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Oxidative Medicine and Cellular Longevity
Volume 2016, Article ID 8902954, 9 pages
http://dx.doi.org/10.1155/2016/8902954
Research Article

Effects of Bauhinia forficata Tea on Oxidative Stress and Liver Damage in Diabetic Mice

1Programa de Pós-Graduação em Bioquímica, Universidade Federal do Pampa, Campus Uruguaiana, BR 472 Km 585, Caixa Postal 118, 97508-000 Uruguaiana, RS, Brazil
2Faculdade de Farmácia, Universidade Federal do Rio Grande do Sul, Avenida Ipiranga 2752, 90610-000 Porto Alegre, RS, Brazil
3Programa de Pós-Graduação em Ciências Biológicas, Universidade Federal do Pampa, Campus São Gabriel, Avenida Antônio Trilha 1847, Centro, 97300-000 São Gabriel, RS, Brazil
4Departamento de Morfologia, Universidade Federal de Santa Maria, Avenida Roraima 1000, Camobi, 97105-900 Santa Maria, RS, Brazil

Received 25 August 2015; Revised 9 October 2015; Accepted 11 October 2015

Academic Editor: Denis Delic

Copyright © 2016 Andréia Caroline Fernandes Salgueiro 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. Y. Pan, B. A. Abd-Rashid, Z. Ismail et al., “In vitro determination of the effect of Andrographis paniculata extracts and andrographolide on human hepatic cytochrome P450 activities,” Journal of Natural Medicines, vol. 65, no. 3-4, pp. 440–447, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. M. Trojan-Rodrigues, T. L. S. Alves, G. L. G. Soares, and M. R. Ritter, “Plants used as antidiabetics in popular medicine in Rio Grande do Sul, southern Brazil,” Journal of Ethnopharmacology, vol. 139, no. 1, pp. 155–163, 2012. View at Publisher · View at Google Scholar · View at Scopus
  3. V. Cechinel Filho, “Chemical composition and biological potential of plants from the genus Bauhinia,” Phytotherapy Research, vol. 23, no. 10, pp. 1347–1354, 2009. View at Publisher · View at Google Scholar · View at Scopus
  4. A. M. da Cunha, S. Menon, R. Menon, A. G. Couto, C. Bürger, and M. W. Biavatti, “Hypoglycemic activity of dried extracts of Bauhinia forficata Link,” Phytomedicine, vol. 17, no. 1, pp. 37–41, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. C. S. De Lino, J. P. L. Diógenes, B. A. Pereira et al., “Antidiabetic activity of Bauhinia forficata extracts in alloxan-diabetic rats,” Biological and Pharmaceutical Bulletin, vol. 27, no. 1, pp. 125–127, 2004. View at Publisher · View at Google Scholar · View at Scopus
  6. E. R. Almeida, M. C. Guedes, J. F. C. Albuquerque, and H. Xavier, “Hypoglycemic effect of Bauhinia cheilandra in rats,” Fitoterapia, vol. 77, no. 4, pp. 276–278, 2006. View at Publisher · View at Google Scholar · View at Scopus
  7. D. C. Damasceno, G. T. Volpato, I. De Mattos Paranhos Calderon, R. Aguilar, and M. V. C. Rudge, “Effect of Bauhinia forficata extract in diabetic pregnant rats: maternal repercussions,” Phytomedicine, vol. 11, no. 2-3, pp. 196–201, 2004. View at Publisher · View at Google Scholar · View at Scopus
  8. M. Gupta, U. K. Mazumder, T. S. Kumar et al., “Antioxidant and hepatoprotective effects of Bauhinia racemosa against paracetamol and carbon tetra-chloride induced liver damage in rats,” Iranian Journal of Pharmacology & Therapeutics, vol. 3, pp. 12–20, 2004. View at Google Scholar
  9. S. H. Bodakhe and A. Ram, “Hepatoprotective properties of Bauhinia variegata bark extract,” Yakugaku Zasshi, vol. 127, no. 9, pp. 1503–1507, 2007. View at Publisher · View at Google Scholar · View at Scopus
  10. E. de Sousa, L. Zanatta, I. Seifriz et al., “Hypoglycemic effect and antioxidant potential of kaempferol-3,7-O-(α)-dirhamnoside from Bauhinia forficata leaves,” Journal of Natural Products, vol. 67, no. 5, pp. 829–832, 2004. View at Publisher · View at Google Scholar · View at Scopus
  11. A. C. F. Salgueiro, C. Q. Leal, M. C. Bianchini et al., “The influence of Bauhinia forficata Link subsp. pruinosa tea on lipid peroxidation and non-protein SH groups in human erythrocytes exposed to high glucose concentrations,” Journal of Ethnopharmacology, vol. 148, no. 1, pp. 81–87, 2013. View at Publisher · View at Google Scholar · View at Scopus
  12. A. C. Maritim, R. A. Sanders, and J. B. Watkins III, “Diabetes, oxidative stress, and antioxidants: a review,” Journal of Biochemical and Molecular Toxicology, vol. 17, no. 1, pp. 24–38, 2003. View at Publisher · View at Google Scholar · View at Scopus
  13. V. Folmer, J. C. M. Soares, D. Gabriel, and J. B. T. Rocha, “A high fat diet inhibits δ-aminolevulinate dehydratase and increases lipid peroxidation in mice (Mus musculus),” The Journal of Nutrition, vol. 133, no. 7, pp. 2165–2170, 2003. View at Google Scholar · View at Scopus
  14. V. Folmer, J. C. M. Soares, and J. B. T. Rocha, “Oxidative stress in mice is dependent on the free glucose content of the diet,” International Journal of Biochemistry and Cell Biology, vol. 34, no. 10, pp. 1279–1285, 2002. View at Publisher · View at Google Scholar · View at Scopus
  15. J. C. M. Soares, V. Folmer, G. Puntel, and J. B. T. Da Rocha, “Exercise training reverses the deleterious effect of sucrose intake on insulin resistance and visceral fat mass deposition on mice,” American Journal of Biochemistry and Biotechnology, vol. 10, no. 1, pp. 50–57, 2014. View at Publisher · View at Google Scholar · View at Scopus
  16. K. Chan, X.-D. Han, and Y. W. Kan, “An important function of Nrf2 in combating oxidative stress: detoxification of acetaminophen,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 8, pp. 4611–4616, 2001. View at Publisher · View at Google Scholar · View at Scopus
  17. J.-M. Lee, M. J. Calkins, K. Chan, Y. W. Kan, and J. A. Johnson, “Identification of the NF-E2-related factor-2-dependent genes conferring protection against oxidative stress in primary cortical astrocytes using oligonucleotide microarray analysis,” The Journal of Biological Chemistry, vol. 278, no. 14, pp. 12029–12038, 2003. View at Publisher · View at Google Scholar · View at Scopus
  18. S.-H. Yeo, J.-R. Noh, Y.-H. Kim et al., “Increased vulnerability to β-cell destruction and diabetes in mice lacking NAD(P)H: quinone oxidoreductase 1,” Toxicology Letters, vol. 219, no. 1, pp. 35–41, 2013. View at Publisher · View at Google Scholar · View at Scopus
  19. L. D. S. Farias and A. S. L. Mendez, “LC/ESI-MS method applied to characterization of flavonoids glycosides in B. forficata subsp. Pruinosa,” Quimica Nova, vol. 37, no. 3, pp. 483–486, 2014. View at Publisher · View at Google Scholar · View at Scopus
  20. Animal Models of Diabetic Complications Consortium (AMDCC) Protocols, High-Dose Streptozotocin Induction Protocol (Mouse), The University of Michigan Medical Center, 2009, https://www.diacomp.org/shared/showFile.aspx?doctypeid=3&docid=74.
  21. O. Myhre, J. M. Andersen, H. Aarnes, and F. Fonnum, “Evaluation of the probes 2′,7′-dichlorofluorescin diacetate, luminol, and lucigenin as indicators of reactive species formation,” Biochemical Pharmacology, vol. 65, no. 10, pp. 1575–1582, 2003. View at Publisher · View at Google Scholar · View at Scopus
  22. H. Ohkawa, N. Ohishi, and K. Yagi, “Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction,” Analytical Biochemistry, vol. 95, no. 2, pp. 351–358, 1979. View at Publisher · View at Google Scholar · View at Scopus
  23. R. L. Levine, D. Garland, C. N. Oliver et al., “Determination of carbonyl content in oxidatively modified proteins,” in Methods in Enzymology, vol. 186, pp. 464–478, Elsevier, 1990. View at Publisher · View at Google Scholar
  24. V. A. Kostyuk and A. I. Potapovich, “Superoxide—driven oxidation of quercetin and a simple sensitive assay for determination of superoxide dismutase,” Biochemistry International, vol. 19, no. 5, pp. 1117–1124, 1989. View at Google Scholar · View at Scopus
  25. H. Aebi, “Catalase in vitro,” in Methods in Enzymology, vol. 105, pp. 121–126, Elsevier, 1984. View at Google Scholar
  26. S. Sassa, “Delta-aminolevulinic acid dehydratase assay,” Enzyme, vol. 28, no. 2-3, pp. 133–143, 1982. View at Google Scholar · View at Scopus
  27. G. L. Ellman, “Tissue sulfhydryl groups,” Archives of Biochemistry and Biophysics, vol. 82, no. 1, pp. 70–77, 1959. View at Publisher · View at Google Scholar · View at Scopus
  28. M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Publisher · View at Google Scholar · View at Scopus
  29. T. Posser, J. L. Franco, L. Bobrovskaya, R. B. Leal, P. W. Dickson, and P. R. Dunkley, “Manganese induces sustained Ser40 phosphorylation and activation of tyrosine hydroxylase in PC12 cells,” Journal of Neurochemistry, vol. 110, no. 3, pp. 848–856, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. E. Seo, E.-K. Lee, C. S. Lee, K.-H. Chun, M.-Y. Lee, and H.-S. Jun, “Psoralea corylifolia L. seed extract ameliorates streptozotocin-induced diabetes in mice by inhibition of oxidative stress,” Oxidative Medicine and Cellular Longevity, vol. 2014, Article ID 897296, 9 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  31. E. G. Giannini, R. Testa, and V. Savarino, “Liver enzyme alteration: a guide for clinicians,” Canadian Medical Association Journal, vol. 172, no. 3, pp. 367–379, 2005. View at Publisher · View at Google Scholar · View at Scopus
  32. E. H. Harris, “Elevated liver function tests in type 2 diabetes,” Clinical Diabetes, vol. 23, no. 3, pp. 115–119, 2005. View at Publisher · View at Google Scholar · View at Scopus
  33. C. T. Sayago, V. B. Camargo, F. Barbosa et al., “Chemical composition and in vitro antioxidant activity of hydro-ethanolic extracts from Bauhinia forficata subsp. pruinosa and B. variegata,” Acta Biologica Hungarica, vol. 64, no. 1, pp. 21–33, 2013. View at Publisher · View at Google Scholar · View at Scopus
  34. F. A. Caballero, E. N. Gerez, C. F. Polo, E. S. Vazquez, and A. M. Del C. Batlle, “Reducing sugars trigger δ-aminolevulinic dehydratase inactivation: evidence of in vitro aspirin prevention,” General Pharmacology, vol. 31, no. 3, pp. 441–445, 1998. View at Publisher · View at Google Scholar · View at Scopus
  35. D. A. Dickinson and H. J. Forman, “Cellular glutathione and thiols metabolism,” Biochemical Pharmacology, vol. 64, no. 5-6, pp. 1019–1026, 2002. View at Publisher · View at Google Scholar · View at Scopus
  36. D. Siegel, D. L. Gustafson, D. L. Dehn et al., “NAD(P)H:quinone oxidoreductase 1: role as a superoxide scavenger,” Molecular Pharmacology, vol. 65, no. 5, pp. 1238–1247, 2004. View at Publisher · View at Google Scholar · View at Scopus
  37. D. Xu, L. Hu, X. Xia et al., “Tetrachlorobenzoquinone induces acute liver injury, up-regulates HO-1 and NQO1 expression in mice model: the protective role of chlorogenic acid,” Environmental Toxicology and Pharmacology, vol. 37, no. 3, pp. 1212–1220, 2014. View at Publisher · View at Google Scholar · View at Scopus
  38. D. Siegel, A. Anwar, S. L. Winski, J. K. Kepa, K. L. Zolman, and D. Ross, “Rapid polyubiquitination and proteasomal degradation of a mutant form of NAD(P)H:quinone oxidoreductase 1,” Molecular Pharmacology, vol. 59, no. 2, pp. 263–268, 2001. View at Google Scholar · View at Scopus
  39. T. Nguyen, P. Nioi, and C. B. Pickett, “The Nrf2-antioxidant response element signaling pathway and its activation by oxidative stress,” The Journal of Biological Chemistry, vol. 284, no. 20, pp. 13291–13295, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. D. Stewart, E. Killeen, R. Naquin, S. Alam, and J. Alam, “Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium,” The Journal of Biological Chemistry, vol. 278, no. 4, pp. 2396–2402, 2003. View at Publisher · View at Google Scholar · View at Scopus
  41. D. Li and R. F. Duncan, “Transient acquired thermotolerance in Drosophila, correlated with rapid degradation of Hsp70 during recovery,” European Journal of Biochemistry, vol. 231, no. 2, pp. 454–465, 1995. View at Publisher · View at Google Scholar · View at Scopus