Application of monoclonal antibody libraries for the measurement of glycation adducts.
Immunological approaches have been used to demonstrate the presence of advanced glycation end-products (AGEs) in several human and experimental animal tissues. We previously prepared polyclonal and monoclonal anti-AGE antibodies by immunizing AGE-modified proteins such as BSA and RNase. Although these antibodies contributed to demonstrate the presence of AGE-modified protein in vivo, the epitope structure of these antibodies had not been identified. We subsequently prepared several antibodies against AGE structures such as pentosidine, pyrraline, 3-deoxyglucosone imidazolone and N epsilon-(carboxyethyl)lysine by immunizing single AGE structures. These structure-specific antibodies have greatly helped broaden our understanding of AGE structures in aging and age-enhanced disease process. Monoclonal anti-AGE antibody is also used for the identification of major AGE structures in some pathological tissues, such as human atherosclerosis lesions. Based on the strategy, we successfully identified a novel AGE structure named glycolaldehyde-pyridine, which is the major antigenic AGE derived from glycolaldehyde. Therefore a monoclonal antibody library for AGE structures has served an important role in the elucidation of the biological significance of AGE.
Nagai
R
R
Department of Medical Biochemistry, Graduate School of Medical and Pharmaceutical Sciences, Kumamoto University, Honjo 1-1-1, Kumamoto 860-8556, Japan.
Horiuchi
S
S
Unno
Y
Y
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry / Q000276:immunology*; D017127:Glycation End Products, Advanced / Q000276:immunology*; D051379:Mice; D008807:Mice, Inbred BALB C
D000911:Antibodies, Monoclonal; D017127:Glycation End Products, Advanced