Affiliations: Department of Biochemistry, J N Medical College, AMU,
Aligarh-02, India
Note: [] Corresponding author: Department of Biochemistry, Institute of
Medical Sciences, Banaras Hindu University, Varanasi-221005, India. Tel.: +91
9760228860; E-mail: anadeem1@rediffmail.com
Abstract: Nonenzymatic glycosylation or glycation of macromolecules,
especially proteins leading to their oxidation, play an important role in
diseases. Glycation of proteins primarily results in the formation of an early
stage and stable Amadori-lysine product which undergo further irreversible
chemical reactions to form advanced glycation endproducts (AGEs). This review
focuses these products in lysine rich proteins such as collagen and human serum
albumin for their role in aging and age-related diseases. Antigenic
characteristics of glycated lysine residues in proteins together with the
presence of serum autoantibodies to the glycated lysine products and
lysine-rich proteins in diabetes and arthritis patients indicates that these
modified lysine residues may be a novel biomarker for protein glycation in
aging and age-related diseases.
