. halide 128-134 myeloperoxidase Homo sapiens 112-127 1337069-6 1992 Both antimicrobial agents caused a dose-related stimulation of neutrophil migration which was associated with inhibition of leucoattractant-activated generation of superoxide and activity of the myeloperoxidase/H2O2/halide system. halide 216-222 myeloperoxidase Homo sapiens 195-210 1847831-0 1991 Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I. EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide. halide 15-21 myeloperoxidase Homo sapiens 51-66 1662050-1 1991 The degranulation and myeloperoxidase-H2O2-halide activities of human polymorphonuclear leukocytes from healthy donors were tested after co-incubation with either Brucella melitensis 16M, Staphylococcus aureus or Staphylococcus aureus in presence of lipopolysaccharide, protein fraction, native hapten and soluble fractions released at 65 degrees C from smooth strain of Brucella melitensis 16M. halide 43-49 myeloperoxidase Homo sapiens 22-37 1849170-7 1991 On the basis of above findings, we speculate that phagocytosis of CGD PMNs is increased because the H2O2-myeloperoxidase-halide system, which may modulate phagocytic activity of PMNs, fails to operate. halide 121-127 myeloperoxidase Homo sapiens 105-120 1847831-0 1991 Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I. EPR spectra of the low-spin cyanide complex of myeloperoxidase have been measured in the absence and presence of halide substrates; chloride, bromide and iodide. halide 15-21 myeloperoxidase Homo sapiens 160-175 2165113-3 1990 Further, both azide and catalase + superoxide dismutase inhibited the ability of normal neutrophils to damage hyphae, suggesting that this damage is mediated by products of the respiratory burst and by the MPO-halide system. halide 210-216 myeloperoxidase Homo sapiens 206-209 2560462-5 1989 Pretreatment with inhibitors of oxidative burst demonstrated that the yeast cell killing by MDP-stimulated PMN was not affected by SOD but was inhibited by sodium azide, indicating the involvement of myeloperoxidase (MPO)-halide system in fungicidal mechanisms induced by MDP. halide 222-228 myeloperoxidase Homo sapiens 217-220 2560462-7 1989 Inhibition by sodium azide and sodium benzoate indicated that these oxygen metabolites could be derived from the MPO-halide system but also from hydroxyl radical production. halide 117-123 myeloperoxidase Homo sapiens 113-116 2785522-4 1989 Ligand binding via this receptor is rapidly inactivated by products of the myeloperoxidase-hydrogen peroxide-halide system of PMN. halide 109-115 myeloperoxidase Homo sapiens 75-90 2556228-1 1989 We have demonstrated that penicillamine (PSH) has the capacity to effect phagocytic cells by its interaction with the myeloperoxidase-halide system (MPOHS). halide 134-140 myeloperoxidase Homo sapiens 118-133 2556228-9 1989 In conclusion, PSH inhibits the myeloperoxidase-halide system at a cellular level by scavenging H2O2 rather than by oxidation of the myeloperoxidase enzyme. halide 48-54 myeloperoxidase Homo sapiens 32-47 6095920-7 1984 Since the myeloperoxidase-H2O2-halide system also affects chemotactic factors, leukotrienes, proteinases and membrane receptors, the system may in several ways affect the development of the inflammatory response. halide 31-37 myeloperoxidase Homo sapiens 10-25 2848083-1 1988 The neutrophil myeloperoxidase-H2O2-halide enzyme system produces hypochlorous acid and chlorinated amine compounds capable of killing a variety of target cells. halide 36-42 myeloperoxidase Homo sapiens 15-30 3034783-17 1987 These findings suggest that cellular products generated by the H2O2-MPO-halide system down-regulate the rosette-forming and phagocytic activity of PMNs from normal healthy individuals, but not that from CGD and MPO-deficient patients. halide 72-78 myeloperoxidase Homo sapiens 68-71 3032797-10 1987 Arginine, a scavenger of hypochlorite, significantly depressed the ability of sCM-treated neutrophils to kill amoebae and also prevented the amoebicidal properties of the MPO-H2O2-halide system. halide 180-186 myeloperoxidase Homo sapiens 171-174 3032797-11 1987 These results suggest that the MPO-H2O2-halide system is important in the killing of naegleriae by sCM-treated neutrophils and that hypochlorite may be the amoebicidal agent. halide 40-46 myeloperoxidase Homo sapiens 31-34 3009589-3 1986 The azurophilic granules supply enzymes for digestive and bactericidal functions and supply MPO to the MPO-halide-hydrogen peroxide bactericidal system. halide 107-113 myeloperoxidase Homo sapiens 92-95 3009589-3 1986 The azurophilic granules supply enzymes for digestive and bactericidal functions and supply MPO to the MPO-halide-hydrogen peroxide bactericidal system. halide 107-113 myeloperoxidase Homo sapiens 103-106 3002685-0 1985 Differentiated HL60 promyelocytic leukaemia cells have a deficient myeloperoxidase/halide killing system. halide 83-89 myeloperoxidase Homo sapiens 67-82 2991014-1 1985 We have previously studied purified human myeloperoxidase-hydrogen peroxide-halide ion systems as models of possible singlet oxygen production by granulocytes. halide 76-82 myeloperoxidase Homo sapiens 42-57 2981925-3 1985 Neutrophils and other phagocytes can injure cells by means of oxygen-dependent mechanisms, particularly the myeloperoxidase (MPO)-H2O2-halide system. halide 135-141 myeloperoxidase Homo sapiens 108-123 2981925-3 1985 Neutrophils and other phagocytes can injure cells by means of oxygen-dependent mechanisms, particularly the myeloperoxidase (MPO)-H2O2-halide system. halide 135-141 myeloperoxidase Homo sapiens 125-128 2981586-5 1985 These data indicate extracellular destruction of functional B12 binding protein by the halide-dependent heme enzyme myeloperoxidase and H2O2. halide 87-93 myeloperoxidase Homo sapiens 116-131 6090506-1 1984 The myeloperoxidase (MPO)-hydrogen peroxide (H2O2)-halide systems were found to produce chemiluminescence at 1,268 nm, a characteristic emission band for singlet oxygen (1O2). halide 51-57 myeloperoxidase Homo sapiens 4-19 6090506-1 1984 The myeloperoxidase (MPO)-hydrogen peroxide (H2O2)-halide systems were found to produce chemiluminescence at 1,268 nm, a characteristic emission band for singlet oxygen (1O2). halide 51-57 myeloperoxidase Homo sapiens 21-24 6090506-12 1984 While the MPO-H2O2-halide systems can efficiently produce 1O2, the conditions required are not physiologic, which suggests that the chemiluminescence of the stimulated neutrophil does not derive from 1O2 generated by a MPO mechanism. halide 19-25 myeloperoxidase Homo sapiens 10-13 6487320-1 1984 A method for investigating the cellular response of polymorphonuclear leukocytes to various stimuli was introduced using simultaneously native (luminol-independent) and luminol dependent luminescence as an indicator for myeloperoxidase (MPO)-H2O2-halide and O2- mediated reactions. halide 247-253 myeloperoxidase Homo sapiens 220-235 6487320-1 1984 A method for investigating the cellular response of polymorphonuclear leukocytes to various stimuli was introduced using simultaneously native (luminol-independent) and luminol dependent luminescence as an indicator for myeloperoxidase (MPO)-H2O2-halide and O2- mediated reactions. halide 247-253 myeloperoxidase Homo sapiens 237-240 6487320-3 1984 Consequently the MPO-H2O2-halide system could be distinguished from the O2- dependent system by interpreting the recorded temporal traces of the emitted light. halide 26-32 myeloperoxidase Homo sapiens 17-20 6321554-10 1984 These data indicate that, apart from being a potent antimicrobial system, the oxidizing activity of the MPO-H2O2-halide system may modulate the inflammatory response by impairing certain receptor-mediated recognition mechanisms of phagocytic cells, which otherwise could elicit inflammatory reactions and tissue injury. halide 113-119 myeloperoxidase Homo sapiens 104-107 6315700-2 1983 We report here that both the myeloperoxidase-H2O2-halide system and OH released in this way can degrade the leukotrienes (LT) formed by neutrophils. halide 50-56 myeloperoxidase Homo sapiens 29-44 6322510-8 1984 In addition, the MPO deficiency impairs the H2O2-halide-MPO system, which is of particular importance for fungal killing, e.g. of C. albicans, which has also been reported to be deficient in DS. halide 49-55 myeloperoxidase Homo sapiens 17-20 6315700-6 1983 LTC4 degradation by the cell-free myeloperoxidase-H2O2-halide system and the OH -generating acetaldehyde-xanthine oxidase-Fe2+ system had inhibitor profiles comparable to normal and myeloperoxidase-deficient neutrophils, respectively. halide 55-61 myeloperoxidase Homo sapiens 34-49 6311062-2 1983 The exposure of alpha 1-protease inhibitor to the myeloperoxidase-hydrogen peroxide-halide system resulted in a nearly complete loss of its ability to bind and inactivate purified human neutrophil elastase. halide 84-90 myeloperoxidase Homo sapiens 50-65 6307386-2 1983 The process of inactivation is impeded by the addition of inhibitors of myeloperoxidase (KCN, NaN3), of catalase, of methionine but not by the addition of superoxide dismutase, indicating that the mechanism of inactivation is the oxidation of methionine residue by myeloperoxidase-H2O2-halide system. halide 286-292 myeloperoxidase Homo sapiens 72-87 6312841-2 1983 MPO is found in polymorphonuclear leukocytes and is important as a bactericidal agent in the presence of H2O2 and halide ions. halide 114-120 myeloperoxidase Homo sapiens 0-3 6286969-4 1982 The MPO-mediated oxidation of GSH required the simultaneous presence of MPO, H2O2, and a halide ion. halide 89-95 myeloperoxidase Homo sapiens 4-7 6186607-4 1983 In the present investigation we show that the MPO-H2O2-halide system can degranulate isolated mast cells with release of histamine and 3H-serotonin. halide 55-61 myeloperoxidase Homo sapiens 46-49 6300255-2 1983 Inhibition by anaerobiosis, azide, cyanide, halide-free conditions, catalase, histidine, and tryptophan suggested mediation of hyphal damage primarily through the myeloperoxidase system. halide 44-50 myeloperoxidase Homo sapiens 163-178 6295926-9 1983 Our results suggest that Raji target cell destruction by PMA-activated neutrophils depends on the myeloperoxidase-hydrogen peroxide-halide system. halide 132-138 myeloperoxidase Homo sapiens 98-113 6292313-11 1982 These evidences suggest that the inactivation of lysosomal enzymes is mainly due to MPO-H2O2-halide system, resulting in inhibition of lysosomal enzyme release from PMN during phagocytosis. halide 93-99 myeloperoxidase Homo sapiens 84-87 6292103-6 1982 Both A. fumigatus and R. oryzae hyphae were damaged by the myeloperoxidase-hydrogen peroxide-halide system either with reagent hydrogen peroxide or enzymatic systems for generating hydrogen peroxide (glucose oxidase with glucose, or xanthine oxidase with either hypoxanthine or acetaldehyde). halide 93-99 myeloperoxidase Homo sapiens 59-74 6288561-4 1982 Both chlamydial biotypes were also rapidly inactivated by the cell-free myeloperoxidase-H2O2-halide system. halide 93-99 myeloperoxidase Homo sapiens 72-87 6282274-5 1982 Preincubation experiments indicated suppression of the myeloperoxidase-halide system. halide 71-77 myeloperoxidase Homo sapiens 55-70 6276480-6 1982 This suggests that the oxidation of met5-enkephalin by phagocytosing PMN was, at least in part, dependent on the MPO system (MPO-H2O2-halide). halide 134-140 myeloperoxidase Homo sapiens 113-116 6276480-6 1982 This suggests that the oxidation of met5-enkephalin by phagocytosing PMN was, at least in part, dependent on the MPO system (MPO-H2O2-halide). halide 134-140 myeloperoxidase Homo sapiens 125-128 6811483-2 1982 Stimulation of neutrophil migration and lymphocyte transformation following a single intravenous injection of 1 g of ascorbate was associated with inhibition of the MPO/H2O2/halide system. halide 174-180 myeloperoxidase Homo sapiens 165-168 6267057-5 1981 In a cell-free system, the fluorescence of 3,3"-dipropylthiodicarbocyanine, but not that of 3,3"-dipentyloxadicarbocyanine, was rapidly eliminated by myeloperoxidase in the presence of hydrogen peroxide and a halide; this loss of fluorescence was inhibited by azide, cyanide, or catalase. halide 209-215 myeloperoxidase Homo sapiens 150-165 6259027-5 1980 It has been suggested that observed intracellular deficiencies of selected enzymes within the neutrophils are of importance with regard to lowered antitumor activity of that cells operating mainly through the myeloperoxidase-H2O2-halide system. halide 230-236 myeloperoxidase Homo sapiens 209-224 6255998-0 1980 The halide complexes of myeloperoxidase and the mechanism of the halogenation reactions. halide 4-10 myeloperoxidase Homo sapiens 24-39 6255998-1 1980 The spectral changes caused by the addition of halides to myeloperoxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7) have been investigated and the dissociation constants of the enzyme-halide complexes have been determined. halide 47-53 myeloperoxidase Homo sapiens 58-73 6255998-2 1980 The pH dependence of the dissociation constants suggests that halide binding is associated with a protonation step in myeloperoxidase. halide 62-68 myeloperoxidase Homo sapiens 118-133 6259068-6 1980 It is suggested that enhanced neutrophil motility is not related to beta-receptor blockade but rather to restricting the availability of hydrogen peroxide and reactive products of the MPO/H2O2/halide system. halide 193-199 myeloperoxidase Homo sapiens 184-187 225268-1 1979 Estradiol 17 beta prevented the fall in the microbicidal activity of the myeloperoxidase-H2O2-halide system induced by high H2O2 concentrations. halide 94-100 myeloperoxidase Homo sapiens 73-88 225353-0 1979 Chemotactic factor inactivation by the myeloperoxidase-hydrogen peroxide-halide system. halide 73-79 myeloperoxidase Homo sapiens 39-54 225353-2 1979 The ability of the myeloperoxidase-H(2)O(2)-halide system of the neutrophil to inactivate chemoattractants was examined using both a radioassay and a morphologic assay of chemotaxis. halide 44-50 myeloperoxidase Homo sapiens 19-34 225268-2 1979 In contrast, when the H2O2 (and halide) concentrations were low the myeloperoxidase-H2O2-halide antimicrobial system was inhibited by estradiol. halide 32-38 myeloperoxidase Homo sapiens 68-83 225268-2 1979 In contrast, when the H2O2 (and halide) concentrations were low the myeloperoxidase-H2O2-halide antimicrobial system was inhibited by estradiol. halide 89-95 myeloperoxidase Homo sapiens 68-83 396794-5 1979 Optimal killing requires the translocation of granule myeloperoxidase into the phagocytic vacuole containing the bacteria and a suitable halide ion. halide 137-143 myeloperoxidase Homo sapiens 54-69 207742-6 1978 Using dapsone concentrations (1-30 mug/ml) comparable with those found after therapeutic doses, we have found that the drug interferes primarily with the myeloperoxidase (MPO)-H(2)O(2)-halide-mediated cytotoxic system in the PMNL. halide 185-191 myeloperoxidase Homo sapiens 154-169 207742-6 1978 Using dapsone concentrations (1-30 mug/ml) comparable with those found after therapeutic doses, we have found that the drug interferes primarily with the myeloperoxidase (MPO)-H(2)O(2)-halide-mediated cytotoxic system in the PMNL. halide 185-191 myeloperoxidase Homo sapiens 171-174 207742-10 1978 Because the MPO-H(2)O(2)-halide system not only fulfills the antimicrobial activity but is suggested to be a modulator of the inflammatory reaction as well, the action of dapsone in dermatitis herpetiformis may in part be explained by its effect on this system. halide 25-31 myeloperoxidase Homo sapiens 12-15 225142-2 1978 After phagocytosis, MPO is released into the phagosome from adjacent granules where it interacts with H2O2 generated either by leukocytic or microbial metabolism and a halide such as chloride or iodide to form agents toxic to the ingested organisms. halide 168-174 myeloperoxidase Homo sapiens 20-23 225142-15 1978 Both the xanthine oxidase system and the MPO-H2O2-halide system convert diphenylfuran into cis-dibenzoylethylene, an effect which is compatible with, although not proof of, the formation of 1O2 by these systems. halide 50-56 myeloperoxidase Homo sapiens 41-44 194641-0 1977 Myeloperoxidase--H2O2--halide system: cytotoxic effect on human blood leukocytes. halide 23-29 myeloperoxidase Homo sapiens 0-15 33040403-7 2021 Compared to the peptide agonist fMLF, RE-04-001 is more resistant to inactivation by the MPO-H2 O2 -halide system. halide 100-106 myeloperoxidase Homo sapiens 89-92 165258-4 1975 The findings support a mechanism involving the phagocytosis-induced extracellular release of MPO and H2O2 and their reation with a halide cofactor to damage the target cells. halide 131-137 myeloperoxidase Homo sapiens 93-96 1131257-0 1975 Halide dependence of the myeloperoxidase-mediated antimicrobial system of the polymorphonuclear leukocyte in the phenomenon of electronic excitation. halide 0-6 myeloperoxidase Homo sapiens 25-40 1120184-4 1975 Myeloperoxidase was effective with either chloride or iodide as the halide, while lastoperoxidase was effective with iodide but not chloride. halide 68-74 myeloperoxidase Homo sapiens 0-15 31424363-4 2020 At the time we demonstrated protein chlorination by HOCl, the major product of neutrophil MPO-halide system enhances protein immunogenicity. halide 94-100 myeloperoxidase Homo sapiens 90-93 31085160-6 2019 In fact, Act-389949 was found to be as potent as the prototype FPR2 peptide agonist WKYMVM and had the advantage of being resistant to oxidation by MPO-H2O2-halide derived oxidants, as compared to the sensitive WKYMVM. halide 157-163 myeloperoxidase Homo sapiens 148-151