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Keywords: myeloperoxidase
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Articles
Biochem J (2014) 457 (1): 89–97.
Published: 10 December 2013
... (myeloperoxidase) in the inflamed artery wall, and smokers have high levels of SCN − , a preferred MPO substrate, with this resulting in HOSCN (hypothiocyanous acid) formation. We hypothesized that this thiol-specific oxidant may target the Zn 2+ –thiol cluster of eNOS (endothelial nitric oxide synthase...
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Biochem J (2011) 439 (3): 423–434.
Published: 13 October 2011
...Raphael F. Queiroz; Sandra M. Vaz; Ohara Augusto The nitroxide tempol (4-hydroxy-2,2,6,6-tetramethyl piperidine-1-oxyl) reduces tissue injury in animal models of inflammation by mechanisms that are not completely understood. MPO (myeloperoxidase), which plays a fundamental role in oxidant...
Includes: Supplementary data
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Biochem J (2010) 425 (1): 285–293.
Published: 14 December 2009
... myeloperoxidase. Among numerous other mediators, platelets liberate serotonin (5-hydroxytryptamine), which is a classical neurotransmitter and vasoactive amine that has significant effects on inflammation and immunity. In the present study, we show that serotonin is a favoured substrate for myeloperoxidase...
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Biochem J (2009) 422 (1): 111–117.
Published: 29 July 2009
...Ojia Skaff; David I. Pattison; Michael J. Davies MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate by H 2 O 2 to HOCl (hypochlorous acid), HOBr (hypobromous acid) and HOSCN (hypothiocyanous acid, also know as cyanosulfenic acid) respectively. Specificity constants...
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Biochem J (2009) 421 (1): 79–86.
Published: 12 June 2009
...Martin D. Rees; Steven E. Bottle; Kathryn E. Fairfull-Smith; Ernst Malle; John M. Whitelock; Michael J. Davies Tissue damage resulting from the extracellular production of HOCl (hypochlorous acid) by the MPO (myeloperoxidase)-hydrogen peroxide-chloride system of activated phagocytes is implicated...
Includes: Supplementary data
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Biochem J (2009) 417 (3): 773–781.
Published: 16 January 2009
...Anna L. P. Chapman; Ojia Skaff; Revathy Senthilmohan; Anthony J. Kettle; Michael J. Davies MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate to their respective hypohalous acids. We have investigated the generation of HOBr by human neutrophils in the presence...
Includes: Supplementary data
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Biochem J (2008) 416 (3): 441–452.
Published: 26 November 2008
...Clare L. Hawkins; David I. Pattison; Naomi R. Stanley; Michael J. Davies Myeloperoxidase, released by activated phagocytes, forms reactive oxidants by catalysing the reaction of halide and pseudo-halide ions with H 2 O 2 . These oxidants have been linked to tissue damage in a range of inflammatory...
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Biochem J (2007) 404 (2): 269–277.
Published: 14 May 2007
...-lysine and the methylglyoxal-derived products, carboxyethyl-lysine, argpyrimidine and MODIC (methylglyoxal-derived imidazolium cross-link). These results provide support for the presence of metal-catalysed oxidation (the Suyama pathway) in diabetes and the possible activation of myeloperoxidase during...
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Biochem J (2007) 402 (2): 229–239.
Published: 12 February 2007
... characterized. We show that the small GTPase Rab27a is an essential component of the secretory machinery of azurophilic granules in granulocytes. Rab27a-deficient mice have impaired secretion of MPO (myeloperoxidase) into the plasma in response to lipopolysaccharide. Cell fractionation analysis revealed...
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Biochem J (2007) 401 (2): 587–596.
Published: 21 December 2006
...Martin D. Rees; Tane N. McNiven; Michael J. Davies EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid). They are released extracellularly by activated leucocytes and their binding to the polyanionic glycosa...
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Biochem J (2006) 394 (3): 707–713.
Published: 24 February 2006
... of eosinophil peroxidase than with the analogous redox intermediate of myeloperoxidase. Nitration by eosinophils was increased 3-fold by superoxide dismutase, which indicates that superoxide interferes with nitration. We propose that at sites of eosinophilic inflammation, low concentrations of nitrite...
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Biochem J (2005) 391 (1): 125–134.
Published: 26 September 2005
...Martin D. Rees; David I. Pattison; Michael J. Davies Activated phagocytes release the haem enzyme MPO (myeloperoxidase) and produce superoxide radicals and H 2 O 2 via an oxidative burst. MPO uses H 2 O 2 and Cl − to form HOCl, the physiological mixture of hypochlorous acid and its anion present...
Includes: Supplementary data
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Biochem J (2004) 381 (1): 175–184.
Published: 22 June 2004
...Martin D. REES; Clare L. HAWKINS; Michael J. DAVIES Activated phagocytes release the haem enzyme MPO (myeloperoxidase) and also generate superoxide radicals (O 2 •− ), and hence H 2 O 2 , via an oxidative burst. Reaction of MPO with H 2 O 2 in the presence of chloride ions generates HOCl...
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Biochem J (2003) 376 (1): 219–227.
Published: 15 November 2003
... for the haem enzyme MPO (myeloperoxidase), released by activated monocytes (and possibly macrophages), in oxidative events within the artery wall. As MPO is released extracellularly, and is highly basic, it might be expected to associate with poly-anionic matrix components thereby localizing damage...
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Biochem J (2003) 375 (1): 33–40.
Published: 01 October 2003
...Anna L. P. CHAPMAN; Christine C. WINTERBOURN; Stephen O. BRENNAN; T. William JORDAN; Anthony J. KETTLE Hypochlorous acid (HOCl) is a potent oxidant produced by myeloperoxidase that causes aggregation of many proteins. Treatment of apohaemoglobin and apomyoglobin with HOCl produced a regular series...
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Biochem J (2003) 370 (2): 729–735.
Published: 01 March 2003
... myeloperoxidase (MPO). As MPO is released extracellularly by activated monocytes (and possibly macrophages) and is a highly basic protein, it would be expected to associate with polyanions such as the glycosaminoglycans of the extracellular matrix, and might result in damage being localized at such sites...
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Biochem J (2002) 367 (2): 467–473.
Published: 15 October 2002
...-stimulated leucocytes. The inhibition of myeloperoxidase activity did not reduce protein nitration; on the other hand, the myeloperoxidase inhibitor aminobenzoic hydrazide caused increased nitration, which was mediated by ONOO - . These results suggest that protein nitration is predominantly mediated...
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Biochem J (2001) 358 (1): 233–239.
Published: 08 August 2001
... and 0.15mM respectively. On the basis of these values thiocyanate is preferred 2.8-fold over bromide as a substrate for eosinophil peroxidase. Eosinophil peroxidase catalysed substantive oxidation of chloride only below pH6.5. We found that when eosinophil peroxidase or myeloperoxidase oxidized thiocyanate...
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