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Evidence-Based Complementary and Alternative Medicine
Volume 2011, Article ID 978682, 11 pages
http://dx.doi.org/10.1093/ecam/neq007
Original Article

KIOM-4 Protects against Oxidative Stress-Induced Mitochondrial Damage in Pancreatic β-cells via Its Antioxidant Effects

1School of Medicine, Jeju National University, Jeju-si 690-756, Republic of Korea
2Diabetic Complication Research Center, Division of Traditional Korean Medicine Integrated Research, Korea Institute of Oriental Medicine, Daejeon, Republic of Korea
3Department of Biomaterials, DNA Repair Center, Chosun University, Gwangju, Republic of Korea
4Department of Microbiology and Caner Research Institute, Seoul National University College of Medicine, Seoul, Republic of Korea

Received 22 October 2009; Accepted 29 December 2009

Copyright © 2011 Kyoung Ah Kang 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. D. C. Wallace, “Mitochondrial diseases in man and mouse,” Science, vol. 283, no. 5407, pp. 1482–1488, 1999. View at Publisher · View at Google Scholar · View at Scopus
  2. B. S. Kristal, C. T. Jackson, H.-Y. Chung, M. Matsuda, H. D. Nguyen, and B. P. Yu, “Defects at center P underlie diabetes-associated mitochondrial dysfunction,” Free Radical Biology and Medicine, vol. 22, no. 5, pp. 823–833, 1997. View at Publisher · View at Google Scholar · View at Scopus
  3. T. Nishikawa, D. Edelstein, X. L. Du et al., “Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage,” Nature, vol. 404, no. 6779, pp. 787–790, 2000. View at Publisher · View at Google Scholar · View at Scopus
  4. M. A. Moro, A. Almeida, J. P. Bolaños, and I. Lizasoain, “Mitochondrial respiratory chain and free radical generation in stroke,” Free Radical Biology and Medicine, vol. 39, no. 10, pp. 1291–1304, 2005. View at Publisher · View at Google Scholar · View at Scopus
  5. P. Singh, A. Jain, and G. Kaur, “Impact of hypoglycemia and diabetes on CNS: correlation of mitochondrial oxidative stress with DNA damage,” Molecular and Cellular Biochemistry, vol. 260, no. 1, pp. 153–159, 2004. View at Publisher · View at Google Scholar · View at Scopus
  6. P. Ježek and L. Hlavatá, “Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism,” International Journal of Biochemistry and Cell Biology, vol. 37, no. 12, pp. 2478–2503, 2005. View at Publisher · View at Google Scholar · View at Scopus
  7. D. J. P. Barker and C. Osmond, “Infant mortality, childhood nutrition, and ischaemic heart disease in England and Wales,” The Lancet, vol. 1, no. 8489, pp. 1077–1081, 1986. View at Google Scholar · View at Scopus
  8. T. Nishikawa, D. Edelstein, and M. Brownlee, “The missing link: a single unifying mechanism for diabetic complications,” Kidney International, vol. 58, no. 77, pp. S26–S30, 2000. View at Google Scholar · View at Scopus
  9. M. Brownlee, “Biochemistry and molecular cell biology of diabetic complications,” Nature, vol. 414, no. 6865, pp. 813–820, 2001. View at Publisher · View at Google Scholar · View at Scopus
  10. T. Ohkuwa, Y. Sato, and M. Naoi, “Hydroxyl radical formation in diabetic rats induced by streptozotocin,” Life Sciences, vol. 56, no. 21, pp. 1789–1798, 1995. View at Publisher · View at Google Scholar · View at Scopus
  11. X. Chen, R. M. Touyz, J. B. Park, and E. L. Schiffrin, “Antioxidant effects of vitamins C and E are associated with altered activation of vascular NADPH oxidase and superoxide dismutase in stroke-prone SHR,” Hypertension, vol. 38, no. 3, pp. 606–611, 2001. View at Google Scholar · View at Scopus
  12. H. Raza, S. K. Prabu, M.-A. Robin, and N. G. Avadhani, “Elevated mitochondrial cytochrome P450 2E1 and glutathione S-transferase A4-4 in streptozotocin-induced diabetic rats tissue-specific variations and roles in oxidative stress,” Diabetes, vol. 53, no. 1, pp. 185–194, 2004. View at Publisher · View at Google Scholar · View at Scopus
  13. J. Saito, Y. Sakai, and H. Nagase, “In vitro anti-mutagenic effect of magnolol against direct and indirect mutagens,” Mutation Research, vol. 609, no. 1, pp. 68–73, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. E.-J. Park, S.-Y. Kim, Y.-Z. Zhao, and D. H. Sohn, “Honokiol reduces oxidative stress, c-jun-NH2-terminal kinase phosphorylation and protects against glycochenodeoxycholic acid-induced apoptosis in primary cultured rat hepatocytes,” Planta Medica, vol. 72, no. 7, pp. 661–664, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. A. H. Cao, L. T. Vo, and R. G. King, “Honokiol protects against carbon tetrachloride induced liver damage in the rat,” Phytotherapy Research, vol. 19, no. 11, pp. 932–937, 2005. View at Publisher · View at Google Scholar · View at Scopus
  16. Y.-R. Lin, H.-H. Chen, C.-H. Ko, and M.-H. Chan, “Neuroprotective activity of honokiol and magnolol in cerebellar granule cell damage,” European Journal of Pharmacology, vol. 537, no. 1–3, pp. 64–69, 2006. View at Publisher · View at Google Scholar · View at Scopus
  17. J. Lee, E. Jung, J. Park et al., “Anti-inflammatory effects of magnolol and honokiol are mediated through inhibition of the downstream pathway of MEKK-1 in NF-κB activation signaling,” Planta Medica, vol. 71, no. 4, pp. 338–343, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. K. Y. Ho, C. C. Tsai, C. P. Chen, J. S. Huang, and C. C. Lin, “Antimicrobial activity of honokiol and magnolol isolated from Magnolia officinalis,” Phytotherapy Research, vol. 15, no. 2, pp. 139–141, 2001. View at Publisher · View at Google Scholar · View at Scopus
  19. M. Miyazawa, K. Sakano, S.-I. Nakamura, and H. Kosaka, “Antimutagenic activity of isoflavone from Pueraria lobata,” Journal of Agricultural and Food Chemistry, vol. 49, no. 1, pp. 336–341, 2001. View at Publisher · View at Google Scholar · View at Scopus
  20. K. T. Lee, I. C. Sohn, D. H. Kim, J. W. Choi, S. H. Kwon, and H. J. Park, “Hypoglycemic and hypolipidemic effects of tectorigenin and kaikasaponin III in the streptozotocin-lnduced diabetic rat and their antioxidant activity in vitro,” Archives of Pharmacal Research, vol. 23, no. 5, pp. 461–466, 2000. View at Google Scholar · View at Scopus
  21. K.-T. Lee, I.-C. Sohn, Y.-K. Kim et al., “Tectorigenin, an isoflavone of Pueraria thunbergiana BENTH., induces differentiation and apoptosis in human promyelocytic leukemia HL-60 cells,” Biological and Pharmaceutical Bulletin, vol. 24, no. 10, pp. 1117–1121, 2001. View at Publisher · View at Google Scholar · View at Scopus
  22. H. Liao, L. K. Banbury, and D. N. Leach, “Elucidation of Danzhixiaoyao Wan and its constituent herbs on antioxidant activity and inhibition of nitric oxide production,” Evidence-Based Complementary and Alternative Medicine, vol. 4, no. 4, pp. 425–430, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. Z. Y. Wang and D. W. Nixon, “Licorice and cancer,” Nutrition and Cancer, vol. 39, no. 1, pp. 1–11, 2001. View at Google Scholar · View at Scopus
  24. D. G. Popovich, S. Y. Yeo, and W. Zhang, “Ginseng (Panax quinquefolius) and Licorice (Glycyrrhiza uralensis) root extract combinations increase hepatocarcinoma cell (Hep-G2) viability,” Evidence-Based Complementary and Alternative Medicine. In press. View at Publisher · View at Google Scholar
  25. M. J. Ahn, C. Y. Kim, J. S. Lee et al., “Inhibition of HIV-1 integrase by galloyl glucoses from Terminalia chebula and flavonol glycoside gallates from Euphorbia pekinensis,” Planta Medica, vol. 68, no. 5, pp. 457–459, 2002. View at Publisher · View at Google Scholar · View at Scopus
  26. L.-Y. Kong, Y. Li, X.-L. Wu, and Z.-D. Min, “Cytotoxic diterpenoids from Euphorbia pekinensis,” Planta Medica, vol. 68, no. 3, pp. 249–252, 2002. View at Publisher · View at Google Scholar · View at Scopus
  27. K. A. Kang, J. S. Kim, and J. W. Hyun, “KIOM-4 protects RINm5F pancreatic β-cells against streptozotocin induced oxidative stress in vitro,” Biotechnology and Bioprocess Engineering, vol. 13, no. 2, pp. 150–157, 2008. View at Publisher · View at Google Scholar · View at Scopus
  28. K. A. Kang, J. S. Kim, R. Zhang et al., “Protective mechanism of KIOM-4 against streptozotocin induced diabetic cells: involvement of heme oxygenase-1,” Biotechnology and Bioprocess Engineering, vol. 14, no. 3, pp. 295–301, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. Y. Yoshimura, T. Inomata, H. Nakazawa, H. Kubo, F. Yamaguchi, and T. Ariga, “Evaluation of free radical scavenging activities of antioxidants with an H2O2/NaOH/DMSO system by electron spin resonance,” Journal of Agricultural and Food Chemistry, vol. 47, no. 11, pp. 4653–4656, 1999. View at Publisher · View at Google Scholar · View at Scopus
  30. L. M. Casano, M. Martin, and B. Sabater, “Sensitivity of superoxide dismutase transcript levels and activities to oxidative stress is lower in mature-senescent than in young barley leaves,” Plant Physiology, vol. 106, no. 3, pp. 1033–1039, 1994. View at Google Scholar · View at Scopus
  31. R. Manzer, J. Wang, K. Nishina, G. McConville, and R. J. Mason, “Alveolar epithelial cells secrete chemokines in response to IL-1β and lipopolysaccharide but not to ozone,” American Journal of Respiratory Cell and Molecular Biology, vol. 34, no. 2, pp. 158–166, 2006. View at Publisher · View at Google Scholar · View at Scopus
  32. A. Cossarizza, M. Baccarani-Contri, G. Kalashnikova, and C. Franceschi, “A new method for the cytofluorimetric analysis of mitochondrial membrane potential using the J-aggregate forming lipophilic cation 5,5',6,6'-tetrachloro-1,1',3,3'-tetraethylbenzimidazolcarbocyanine iodide (JC-1),” Biochemical and Biophysical Research Communications, vol. 197, no. 1, pp. 40–45, 1993. View at Publisher · View at Google Scholar · View at Scopus
  33. B. P. Connop, R. L. Thies, K. Beyreuther, N. Ida, and P. B. Reiner, “Novel effects of FCCP [carbonyl cyanide p-(trifluoromethoxy)phenylhydrazone] on amyloid precursor protein processing,” Journal of Neurochemistry, vol. 72, no. 4, pp. 1457–1465, 1999. View at Publisher · View at Google Scholar · View at Scopus
  34. J. C. Wataha, C. T. Hanks, and R. G. Craig, “The in vitro effects of metal cations on eukaryotic cell metabolism,” Journal of Biomedical Materials Research, vol. 25, no. 9, pp. 1133–1149, 1991. View at Google Scholar · View at Scopus
  35. J. Carmichael, W. G. DeGraff, and A. F. Gazdar, “Evaluation of a tetrazolium-based semiautomated colorimetric assay: assessment of chemosensitivity testing,” Cancer Research, vol. 47, no. 4, pp. 936–942, 1987. View at Google Scholar · View at Scopus
  36. I. Fridovich, “Superoxide radical and superoxide dismutases,” Annual Review of Biochemistry, vol. 64, pp. 97–112, 1995. View at Google Scholar · View at Scopus
  37. R. L. Levine, D. Garland, C. N. Oliver et al., “Determination of carbonyl content in oxidatively modified proteins,” Methods in Enzymology, vol. 186, pp. 464–478, 1990. View at Publisher · View at Google Scholar · View at Scopus
  38. M. Toraason, J. Clark, D. Dankovic et al., “Oxidative stress and DNA damage in Fischer rats following acute exposure to trichloroethylene or perchloroethylene,” Toxicology, vol. 138, pp. 43–53, 1999. View at Google Scholar
  39. J. Cai, J. Yang, and D. P. Jones, “Mitochondrial control of apoptosis: the role of cytochrome c,” Biochimica et Biophysica Acta, vol. 1366, no. 1-2, pp. 139–149, 1998. View at Publisher · View at Google Scholar · View at Scopus
  40. T. Nishikawa and E. Araki, “Impact of mitochondrial ROS production in the pathogenesis of diabetes mellitus and its complications,” Antioxidants & Redox Signaling, vol. 9, pp. 343–353, 2007. View at Google Scholar
  41. K. Green, M. D. Brand, and M. P. Murphy, “Prevention of mitochondrial oxidative damage as a therapeutic strategy in diabetes,” Diabetes, vol. 53, no. 1, pp. S110–S118, 2004. View at Google Scholar · View at Scopus
  42. Y. Y. Jang, J. H. Song, Y. K. Shin, E. S. Han, and C. S. Lee, “Protective effect of boldine on oxidative mitochondrial damage in streptozotocin-induced diabetic rats,” Pharmacological Research, vol. 42, no. 4, pp. 361–371, 2000. View at Publisher · View at Google Scholar · View at Scopus
  43. L. Zhang, A. Zalewski, Y. Liu et al., “Diabetes-induced oxidative stress and low-grade inflammation in porcine coronary arteries,” Circulation, vol. 108, no. 4, pp. 472–478, 2003. View at Publisher · View at Google Scholar · View at Scopus
  44. H.-C. Yen, T. D. Oberley, C. G. Gairola, L. I. Szweda, and D. K. St. Clair, “Manganese superoxide dismutase protects mitochondrial complex I against adriamycin-induced cardiomyopathy in transgenic mice,” Archives of Biochemistry and Biophysics, vol. 362, no. 1, pp. 59–66, 1999. View at Publisher · View at Google Scholar · View at Scopus
  45. R. Kakkar, S. V. Mantha, J. Radhi, K. Prasad, and J. Kalra, “Increased oxidative stress in rat liver and pancreas during progression of streptozotocin-induced diabetes,” Clinical Science, vol. 94, no. 6, pp. 623–632, 1998. View at Google Scholar · View at Scopus
  46. T. Adachi, H. Ohta, K. Hirano, K. Hayashi, and S. L. Marklund, “Non-enzymic glycation of human extracellular superoxide dismutase,” Biochemical Journal, vol. 279, no. 1, pp. 263–267, 1991. View at Google Scholar · View at Scopus
  47. S. Salvioli, E. Sikora, E. L. Cooper, and C. Franceschi, “Curcumin in cell death processes: a challenge for CAM of age-related pathologies,” Evidence-Based Complementary and Alternative Medicine, vol. 4, no. 2, pp. 181–190, 2007. View at Publisher · View at Google Scholar · View at Scopus
  48. D. L. Croteau, C. M. J. ap Rhys, E. K. Hudson, G. L. Dianov, R. G. Hansford, and V. A. Bohr, “An oxidative damage-specific endonuclease from rat liver mitochondria,” Journal of Biological Chemistry, vol. 272, no. 43, pp. 27338–27344, 1997. View at Publisher · View at Google Scholar · View at Scopus
  49. F. Cabreiro, C. R. Picot, M. Perichon, J. Castel, B. Friguet, and I. Petropoulos, “Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage,” Journal of Biological Chemistry, vol. 283, no. 24, pp. 16673–16681, 2008. View at Publisher · View at Google Scholar · View at Scopus
  50. K. Yao, P. P. Ye, L. Zhang, J. Tan, X. J. Tang, and Y. D. Zhang, “Epigallocatechin gallate protects against oxidative stress-induced mitochondria-dependent apoptosis in human lens epithelial cells,” Molecular Vision, vol. 14, pp. 217–223, 2008. View at Google Scholar · View at Scopus
  51. K. K. Singh, “Mitochondria damage checkpoint in apoptosis and genome stability,” FEMS Yeast Research, vol. 5, no. 2, pp. 127–132, 2004. View at Publisher · View at Google Scholar · View at Scopus
  52. N. Morita, K. Iizuka, K. Okita et al., “Exposure to pressure stimulus enhances succinate dehydrogenase activity in L6 myoblasts,” American Journal of Physiology, vol. 287, no. 6, pp. E1064–E1069, 2004. View at Publisher · View at Google Scholar · View at Scopus
  53. K. Sakai, K. Matsumoto, T. Nishikawa et al., “Mitochondrial reactive oxygen species reduce insulin secretion by pancreatic β-cells,” Biochemical and Biophysical Research Communications, vol. 300, no. 1, pp. 216–222, 2003. View at Publisher · View at Google Scholar · View at Scopus