Journal of Clinical and Cellular Immunology
Open Access
ISSN: 2155-9899
ISSN: 2155-9899
Alok Raghav and Jamal Ahmad
Aligarh Muslim University, India
Posters & Accepted Abstracts: J Clin Cell Immunol
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 Γ?ΒΌM) 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-Γ?Β± and NF-ΓΒΊΓ?Β² 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-Γ?Β± were found significantly higher in subjects with CKD compared to T2DM and healthy. mRNA expression of IL-4, IL-6 and NF-ΓΒΊΓ?Β² 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