Table of Contents
Journal of Biomarkers
Volume 2013, Article ID 430813, 7 pages
http://dx.doi.org/10.1155/2013/430813
Research Article

Glucose-6-Phosphate Dehydrogenase Activity and Protein Oxidative Modification in Patients with Type 2 Diabetes Mellitus

1Biochemistry Department, Faculty of Medicine, Sohag University, Sohag, Egypt
2Internal Medicine Department, Faculty of Medicine, Sohag University, Sohag, Egypt

Received 23 August 2013; Revised 24 October 2013; Accepted 20 November 2013

Academic Editor: Philip Thomas

Copyright © 2013 Aida A. Mahmoud and Amal K. A. Nor El-Din. 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.

Linked References

  1. American Diabetes Association, “Diagnosis and classification of diabetes mellitus,” Diabetes Care, vol. 33, supplement 1, pp. S62–S69, 2010. View at Google Scholar
  2. T. V. Fiorentino, A. Prioletta, P. Zuo, and F. Folli, “Hyperglycemia-induced oxidative stress and its role in diabetes mellitus related cardiovascular diseases,” Current Pharmaceutical Design, vol. 19, no. 32, pp. 5695–5703, 2013. View at Google Scholar
  3. W. M. Frederiks, K. S. Bosch, J. S. S. G. De Jong, and C. J. F. Van Noorden, “Post-translational regulation of glucose-6-phosphate dehydrogenase activity in (pre)neoplastic lesions in rat liver,” Journal of Histochemistry & Cytochemistry, vol. 51, no. 1, pp. 105–112, 2003. View at Google Scholar · View at Scopus
  4. R. C. Stanton, “Glucose-6-phosphate dehydrogenase, NADPH, and cell survival,” IUBMB Life, vol. 64, no. 5, pp. 362–369, 2012. View at Publisher · View at Google Scholar · View at Scopus
  5. K. Winzer, C. J. F. Van Noorden, and A. Köhler, “Quantitative cytochemical analysis of glucose-6-phosphate dehydrogenase activity in living isolated hepatocytes of European flounder for rapid analysis of xenobiotic effects,” Journal of Histochemistry and Cytochemistry, vol. 49, no. 8, pp. 1025–1032, 2001. View at Google Scholar · View at Scopus
  6. Y. Xu, B. W. Osborne, and R. C. Stanton, “Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex,” American Journal of Physiology—Renal Physiology, vol. 289, no. 5, pp. F1040–F1047, 2005. View at Publisher · View at Google Scholar · View at Scopus
  7. I. Dalle-Donne, D. Giustarini, R. Colombo, R. Rossi, and A. Milzani, “Protein carbonylation in human diseases,” Trends in Molecular Medicine, vol. 9, no. 4, pp. 169–176, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. R. Rossi, D. Giustarini, A. Milzani, and I. Dalle-Donne, “Cysteinylation and homocysteinylation of plasma protein thiols during ageing of healthy human beings,” Journal of Cellular and Molecular Medicine, vol. 13, no. 9, pp. 3131–3140, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. M. E. Sitar, S. Aydin, and U. Çakatay, “Human serum albumin and its relation with oxidative stress,” Clinical Laboratory, vol. 59, no. 9-10, pp. 945–952, 2013. View at Google Scholar
  10. U. Çakatay, “Pro-oxidant actions of α-lipoic acid and dihydrolipoic acid,” Medical Hypotheses, vol. 66, no. 1, pp. 110–117, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. Expert Committee on the Diagnosis and Classification of Diabetes Mellitus, “Report of the Expert Committee on the Diagnosis and Classification of Diabetes Mellitus,” Diabetes Care, vol. 20, no. 7, pp. 1183–1197, 1997. View at Google Scholar · View at Scopus
  12. W.-N. Tian, L. D. Braunstein, J. Pang et al., “Importance of glucose-6-phosphate dehydrogenase activity for cell growth,” The Journal of Biological Chemistry, vol. 273, no. 17, pp. 10609–10617, 1998. View at Publisher · View at Google Scholar · View at Scopus
  13. A. Z. Reznick and L. Packer, “Oxidative damage to proteins: spectrophotometric method for carbonyl assay,” Methods in Enzymology, vol. 233, pp. 357–363, 1994. View at Publisher · View at Google Scholar · View at Scopus
  14. M.-L. Hu, “Measurement of protein thiol groups and glutathione in plasma,” Methods in Enzymology, vol. 233, pp. 380–385, 1994. View at Publisher · View at Google Scholar · View at Scopus
  15. Z. Zang, K. Apse, J. Pang, and R. C. Stanton, “High glucose inhibits glucose-6-phosphate dehydrogenase via cAMP in aortic endothelial cells,” The Journal of Biological Chemistry, vol. 275, no. 51, pp. 40042–40047, 2000. View at Publisher · View at Google Scholar · View at Scopus
  16. Y. Xu, B. W. Osborne, and R. C. Stanton, “Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex,” American Journal of Physiology—Renal Physiology, vol. 289, no. 5, pp. F1040–F1047, 2005. View at Publisher · View at Google Scholar · View at Scopus
  17. Z. Zhang, C. W. Liew, D. E. Handy et al., “High glucose inhibits glucose-6-phosphate dehydrogenase, leading to increased oxidative stress and β-cell apoptosis,” FASEB Journal, vol. 24, no. 5, pp. 1497–1505, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. Z. Zhang, Z. Yang, B. Zhu et al., “Increasing glucose 6-phosphate dehydrogenase activity restores redox balance in vascular endothelial cells exposed to high glucose,” PLoS One, vol. 7, no. 11, Article ID e49128, 2012. View at Google Scholar
  19. F. Giacco, M. Brownlee, and A. M. Schmidt, “Oxidative stress and diabetic complications,” Circulation Research, vol. 107, no. 9, pp. 1058–1070, 2010. View at Publisher · View at Google Scholar · View at Scopus
  20. E. Wright Jr., J. L. Scism-Bacon, and L. C. Glass, “Oxidative stress in type 2 diabetes: the role of fasting and postprandial glycaemia,” International Journal of Clinical Practice, vol. 60, no. 3, pp. 308–314, 2006. View at Publisher · View at Google Scholar · View at Scopus
  21. M. Arif, M. R. Islam, T. M. Z. Waise, F. Hassan, S. I. Mondal, and Y. Kabir, “DNA damage and plasma antioxidant indices in Bangladeshi type 2 diabetic patients,” Diabetes & Metabolism, vol. 36, no. 1, pp. 51–57, 2010. View at Publisher · View at Google Scholar · View at Scopus
  22. U. Çakatay, “Protein oxidation parameters in type 2 diabetic patients with good and poor glycaemic control,” Diabetes & Metabolism, vol. 31, no. 6, pp. 551–557, 2005. View at Publisher · View at Google Scholar · View at Scopus
  23. E. R. Stadtman and R. L. Levine, “Free radical-mediated oxidation of free amino acids and amino acid residues in proteins,” Amino Acids, vol. 25, no. 3-4, pp. 207–218, 2003. View at Publisher · View at Google Scholar · View at Scopus
  24. A. Telci, U. Çakatay, R. Kayali et al., “Oxidative protein damage in plasma of type 2 diabetic patients,” Hormone and Metabolic Research, vol. 32, pp. 40–43, 2000. View at Google Scholar
  25. P. Atukeren, S. Aydin, E. Uslu, M. K. Gumustas, and U. Cakatay, “Redox homeostasis of albumin in relation to alpha-lipoic acid and dihydrolipoic acid,” Oxidative Medicine and Cellular Longevity, vol. 3, no. 3, pp. 206–213, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. D. A. Butterfield, T. Koppal, B. Howard et al., “Structural and functional changes in proteins induced by free radical-mediated oxidative stress and protective action of the antioxidants N-tert-butyl-α-phenylnitrone and vitamin E,” Annals of the New York Academy of Sciences, vol. 854, pp. 448–462, 1998. View at Publisher · View at Google Scholar · View at Scopus
  27. A. Van Campenhout, C. Van Campenhout, A. R. Lagrou et al., “Impact of diabetes mellitus on the relationships between iron-, inflammatory- and oxidative stress status,” Diabetes/Metabolism Research and Reviews, vol. 22, no. 6, pp. 444–454, 2006. View at Publisher · View at Google Scholar · View at Scopus
  28. J. K. Shetty, M. Prakash, and M. S. Ibrahim, “Relationship between free iron and glycated hemoglobin in uncontrolled type 2 diabetes patients associated with complications,” Indian Journal of Clinical Biochemistry, vol. 23, no. 1, pp. 67–70, 2008. View at Publisher · View at Google Scholar · View at Scopus
  29. J. Zeng and M. J. Davies, “Protein and low molecular mass thiols as targets and inhibitors of glycation reactions,” Chemical Research in Toxicology, vol. 19, no. 12, pp. 1668–1676, 2006. View at Publisher · View at Google Scholar · View at Scopus