Neutrophils convert tyrosyl residues in albumin to chlorotyrosine

Kettle, Anthony J.

doi:10.1016/0014-5793(95)01494-2

Cited by 183 publications

(125 citation statements)

References 23 publications

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“…There is good evidence for limited protein oxidation during inflammatory reactions ; for example, broncheoalveolar fluids have elevated methionine sulphoxide\methionine ratios under conditions in which leucocyte activation is apparent [221]. Furthermore, oxidized proteins (and DNA) form inside the leucocytes during their triggering, as judged by protein carbonyls [222] and tyrosine modification [223], although it is not clear whether this affects protein function directly.…”

Section: Protein Oxidation In Host Defence and Tissue Catabolismmentioning

confidence: 99%

Biochemistry and pathology of radical-mediated protein oxidation

Dean

Stocker

et al. 1997

Biochemical Journal

1,551

982

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Radical-mediated damage to proteins may be initiated by electron leakage, metal-ion-dependent reactions and autoxidation of lipids and sugars. The consequent protein oxidation is O2-dependent, and involves several propagating radicals, notably alkoxyl radicals. Its products include several categories of reactive species, and a range of stable products whose chemistry is currently being elucidated. Among the reactive products, protein hydroperoxides can generate further radical fluxes on reaction with transition-metal ions; protein-bound reductants (notably dopa) can reduce transition-metal ions and thereby facilitate their reaction with hydroperoxides; and aldehydes may participate in Schiff-base formation and other reactions. Cells can detoxify some of the reactive species, e.g. by reducing protein hydroperoxides to unreactive hydroxides. Oxidized proteins are often functionally inactive and their unfolding is associated with enhanced susceptibility to proteinases. Thus cells can generally remove oxidized proteins by proteolysis. However, certain oxidized proteins are poorly handled by cells, and together with possible alterations in the rate of production of oxidized proteins, this may contribute to the observed accumulation and damaging actions of oxidized proteins during aging and in pathologies such as diabetes, atherosclerosis and neurodegenerative diseases. Protein oxidation may also sometimes play controlling roles in cellular remodelling and cell growth. Proteins are also key targets in defensive cytolysis and in inflammatory self-damage. The possibility of selective protection against protein oxidation (antioxidation) is raised.

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Section: Protein Oxidation In Host Defence and Tissue Catabolismmentioning

confidence: 99%

Biochemistry and pathology of radical-mediated protein oxidation

Dean

Stocker

et al. 1997

Biochemical Journal

1,551

982

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“…The first of these involves oxygen-radical formation catalysed by trace transitionmetal ions ; the second involves chlorinating and oxidizing species, such as HOCl [the physiological mixture of hypochlorous acid and its anion ( − OCl) present at pH 7.4] or Cl # , generated by the haem enzyme myeloperoxidase (MPO) [22,23,25]. DOPA, diTyr, o-and m-Tyr, valine and leucine alcohols are known products of hydroxyl-radical-mediated oxidation of Tyr, Phe, Val and Leu side chains, whereas di-Tyr and 3-chloroTyr are well-defined products of Tyr oxidation induced by MPO-derived species ( [22,26,27], reviewed in [28]). MPO, released from activated leucocytes, catalyses the formation of HOCl from physiological concentrations of Cl − ions and H # O # (generated via the oxidative burst of leucocytes as well as other cells) [29].…”

Section: Introductionmentioning

confidence: 99%

Detection of HOCl-mediated protein oxidation products in the extracellular matrix of human atherosclerotic plaques

Woods

Linton

Davies

2003

Biochemical Journal

107

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Oxidation is believed to play a role in atherosclerosis. Oxidized lipids, sterols and proteins have been detected in early, intermediate and advanced human lesions at elevated levels. The spectrum of oxidized side-chain products detected on proteins from homogenates of advanced human lesions has been interpreted in terms of the occurrence of two oxidative mechanisms, one involving oxygen-derived radicals catalysed by trace transition metal ions, and a second involving chlorinating species (HOCl or Cl2), generated by the haem enzyme 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. In this study proteins extracted from extracellular matrix material obtained from advanced human atherosclerotic lesions are shown to contain elevated levels of oxidized amino acids [3,4-dihydroxyphenylalanine (DOPA), di-tyrosine, 2-hydroxyphenylalanine (o-Tyr)] when compared with healthy (human and pig) arterial tissue. These matrix-derived materials account for 83—96% of the total oxidized protein side-chain products detected in these plaques. Oxidation of matrix components extracted from healthy artery tissue, and model proteins, with reagent HOCl is shown to give rise to a similar pattern of products to those detected in advanced human lesions. The detection of elevated levels of DOPA and o-Tyr, which have been previously attributed to the occurrence of oxygen-radical-mediated reactions, by HOCl treatment, suggests an alternative route to the formation of these materials in plaques. This is believed to involve the formation and subsequent decomposition of protein chloramines.

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“…HOCl reacts with aromatic rings, such as in tyrosine, yielding 3-chlorotyrosine and 3,5-dichlorotyrosine (5,18,19). These products have been detected in proteins exposed to MPO or stimulated neutrophils (20) and in low-density lipoprotein isolated from atherosclerotic lesions (19).…”

mentioning

confidence: 99%

Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen

Miyamoto

Martinez²,

Rettori³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

124

108

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The reaction of hypochlorous acid (HOCl) with hydrogen peroxide is known to generate stoichiometric amounts of singlet molecular oxygen [O2 ( 1 ⌬g)]. This study shows that HOCl can also react with linoleic acid hydroperoxide (LAOOH), generating O2 ( 1 ⌬g) with a yield of 13 ؎ 2% at physiological pH. Characteristic light emission at 1,270 nm, corresponding to O2 ( 1 ⌬g) monomolecular decay, was observed when HOCl was reacted with LAOOH or with liposomes containing phosphatidylcholine hydroperoxides, but not with cumene hydroperoxide or tert-butyl hydroperoxide. The generation of O2 ( 1 ⌬g lipid hydroperoxides ͉ mass spectrometry ͉ myeloperoxidase ͉ near-infrared emission ͉ 18 O-labeled oxygen

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Neutrophils convert tyrosyl residues in albumin to chlorotyrosine

Cited by 183 publications

References 23 publications

Biochemistry and pathology of radical-mediated protein oxidation

Biochemistry and pathology of radical-mediated protein oxidation

Detection of HOCl-mediated protein oxidation products in the extracellular matrix of human atherosclerotic plaques

Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen

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