title: Advanced glycation end products of the Maillard reaction and their relation to aging.
abstract: Long-term incubation of proteins with glucose leads to advanced glycation end products (AGE). Demonstration of AGE in vivo as well as determination of its main structure are crucial to elucidate its potential link to aging processes and diabetic complications. We prepared polyclonal and monoclonal anti-AGE antibodies and used them to identify and quantitate AGE in human lens proteins. Results suggest that there occurs a common AGE structure and provide the direct evidence for the presence of AGE in human lens crystallins and its age-related increase.
authors.affiliation: Department of Biochemistry, Kumamoto University School of Medicine, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Horiuchi
authors.forename: N
authors.initials: N
authors.lastname: Araki
mesh_terms: D000375:Aging / Q000502:physiology*; D004797:Enzyme-Linked Immunosorbent Assay; D017127:Glycation End Products, Advanced / Q000032:analysis* / Q000096:biosynthesis; D006801:Humans; D015151:Immunoblotting; D007908:Lens, Crystalline / Q000737:chemistry* / Q000378:metabolism; D015416:Maillard Reaction
chemical_list: D017127:Glycation End Products, Advanced