GET THE APP

Preferential recognition of advanced glycation end products by se | 57085
Journal of Clinical and Cellular Immunology

Journal of Clinical and Cellular Immunology
Open Access

ISSN: 2155-9899

Preferential recognition of advanced glycation end products by serum antibodies in diabetes mellitus


World Immunology Congress

DECEMBER 14-15, 2017 DUBAI, UAE

Alok Raghav and Jamal Ahmad

Aligarh Muslim University, India

Posters & Accepted Abstracts: J Clin Cell Immunol

Abstract :

This study analyses the detrimental effect of non-enzymatic glycation on human serum albumin (HSA) leading to the production of advanced glycation end products (AGEs). HSA (20 ?¼M) incubated with glucose (400 mg/dL) formed AGEs confirmed by scanning electron microscopy. DNA-damage in subjects with diabetes mellitus was assessed with comet assay. Antibodies against in vitro formed AGEs were evaluated in the sera of diabetic patients by enzyme-linked immune-sorbent assay, Molecular docking to demonstrate affinity of native and glycosylated HSA with IgG. Low-grade systemic inflammation was quantified with IL-4, IL-6, TNF-?± and NF-к?² in serum and mRNA expression. The SEM showed the formation of aggregates in glycated-HSA. Serum auto-antibodies from diabetes patients with chronic kidney disease (CKD) showed appreciably high recognition of glycated-HSA compared to native HSA. Comet showed severe DNA damage in subjects with CKD compared to healthy. Molecular docking showed less affinity of glycosylated-HSA with IgG compared to native-HSA. Serum IL-4, IL-6 and TNF-?± were found significantly higher in subjects with CKD compared to T2DM and healthy. mRNA expression of IL-4, IL-6 and NF-к?² are also found significantly higher in CKD. The non-enzymatic glycation-induced damage to the HSA and generate neo-epitopes that possess immunogenic response and low-grade systemic inflammation. alokalig@gmail.com

Top globaltechsummit