Oxidation of lysine side-chains of elastin by the myeloperoxidase system and by stimulated human neutrophils

Robert A. Clark, Susan Szot, Marcia A. Williams, Herbert M. Kagan

Research output: Contribution to journalArticle

44 Scopus citations

Abstract

Exposure of [3H]-lysine labeled elastin to either purified myeloper-oxidase 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 systems oxidation was blocked by azide, cyanide or catalase, but not by β-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.

Original languageEnglish (US)
Pages (from-to)451-457
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume135
Issue number2
DOIs
StatePublished - Mar 13 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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