Abstract
Introduction: Advanced glycation end-products (AGEs) are contributing factors to diabetes complications. The antigenic nature of AGEs established the theory of incessant accumulation of AG Es can incite an autoimmune response in a diabetic patient. Glycating agents like 3-deoxyglucosone are increased in diabetic patients, leading to the high formation of AGEs aggravating the pathophysiological conditions in diabetes. We aimed to study the immunogenicity of glycated histone HI protein and AGES (N-carboxymethyl-lysine and pentosidine) as well as detection of autoantibodies in the sera of type 2 diabetic subjects.
Materials and Methods: Female rabbits were injected with native HI and glycated-H1 to discern its immunogenicity. Diabetic subjects sera were also scanned for the detection of autoantibodies against glycated-H1 and AGES using immunochemical assay technique.
Results: Glycated-H1 was highly immunogenic, unlike the native analog. Diabetic sera showed 48% (72 of 150 samples) significantly strong binding with glycated-H1, further sera also showed 40% (60 of 150 samples), and 36% (54 of 150 samples) strong binding with CML, and pentosidine, respectively.
Conclusion: The findings support modified H1 as well AGEs are highly immunogenic in nature. The presence of autoantibodies against glycated-H1 and AGEs may be utilized in the assessment of diabetes or its complications.