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BioMed Research International
Volume 2014, Article ID 623509, 9 pages
http://dx.doi.org/10.1155/2014/623509
Research Article

Preparation of Naringenin/β-Cyclodextrin Complex and Its More Potent Alleviative Effect on Choroidal Neovascularization in Rats

1Department of Ophthalmology, Affiliated Hospital of Nanjing University of Traditional Chinese Medicine, 155 Hanzhong Road, Nanjing 210029, China
2College of Pharmacy, Nanjing University of Traditional Chinese Medicine, Nanjing 210023, China
3Department of Clinical Laboratory, Affiliated Hospital of Nanjing University of Traditional Chinese Medicine, Nanjing 210029, China

Received 28 December 2013; Accepted 11 February 2014; Published 27 March 2014

Academic Editor: Kota V. Ramana

Copyright © 2014 Xin-rong Xu 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. M. Lu and A. P. Adamis, “Molecular biology of choroidal neovascularization,” Ophthalmology Clinics of North America, vol. 19, no. 3, pp. 323–334, 2006. View at Publisher · View at Google Scholar · View at Scopus
  2. D. G. Miller and L. J. Singerman, “Vision loss in younger patients: a review of choroidal neovascularization,” Optometry and Vision Science, vol. 83, no. 5, pp. 316–325, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. E. W. Ng and A. P. Adamis, “Targeting angiogenesis, the underlying disorder in neovascular age-related macular degeneration,” Canadian Journal of Ophthalmology, vol. 40, no. 3, pp. 352–368, 2005. View at Google Scholar · View at Scopus
  4. N. Ferrara, “Vascular endothelial growth factor: basic science and clinical progress,” Endocrine Reviews, vol. 25, no. 4, pp. 581–611, 2004. View at Publisher · View at Google Scholar · View at Scopus
  5. E. S. Gragoudas, A. P. Adamis, E. T. Cunningham Jr., M. Feinsod, and D. R. Guyer, “Pegaptanib for neovascular age-related macular degeneration,” The New England Journal of Medicine, vol. 351, no. 27, pp. 2805–2816, 2004. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Michels, P. J. Rosenfeld, C. A. Puliafito, E. N. Marcus, and A. S. Venkatraman, “Systemic bevacizumab (Avastin) therapy for neovascular age-related macular degeneration: twelve-week results of an uncontrolled open-label clinical study,” Ophthalmology, vol. 112, no. 6, pp. 1035–1047, 2005. View at Publisher · View at Google Scholar · View at Scopus
  7. P. J. Rosenfeld, A. A. Moshfeghi, and C. A. Puliafito, “Optical coherence tomography findings after an intravitreal injection of bevacizumab (Avastin) for neovascular age-related macular degeneration,” Ophthalmic Surgery, Lasers & Imaging, vol. 36, no. 4, pp. 331–335, 2005. View at Google Scholar · View at Scopus
  8. Y. Shen, W. Y. Zhang, and G. C. Chiou, “Effect of naringenin on NaIO3-induced retinal pigment epithelium degeneration and laser-induced choroidal neovascularization in rats,” International Journal of Ophthalmology, vol. 3, no. 1, pp. 5–8, 2010. View at Publisher · View at Google Scholar · View at Scopus
  9. K. Uekama, “Design and evaluation of cyclodextrin-based drug formulation,” Chemical and Pharmaceutical Bulletin, vol. 52, no. 8, pp. 900–915, 2004. View at Publisher · View at Google Scholar · View at Scopus
  10. M. D. Moya-Ortega, C. Alvarez-Lorenzo, A. Concheiro, and T. Loftsson, “Cyclodextrin-based nanogels for pharmaceutical and biomedical applications,” International Journal of Pharmaceutics, vol. 428, no. 1-2, pp. 152–163, 2012. View at Publisher · View at Google Scholar · View at Scopus
  11. D. R. Luke, K. Tomaszewski, B. Damle, and H. T. Schlamm, “Review of the basic and clinical pharmacology of sulfobutylether-β- cyclodextrin (SBECD),” Journal of Pharmaceutical Sciences, vol. 99, no. 8, pp. 3291–3301, 2010. View at Publisher · View at Google Scholar · View at Scopus
  12. S. R. Singh, H. E. Grossniklaus, S. J. Kang, H. F. Edelhauser, B. K. Ambati, and U. B. Kompella, “Intravenous transferrin, RGD peptide and dual-targeted nanoparticles enhance anti-VEGF intraceptor gene delivery to laser-induced CNV,” Gene Therapy, vol. 16, no. 5, pp. 645–659, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. Y. Fu, S. Zheng, J. Lin, J. Ryerse, and A. Chen, “Curcumin protects the rat liver from CCl4-caused injury and fibrogenesis by attenuating oxidative stress and suppressing inflammation,” Molecular Pharmacology, vol. 73, no. 2, pp. 399–409, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. T. D. Schmittgen, B. A. Zakrajsek, A. G. Mills, V. Gorn, M. J. Singer, and M. W. Reed, “Quantitative reverse transcription-polymerase chain reaction to study mRNA decay: comparison of endpoint and real-time methods,” Analytical Biochemistry, vol. 285, no. 2, pp. 194–204, 2000. View at Publisher · View at Google Scholar · View at Scopus
  15. “Subfoveal neovascular lesions in age-related macular degeneration. Guidelines for evaluation and treatment in the macular photocoagulation study. Macular Photocoagulation Study Group,” Archives of Ophthalmology, vol. 109, no. 9, pp. 1242–1257, 1991. View at Scopus
  16. M. Caputo, H. Zirpoli, R. di Benedetto, K. de Nadai, and M. F. Tecce, “Perspectives of choroidal neovascularization therapy,” Current Drug Targets, vol. 12, no. 2, pp. 234–242, 2011. View at Google Scholar · View at Scopus
  17. J. Wang, Z. Yang, L. Lin, Z. Zhao, Z. Liu, and X. Liu, “Protective effect of naringenin against lead-induced oxidative stress in rats,” Biological Trace Element Research, vol. 146, no. 3, pp. 354–359, 2012. View at Publisher · View at Google Scholar · View at Scopus
  18. J. Ji, X. Xu, and C. Y. Chiou, “Effects of naringenin on ocular blood flow and choroidal neovascularization in experimental animals,” International Journal of Ophthalmology, vol. 2, no. 4, pp. 320–323, 2009. View at Google Scholar · View at Scopus
  19. S. L. Schreiber, “Target-oriented and diversity-oriented organic synthesis in drug discovery,” Science, vol. 287, no. 5460, pp. 1964–1969, 2000. View at Publisher · View at Google Scholar · View at Scopus
  20. P. Purkayastha, S. S. Jaffer, and P. Ghosh, “Physicochemical perspective of cyclodextrin nano and microaggregates,” Physical Chemistry Chemical Physics, vol. 14, no. 16, pp. 5339–5348, 2012. View at Publisher · View at Google Scholar · View at Scopus
  21. Y. Zhang and Y. Cui, “Influence of 2-hydroxypropyl-β-cyclodextrin complexation on P-glycoprotein drug pump in the intestine of rats,” Chinese Pharmacological Bulletin, vol. 24, no. 10, pp. 1318–1323, 2008. View at Google Scholar · View at Scopus
  22. M. Shulman, M. Cohen, A. Soto-Gutierrez et al., “Enhancement of naringenin bioavailability by complexation with hydroxypropoyl-β-cyclodextrin,” PLoS ONE, vol. 6, no. 4, Article ID e18033, 2011. View at Publisher · View at Google Scholar · View at Scopus
  23. D. Bok, “Evidence for an inflammatory process in age-related macular degeneration gains new support,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 20, pp. 7053–7054, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. M. R. Castro, D. Lutz, and J. L. Edelman, “Effect of COX inhibitors on VEGF-induced retinal vascular leakage and experimental corneal and choroidal neovascularization,” Experimental Eye Research, vol. 79, no. 2, pp. 275–285, 2004. View at Publisher · View at Google Scholar · View at Scopus
  25. T. Kuwano, S. Nakao, H. Yamamoto et al., “Cyclooxygenase 2 is a key enzyme for inflammatory cytokine-induced angiogenesis,” The FASEB Journal, vol. 18, no. 2, pp. 300–310, 2004. View at Publisher · View at Google Scholar · View at Scopus
  26. T. L. Larkins, M. Nowell, S. Singh, and G. L. Sanford, “Inhibition of cyclooxygenase-2 decreases breast cancer cell motility, invasion and matrix metalloproteinase expression,” BMC Cancer, vol. 6, article 181, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. C. Costa and E. Hirsch, “More than just kinases: the scaffolding function of PI3K,” Current Topics in Microbiology and Immunology, vol. 346, pp. 171–181, 2011. View at Publisher · View at Google Scholar · View at Scopus
  28. P. Huang, J. Han, and L. Hui, “MAPK signaling in inflammation-associated cancer development,” Protein & Cell, vol. 1, no. 3, pp. 218–226, 2010. View at Publisher · View at Google Scholar · View at Scopus
  29. D. Colleselli, K. Bijuklic, B. A. Mosheimer, and C. M. Kähler, “Inhibition of cyclooxygenase (COX)-2 affects endothelial progenitor cell proliferation,” Experimental Cell Research, vol. 312, no. 15, pp. 2933–2941, 2006. View at Publisher · View at Google Scholar · View at Scopus
  30. H. Y. Yong, M. S. Koh, and A. Moon, “The p38 MAPK inhibitors for the treatment of inflammatory diseases and cancer,” Expert Opinion on Investigational Drugs, vol. 18, no. 12, pp. 1893–1905, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. C. C. Lin, H. L. Hsieh, R. H. Shih, P. L. Chi, S. E. Cheng, and C. M. Yang, “Up-regulation of COX-2/PGE2 by endothelin-1 via MAPK-dependent NF-κB pathway in mouse brain microvascular endothelial cells,” Cell Communication and Signaling, vol. 11, no. 1, article 8, 2013. View at Publisher · View at Google Scholar
  32. Z. Guan, S. Y. Buckman, B. W. Miller, L. D. Springer, and A. R. Morrison, “Interleukin-1β-induced cyclooxygenase-2 expression requires activation of both c-Jun NH2-terminal kinase and p38 MAPK signal pathways in rat renal mesangial cells,” Journal of Biological Chemistry, vol. 273, no. 44, pp. 28670–28676, 1998. View at Publisher · View at Google Scholar · View at Scopus