Immunochemical approaches to AGE-structures: characterization of anti-AGE antibodies

J Immunol Methods. 1998 Jun 1;215(1-2):95-104. doi: 10.1016/s0022-1759(98)00064-7.

Abstract

Recent immunological approaches have greatly helped broaden our understanding of the biomedical significance of advanced glycation end products (AGEs) in aging and age-enhanced disease processes. Recently, Nepsilon-(carboxymethyl) lysine (CML), one of the glycoxidation products of AGEs, was demonstrated to be a major immunological epitope among AGEs. In the subsequent study, we characterized 13 different polyclonal anti-AGE antibodies and showed that these antibodies could be classified into three groups (Groups I, II and III). Group I was specific for CML and both Group II and Group III were specific for other epitopes (non-CML). Time-course study suggested that the epitope of Group II was formed earlier than that of Group III. In the present study, we prepared two monoclonal anti-AGE antibodies (2A2 and 3A3) whose epitope structures appeared to be closely related to Group III and Group II, respectively. The result indicates that AGE-proteins express at least two major non-CML epitopes.

MeSH terms

  • Animals
  • Antibodies / analysis*
  • Antibodies / immunology
  • Antibodies, Monoclonal / analysis
  • Antibodies, Monoclonal / immunology
  • Antibody Specificity
  • Cloning, Molecular
  • Enzyme-Linked Immunosorbent Assay
  • Epitopes / analysis
  • Glycation End Products, Advanced / analysis
  • Glycation End Products, Advanced / immunology*
  • Immunohistochemistry
  • Lysine / analogs & derivatives
  • Lysine / analysis
  • Lysine / immunology
  • Mice
  • Mice, Inbred BALB C

Substances

  • Antibodies
  • Antibodies, Monoclonal
  • Epitopes
  • Glycation End Products, Advanced
  • N(6)-carboxymethyllysine
  • Lysine