alexa Relevance of Nitroxidation of Albumin in Rheumatoid Arthritis: A Biochemical and Clinical Study | OMICS International | Abstract
ISSN: 2155-9899

Journal of Clinical & Cellular Immunology
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Research Article

Relevance of Nitroxidation of Albumin in Rheumatoid Arthritis: A Biochemical and Clinical Study

Zarina Arif1*, Mir Yasir Arfat2, Jamal Ahmad1, Asif Zaman2, Shireen Naaz Islam2 and M Asad Khan3
1Rajiv Gandhi Centre for Diabetes and Endocrinology, Faculty of Medicine, Aligarh Muslim University, Aligarh 202002, U.P., India
2Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University, Aligarh-202002 (U.P.), India
3Department of Biosciences, Jamia Millia Islamia, New Delhi-110025, India
Corresponding Author : Dr. Zarina Arif, Ph.D
Rajiv Gandhi Centre for Diabetes and Endocrinology
Faculty of Medicine, Aligarh Muslim University
Aligarh 202002, U.P, India
Tel: +91-571-2720030
E-mail: [email protected]
Received March 12, 2015; Accepted April 27, 2015; Published April 29, 2015
Citation: Arif Z, Arfat MY, Ahmad J, Zaman A, Islam SN, et al.x (2015) Relevance of Nitroxidation of Albumin in Rheumatoid Arthritis: A Biochemical and Clinical Study. J Clin Cell Immunol 6:324. doi: 10.4172/2155-9899.1000324.
Copyright: © 2015 Arif Z et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Abstract

Objective: To study the role of peroxynitrite-modified human serum albumin (nitroxidized-albumin) in rheumatoid arthritis. Methods: Human serum albumin was exposed to peroxynitrite and changes in albumin structure were monitored by UV-visible, fluorescence and circular dichroism spectroscopy, thioflavin T, Congo red binding and attenuated total reflection-Fourier transformed infrared spectroscopy (ATR-FTIR). Antioxidant properties of nitroxidized-albumin were evaluated by free radical induced RBC hemolysis test. Markers of protein oxidation like carbonyl, thiol, dityrosine and RBC hemolysis were evaluated in RA patients’ sera. Binding of autoantibodies in RA sera (n=50) with nitroxidized-albumin was studied by direct binding, inhibition ELISA and electrophoretic mobility shift gel assay. Results: The nitroxidized-albumin indicated the generation of nitrotyrosine, nitrotryptophan, carbonyl, dityrosine and reduction in tyrosine and tryptophan fluorescence and α-helicity. Fluorescence emission intensities of thioflavin T and Congo red got augmented upon binding with nitroxidized-albumin. Furthermore, secondary and tertiary structures of nitroxidized-albumin were altered as evident by ATR- FTIR, far and near-UV CD. Autoantibodies in RA sera (or IgG purified from sera) showed enhanced binding with nitroxidized-albumin as determined by direct binding and inhibition ELISA. Protein carbonyls, dityrosine and RBC hemolysis were significantly high, but thiol was significantly low in RA sera compared to age- and sex- matched control. Conclusion: Endogenously available peroxynitrite can nitrate and oxidize albumin, leading to protein nitration/ oxidation and subsequent formation of crosslinks, aggregates and immunogenic nitroxidized-albumin. Therefore, nitroxidized-albumin may be a potential trigger for autoantibodies in RA patients.

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