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Oxidative Medicine and Cellular Longevity
Volume 2013 (2013), Article ID 403973, 8 pages
http://dx.doi.org/10.1155/2013/403973
Clinical Study

Protein Sulfhydryl Group Oxidation and Mixed-Disulfide Modifications in Stable and Unstable Human Carotid Plaques

1Dipartimento di Scienze Biomediche, Unviversità di Sassari, Via Muroni 25, 07100 Sassari, Italy
2Centro Cardiologico “F. Monzino”, IRCCS, 20138 Milano, Italy

Received 6 December 2012; Accepted 28 December 2012

Academic Editor: Sumitra Miriyala

Copyright © 2013 Antonio Junior Lepedda et al. 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. E. Lutgens, R. J. van Suylen, B. C. Faber et al., “Atherosclerotic plaque rupture: local or systemic process?” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 23, no. 12, pp. 2123–2130, 2003. View at Publisher · View at Google Scholar · View at Scopus
  2. C. M. Dollery and P. Libby, “Atherosclerosis and proteinase activation,” Cardiovascular Research, vol. 69, no. 3, pp. 625–635, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. M. Formato, M. Farina, R. Spirito et al., “Evidence for a proinflammatory and proteolytic environment in plaques from endarterectomy segments of human carotid arteries,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 24, no. 1, pp. 129–135, 2004. View at Publisher · View at Google Scholar · View at Scopus
  4. A. J. Lepedda, A. Cigliano, G. M. Cherchi et al., “A proteomic approach to differentiate histologically classified stable and unstable plaques from human carotid arteries,” Atherosclerosis, vol. 203, no. 1, pp. 112–118, 2009. View at Publisher · View at Google Scholar · View at Scopus
  5. D. Steinberg, “Low density lipoprotein oxidation and its pathobiological significance,” Journal of Biological Chemistry, vol. 272, no. 34, pp. 20963–20966, 1997. View at Publisher · View at Google Scholar · View at Scopus
  6. R. Stocker and J. F. Keaney, “Role of oxidative modifications in atherosclerosis,” Physiological Reviews, vol. 84, no. 4, pp. 1381–1478, 2004. View at Publisher · View at Google Scholar · View at Scopus
  7. P. Eaton, “Protein thiol oxidation in health and disease: techniques for measuring disulfides and related modifications in complex protein mixtures,” Free Radical Biology and Medicine, vol. 40, no. 11, pp. 1889–1899, 2006. View at Publisher · View at Google Scholar · View at Scopus
  8. P. Klatt and S. Lamas, “Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress,” European Journal of Biochemistry, vol. 267, no. 16, pp. 4928–4944, 2000. View at Publisher · View at Google Scholar · View at Scopus
  9. P. J. Hogg, “Disulfide bonds as switches for protein function,” Trends in Biochemical Sciences, vol. 28, no. 4, pp. 210–214, 2003. View at Publisher · View at Google Scholar · View at Scopus
  10. S. Biswas, A. S. Chida, and I. Rahman, “Redox modifications of protein-thiols: emerging roles in cell signaling,” Biochemical Pharmacology, vol. 71, no. 5, pp. 551–564, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. A. Bescond, T. Augier, C. Chareyre, D. Garçon, W. Hornebeck, and P. Charpiot, “Influence of homocysteine on matrix metalloproteinase-2: activation and activity,” Biochemical and Biophysical Research Communications, vol. 263, no. 2, pp. 498–503, 1999. View at Publisher · View at Google Scholar · View at Scopus
  12. T. Okamoto, T. Akaike, T. Sawa, Y. Miyamoto, A. Van der Vliet, and H. Maeda, “Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation,” Journal of Biological Chemistry, vol. 276, no. 31, pp. 29596–29602, 2001. View at Publisher · View at Google Scholar · View at Scopus
  13. A. Zinellu, S. Sotgia, L. Deiana, and C. Carru, “Quantification of thiol-containing amino acids linked by disulfides to LDL,” Clinical Chemistry, vol. 51, no. 3, pp. 658–660, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. A. Zinellu, E. Zinellu, S. Sotgia et al., “Factors affecting S-homocysteinylation of LDL apoprotein B,” Clinical Chemistry, vol. 52, no. 11, pp. 2054–2059, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. A. Zinellu, A. Lepedda Jr., S. Sotgia et al., “Evaluation of low molecular mass thiols content in carotid atherosclerotic plaques,” Clinical Biochemistry, vol. 42, no. 9, pp. 796–801, 2009. View at Publisher · View at Google Scholar · View at Scopus
  16. D. J. Bigelow and G. Inesi, “Frequency-domain fluorescence spectroscopy resolves the location of maleimide-directed spectroscopic probes within the tertiary structure of the Ca-ATPase of sarcoplasmic reticulum,” Biochemistry, vol. 30, no. 8, pp. 2113–2125, 1991. View at Scopus
  17. K. Sugamura and J. F. Keaney Jr., “Reactive oxygen species in cardiovascular disease,” Free Radical Biology and Medicine, vol. 51, no. 5, pp. 978–992, 2011. View at Publisher · View at Google Scholar
  18. C. Smith, M. J. Mitchinson, O. I. Aruoma, and B. Halliwell, “Stimulation of lipid peroxidation and hydroxyl-radical generation by the contents of human atherosclerotic lesions,” Biochemical Journal, vol. 286, no. 3, pp. 901–905, 1992. View at Scopus
  19. D. S. Leake and S. M. Rankin, “The oxidative modification of low-density lipoproteins by macrophages,” Biochemical Journal, vol. 270, no. 3, pp. 741–748, 1990. View at Scopus
  20. D. Lapenna, S. de Gioia, G. Ciofani et al., “Glutathione-related antioxidant defenses in human atherosclerotic plaques,” Circulation, vol. 97, no. 19, pp. 1930–1934, 1998. View at Scopus
  21. T. Peters, All about Albumin: Biochemistry, Genetics, and Medical Applications, Academic Press, San Diego, Calif, USA, 1996.
  22. Y. Ogasawara, Y. Mukai, T. Togawa, T. Suzuki, S. Tanabe, and K. Ishii, “Determination of plasma thiol bound to albumin using affinity chromatography and high-performance liquid chromatography with fluorescence detection: ratio of cysteinyl albumin as a possible biomarker of oxidative stress,” Journal of Chromatography B, vol. 845, no. 1, pp. 157–163, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. J. S. Stamler, O. Jaraki, J. Osborne et al., “Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 16, pp. 7674–7677, 1992. View at Scopus
  24. S. Carballal, B. Alvarez, L. Turell, H. Botti, B. A. Freeman, and R. Radi, “Sulfenic acid in human serum albumin,” Amino Acids, vol. 32, no. 4, pp. 543–551, 2007. View at Publisher · View at Google Scholar · View at Scopus
  25. G. Aldini, G. Vistoli, L. Regazzoni et al., “Albumin is the main nucleophilic target of human plasma: a protective role against pro-atherogenic electrophilic reactive carbonyl species?” Chemical Research in Toxicology, vol. 21, no. 4, pp. 824–835, 2008. View at Publisher · View at Google Scholar · View at Scopus
  26. A. Zinellu, A. Lepedda, S. Sotgia et al., “Albumin-bound low molecular weight thiols analysis in plasma and carotid plaques by CE,” Journal of Separation Science, vol. 33, no. 1, pp. 126–131, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. I. Dalle-Donne, D. Giustarini, R. Rossi, R. Colombo, and A. Milzani, “Reversible S-glutathionylation of Cys374 regulates actin filament formation by inducing structural changes in the actin molecule,” Free Radical Biology and Medicine, vol. 34, no. 1, pp. 23–32, 2003. View at Publisher · View at Google Scholar · View at Scopus
  28. I. Dalle-Donne, R. Rossi, D. Giustarini, R. Colombo, and A. Milzani, “Actin S-glutathionylation: evidence against a thiol-disulphide exchange mechanism,” Free Radical Biology and Medicine, vol. 35, no. 10, pp. 1185–1193, 2003. View at Publisher · View at Google Scholar · View at Scopus
  29. I. Wada, M. Kai, S. Imai, F. Sakane, and H. Kanoh, “Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin,” EMBO Journal, vol. 16, no. 17, pp. 5420–5432, 1997. View at Publisher · View at Google Scholar · View at Scopus
  30. B. Schmidt, L. Ho, and P. J. Hogg, “Allosteric disulfide bonds,” Biochemistry, vol. 45, no. 24, pp. 7429–7433, 2006. View at Publisher · View at Google Scholar · View at Scopus
  31. S. Hutchinson, R. T. Aplin, H. Webb et al., “Molecular effects of homocysteine on cbEGF domain structure: insights into the pathogenesis of homocystinuria,” Journal of Molecular Biology, vol. 346, no. 3, pp. 833–844, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. H. F. Gilbert, “Thiol/disulfide exchange equilibria and disulfide bond stability,” Methods in Enzymology, vol. 251, pp. 8–28, 1995. View at Publisher · View at Google Scholar · View at Scopus
  33. H. E. Van Wart and H. Birkedal-Hansen, “The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 14, pp. 5578–5582, 1990. View at Publisher · View at Google Scholar · View at Scopus
  34. S. Chakraborti, M. Mandal, S. Das, A. Mandal, and T. Chakraborti, “Regulation of matrix metalloproteinases: an overview,” Molecular and Cellular Biochemistry, vol. 253, no. 1-2, pp. 269–285, 2003. View at Publisher · View at Google Scholar · View at Scopus