Identification of N epsilon-(carboxyethyl)lysine, one of the methylglyoxal-derived AGE structures, in glucose-modified protein: mechanism for protein modification by reactive aldehydes

J Chromatogr B Analyt Technol Biomed Life Sci. 2003 May 5;788(1):75-84. doi: 10.1016/s1570-0232(02)01019-x.

Abstract

We have developed a separation system for N(epsilon)-(carboxyethyl)lysine (CEL) and N(epsilon)-(carboxymethyl)lysine (CML) by HPLC equipped with a styrene-divinylbenzene copolymer resin coupled with sulfonic group cation-exchange column and examined whether CEL is formed from proteins modified by glucose via the Maillard reaction. CEL was generated by incubating bovine serum albumin (BSA) with glucose, a reaction inhibited by aminoguanidine, but enhanced by phosphate. Although several aldehydes were detected during incubation of N(alpha)-acetyllysine with glucose, incubation of BSA with methylglyoxal alone generated CEL. These results indicate that methylglyoxal is responsible for CEL formation on protein in vitro.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehydes / chemistry*
  • Chromatography, High Pressure Liquid
  • Glucose / chemistry*
  • Glycation End Products, Advanced / chemistry*
  • Lysine / analogs & derivatives*
  • Lysine / analysis*
  • Maillard Reaction
  • Pyruvaldehyde / chemistry*
  • Serum Albumin, Bovine / chemistry*

Substances

  • Aldehydes
  • Glycation End Products, Advanced
  • Serum Albumin, Bovine
  • N(6)-(1-carboxyethyl)lysine
  • Pyruvaldehyde
  • Glucose
  • Lysine