Hypochlorous acid generates N epsilon-(carboxymethyl)lysine from Amadori products.

Abstract

Since the accumulation of N(epsilon)-(carboxymethyl)lysine (CML), a major antigenic advanced glycation end product, is implicated in tissue disorders in hyperglycemia and inflammation, the identification of the pathway of CML formation will provide important information regarding the development of potential therapeutic strategies for these complications. The present study was designed to measure the effect of hypochlorous acid (HOCl) on CML formation from Amadori products. The incubation of glycated human serum albumin (glycated-HSA), a model of Amadori products, with HOCl led to CML formation, and an increasing HOCl concentration and decreasing pH, which mimics the formation of these products in inflammatory lesions. CML formation was also observed when glycated-HSA was incubated with activated neutrophils, and was completely inhibited in the presence of an HOCl scavenger. These data demonstrated that HOCl-mediated CML formation from Amadori products plays a role in CML formation and tissue damage at sites of inflammation.

• Authors: Katsumi Mera, Ryoji Nagai, Nozomu Haraguchi, Yukio Fujiwara, Tomohiro Araki, Noriyuki Sakata, Masaki Otagiri
• Journal: Free radical research (Free Radic Res) Vol. 41 Issue 6 Pg. 713-8 (Jun 2007) ISSN: 1071-5762 [Print] England
• PMID: 17516244 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Glycation End Products, Advanced
• Serum Albumin
• N(6)-carboxymethyllysine
• Hypochlorous Acid
• Acetaldehyde
• Lysine
• glycolaldehyde

Topics

• Acetaldehyde (analogs & derivatives, pharmacology)
• Chromatography, High Pressure Liquid
• Enzyme-Linked Immunosorbent Assay
• Glycation End Products, Advanced (metabolism)
• Humans
• Hydrogen-Ion Concentration
• Hypochlorous Acid (pharmacology)
• Lysine (analogs & derivatives, metabolism)
• Neutrophils (metabolism)
• Oxidation-Reduction
• Serum Albumin (metabolism)