Oxidation of lysine side-chains of elastin by the myeloperoxidase system and by stimulated human neutrophils.
Exposure of [3H]-lysine labeled elastin to either purified myeloperoxidase plus H2O2 and halides or human neutrophils plus phorbol myristate acetate resulted in oxidation of lysine side chains quantitated as 3H2O release. In both the enzyme and cell system oxidation was blocked by azide, cyanide or catalase, but not by beta-aminopropionitrile, an inhibitor of lysyl oxidase. Myeloperoxidase-deficient neutrophils were ineffective unless exogenous myeloperoxidase was added. These data provide a biochemical basis for inflammatory changes in connective tissue proteins mediated by oxidant secretory products of neutrophils.
D000818:Animals; D002474:Cell-Free System; D002712:Chlorides / Q000494:pharmacology; D004285:Dogs; D004549:Elastin / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D066298:In Vitro Techniques; D007454:Iodides / Q000494:pharmacology; D008239:Lysine / Q000378:metabolism*; D009504:Neutrophils / Q000187:drug effects / Q000378:metabolism*; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D002712:Chlorides; D007454:Iodides; D004549:Elastin; D006861:Hydrogen Peroxide; D009195:Peroxidase; D008239:Lysine; D013755:Tetradecanoylphorbol Acetate