Novel intra-and inter-molecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation

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Show simple item record Raftery, Mark en_US Yang, Zheng en_US Valenzuela, Stella en_US Geczy, Carolyn en_US
dc.contributor.editor en_US 2010-05-28T09:49:26Z 2010-05-28T09:49:26Z 2001 en_US
dc.identifier 2006009317 en_US
dc.identifier.citation Raftery Mark et al. 2001, 'Novel intra-and inter-molecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation', American Society for Biochemistry and Molecular Biology Inc, vol. 276, no. 36, pp. 33393-33401. en_US
dc.identifier.issn 0021-9258 en_US
dc.identifier.other C1UNSUBMIT en_US
dc.description.abstract Hypochlorite is a major oxidant generated when neutrophils and macrophages are activated at inflammatory sites, such as in atherosclerotic lesions. Murine S100A8 (A8) is a major cytoplasmic protein in neutrophils and is secreted by macrophages in response to inflammatory stimuli. After incubation with reagent HOCl for 10 min, ~85% of A8 was converted to 4 oxidation products, with electrospay ionization mass spectrometry masses of m/z 10354, 10388, 10354 ? 1, and 20707 ? 3. All were resistant to reduction by dithiothreitol. Initial formation of a reactive Cys sulfenic acid intermediate was demonstrated by the rapid conjugation of 5,5-dimethyl-1,3-cyclohexanedione (dimedone) to HOCl-treated A8 to form stable adducts. Matrix-assisted laser desorption-reflectron time of flight peptide mass fingerprinting of isolated oxidation products confirmed the mass additions observed in the full-length proteins. Both Met36/73 were converted to Met36/73 sulfoxides. An additional product with an unusual mass addition of m/z 14 (?0.2) was identified and corresponded to the addition of oxygen to Cys41, conjugation to various epsilon -amines of Lys6, Lys34/35, or Lys87 with loss of dihydrogen and formation of stable intra- or inter-molecular sulfinamide cross-links. Specific fragmentations identified in matrix-assisted laser desorption-post source decay spectra and low energy collisional-induced dissociation tandem mass spectroscopy spectra of sulfinamide-containing digest peptides confirmed Lys34/35 to Cys41 sulfinamide bonds. HOCl oxidation of mutants lacking Cys41 (Ala41S100A8) or specific Lys residues (e.g. Lys34/35, Ala34/35S100A8) did not form sulfinamide cross-links. HOCl generated by myeloperoxidase and H2O2 and by phorbol 12-myristate 13-acetate-activated neutrophils also formed these products. en_US
dc.language en_US
dc.publisher American Society for Biochemistry and Molecular Biology Inc en_US
dc.relation.isbasedon en_US
dc.title Novel intra-and inter-molecular sulfinamide bonds in S100A8 produced by hypochlorite oxidation en_US
dc.parent Journal Of Biological Chemistry en_US
dc.journal.volume 276 en_US
dc.journal.number 36 en_US
dc.publocation USA en_US
dc.identifier.startpage 33393 en_US
dc.identifier.endpage 33401 en_US SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 100400 en_US
dc.personcode 0000031962 en_US
dc.personcode 0000031963 en_US
dc.personcode 010690 en_US
dc.personcode CGECZY en_US
dc.percentage 50 en_US Medical Biotechnology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US en_US
dc.location.activity en_US
dc.description.keywords en_US

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