- About this Journal ·
- Abstracting and Indexing ·
- Advance Access ·
- Aims and Scope ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Volume 2013 (2013), Article ID 198065, 5 pages
Biochemical Studies on Methylglyoxal-Mediated Glycated Histones: Implications for Presence of Serum Antibodies against the Glycated Histones in Patients with Type 1 Diabetes Mellitus
1Department of Biochemistry, Institute of Medical Sciences, Banaras Hindu University, Varanasi 221005, India
2Department of Biochemistry, Universal College of Medical Sciences, Paklihawa Campus, Bhairawaha, Nepal
Received 17 June 2013; Accepted 17 July 2013
Academic Editors: K.-i. Isobe and J. Neira
Copyright © 2013 Nadeem A. Ansari and Debabrata Dash. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- J. W. Baynes and S. R. Thorpe, “Role of oxidative stress in diabetic complications: a new perspective on an old paradigm,” Diabetes, vol. 48, no. 1, pp. 1–9, 1997.
- J. W. Baynes and S. R. Thorpe, “Glycoxidation and lipoxidation in atherogenesis,” Free Radical Biology and Medicine, vol. 28, no. 12, pp. 1708–1716, 2000.
- M. J. Roberts, G. T. Wondrak, D. C. Laurean, M. K. Jacobson, and E. Jacobson, “DNA damage by carbonyl stress in human skin cells,” Mutation Research, vol. 522, no. 1-2, pp. 45–56, 2003.
- D. Cervantes-Laurean, M. J. Roberts, E. L. Jacobson, and M. K. Jacobson, “Nuclear proteasome activation and degradation of carboxymethylated histones in human keratinocytes following glyoxal treatment,” Free Radical Biology and Medicine, vol. 38, no. 6, pp. 786–795, 2005.
- A. Gugliucci and M. Bendayan, “Histones from diabetic rats contain increased levels of advanced glycation end products,” Biochemical and Biophysical Research Communications, vol. 212, no. 1, pp. 56–62, 1995.
- N. A. Ansari, M. Moinuddin, K. Alam, and A. Ali, “Preferential recognition of Amadori-rich lysine residues by serum antibodies in diabetes mellitus: role of protein glycation in the disease process,” Human Immunology, vol. 70, no. 6, pp. 417–424, 2009.
- S. Pashikanti, G. A. Boissonneault, and D. Cervantes-Laurean, “Ex vivo detection of histone H1 modified with advanced glycation end products,” Free Radical Biology and Medicine, vol. 50, no. 10, pp. 1410–1416, 2011.
- A. Gugliucci, D. H. M. Bastos, J. Schulze, and M. F. F. Souza, “Caffeic and chlorogenic acids in Ilex paraguariensis extracts are the main inhibitors of AGE generation by methylglyoxal in model proteins,” Fitoterapia, vol. 80, no. 6, pp. 339–344, 2009.
- A. Gugliucci and T. Menini, “The polyamines spermine and spermidine protect proteins from structural and functional damage by AGE precursors: a new role for old molecules?” Life Sciences, vol. 72, no. 23, pp. 2603–2616, 2003.
- R. Ali and K. Alam, “Evaluation of antibodies against oxygen free radical-modified DNA by ELISA,” in Methods in Molecular Biology: Oxidative Stress Biomarkers and Antioxidants Protocols, D. Armstrong, Ed., pp. 171–181, Humana Press, New Jersey, NJ, USA, 2002.
- H. Talasz, S. Wasserer, and B. Puschendorf, “Nonenzymatic glycation of histones in vitro and in vivo,” Journal of Cellular Biochemistry, vol. 85, no. 1, pp. 24–34, 2002.
- A. Schmitt, J. Schmitt, G. Münch, and J. Gasic-Milencovic, “Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics,” Analytical Biochemistry, vol. 338, no. 2, pp. 201–215, 2005.
- Z. Rasheed, L. Kumar, S. Abbas, I. Prasad, N. A. Ansari, and R. Ahmad, “Advanced glycation end-products (AGEs) damaged IgG, a target for circulating autoantibodies in patients with type 1 diabetes mellitus,” Open Glycoscience, vol. 2, pp. 1–8, 2009.
- Y. Choi and S. Lim, “Characterization of anti-advanced glycation end product antibodies to nonenzymatically lysine-derived and arginine-derived glycated products,” Journal of Immunoassay and Immunochemistry, vol. 30, no. 4, pp. 386–399, 2009.
- N. A. Ansari and Z. Rasheed, “Non-enzymatic glycation of proteins: from diabetes to cancer,” Biochemistry B, vol. 3, no. 4, pp. 335–342, 2009.
- N. A. Ansari, M. Moinuddin, and R. Ali, “Glycated lysine residues: a marker for non-enzymatic protein glycation in age-related diseases,” Disease Markers, vol. 30, no. 6, pp. 317–324, 2011.
- H. M. Sims, A. L. Birdwell, K. E. OReilley, A. Bwashi, and B. D. Wing, “Inhibition of protein glycation with varying concentrations of lysine,” The FASEB Journal, vol. 22, 1123. 15, 2008.
- A. Jafarnejad, S. Z. Bathaie, M. Nakhjavani, M. Z. Hassan, and S. Banasadegh, “The improvement effect of L-Lys as a chemical chaperone on STZ-induced diabetic rats, protein structure and function,” Diabetes/Metabolism Research and Reviews, vol. 24, no. 1, pp. 64–73, 2008.