The myeloperoxidase system of human phagocytes generates Nepsilon-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation.

Anderson, M M; Requena, J R; Crowley, J R; Thorpe, S R; Heinecke, J W

Anderson, M M; Requena, J R; Crowley, J R; Thorpe, S R; Heinecke, J W.

Affiliation

Anderson MM; Departments of Medicine, Biochemistry and Biophysics, and Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

J Clin Invest ; 104(1): 103-13, 1999 Jul.

Article in En | MEDLINE | ID: mdl-10393704

Subject(s)

Inflammation/enzymology; Lysine/analogs & derivatives; Peroxidase/metabolism; Protein Processing, Post-Translational; Aldehydes/metabolism; Catalase/pharmacology; Cations; Cells, Cultured; Chelating Agents/pharmacology; Glycosylation; Humans; Hydrogen Peroxide/metabolism; Hypochlorous Acid/metabolism; Hypochlorous Acid/pharmacology; Inflammation/pathology; Lysine/biosynthesis; Maillard Reaction; Neutrophils/enzymology; Oxidation-Reduction; Ribonuclease, Pancreatic/drug effects; Serine/pharmacology; Sodium Azide/pharmacology

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Processing, Post-Translational / Peroxidase / Inflammation / Lysine Limits: Humans Language: En Journal: J Clin Invest Year: 1999 Document type: Article Affiliation country: United States Country of publication: United States

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