Peroxynitration of albumin creates binding site for autoantibodie | 54306
Journal of Clinical and Cellular Immunology

Journal of Clinical and Cellular Immunology
Open Access

ISSN: 2155-9899

+44 1223 790975

Peroxynitration of albumin creates binding site for autoantibodies in diabetes mellitus

6th International Conference and Expo on Immunology

October 24-26, 2016 Chicago, USA

Zarina Arif and Jamal Ahmad

Aligarh Muslim University, India

Posters & Accepted Abstracts: J Clin Cell Immunol

Abstract :

It has been suggested that stress can play a major role in the etiopathogenesis of numerous diseases including diabetes mellitus. Superoxide and nitric oxide are two such stressors produced during inflammation in high amount. They can combine to produce peroxynitrite anion (ONOO-) which is potent oxidizing and nitrating agent. Thus, its interaction with biomolecules can cause oxidation as well as nitration. In the present study, albumin was modified by peroxynitrite and structural changes have been studied by UV, fluorescence, CD and Congo red binding. Analysis of modified-albumin showed increased level of carbonyl, nitrotyrosine and dityrosine. Thiol content was significantly reduced in modified-HSA. Reduction of plasma antioxidant power has been reported in diabetes mellitus and under such conditions peroxynitrite may modify albumin. This may modify the antigenic properties of albumin. Subsequent processing of modified-albumin by immune cells may generate autoantibodies. Thus, peroxynitrite-modified-HSA was used as antigen for detecting autoantibodies in diabetes mellitus sera by ELISA. Peroxynitrite-modified-HSA was bound by the diabetic autoantibodies. The study demonstrates that peroxynitration can generate immunologically active epitope on HSA.

Biography :