Activation of Matrix Metalloproteinases by Peroxynitrite-induced Protein S-Glutathiolation via Disulfide S-Oxide Formation

Journal of Biological Chemistry

Volumn 276, Issue 31, 2001, Pages 29596-29602

  Okamoto, Tatsuya ^a,b   Akaike, Takaaki ^a   Sawa, Tomohiro ^a   Miyamoto, Yoichi ^a   Van der Vliet, Albert ^b   Maeda, Hiroshi ^a  

^a KUMAMOTO UNIV SCHOOL OF MEDICINE   (Japan)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

OXIDATION; PROTEINS; SULFUR COMPOUNDS; TISSUE;

DENATURATION; INFLAMMATION;

BIOCHEMISTRY;

CYSTEINE; DISULFIDE; DITHIOTHREITOL; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE DISULFIDE S OXIDE; MATRIX METALLOPROTEINASE; OXIDIZING AGENT; PEROXYNITRITE; PROCOLLAGENASE; PROTEIN PRECURSOR; S NITROGLUTATHIONE; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG; BOVINE SERUM ALBUMIN; COLLAGENASE; DRUG DERIVATIVE; ENZYME PRECURSOR; GELATINASE B; NITRATE; NITROSO DERIVATIVE; PEPTIDE FRAGMENT; PEROXYNITRIC ACID; PRO MATRIX METALLOPROTEINASE 9; PRO-MATRIX METALLOPROTEINASE 9; S NITROSOGLUTATHIONE; SULFUR; TRITIUM;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; HUMAN; HUMAN CELL; INFLAMMATION; ISOTOPE LABELING; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN DENATURATION; TISSUE INJURY; AMINO ACID SEQUENCE; BINDING SITE; CHEMISTRY; DRUG EFFECT; KINETICS; MASS SPECTROMETRY; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN PROCESSING;

AMINO ACID SEQUENCE; BINDING SITES; COLLAGENASES; DISULFIDES; ENZYME ACTIVATION; ENZYME PRECURSORS; GLUTATHIONE; HUMANS; KINETICS; MATRIX METALLOPROTEINASE 9; MATRIX METALLOPROTEINASES; NITRATES; NITROSO COMPOUNDS; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PROTEIN PROCESSING, POST-TRANSLATIONAL; S-NITROSOGLUTATHIONE; SERUM ALBUMIN, BOVINE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SULFUR RADIOISOTOPES; TRITIUM;

EID: 0035800858     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102417200     Document Type: Article

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