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Our work in this study was made in the microsomal fraction to evaluate the lipid peroxidation by measuring superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and malondialdehyde (MDA) and to elucidate the preventive role of CS in the $CCl_4$-induced oxidative stress. The excessive lipid peroxidation by free radicals derived from $CCl_4$ leads to the condition of oxidative stress which results in the accumulation of MDA. MDA is one of the end-products in the lipid peroxidation process and oxidative stress. MDA, lipid peroxide, produced in this oxidative stress causes various diseases related to aging and hepatotoxicity, etc. Normal cells have a number of enzymatic and nonenzymatic endogenous defense systems to protect themselves from reactive species. The enzymes in the defense systems, for example, are SOD, CAT, and GPx. They quickly eliminate reactive oxygen species (ROS) such as superoxide anion free radicalㆍO$^{[-10]}$ $_2$, hydrogen peroxide $H_2O$$_2$ and hydroxyl free radicalㆍOH. CS inhibited the accumulation of MDA and the deactivation of SOD, CAT and GPx in the dose-dependent and preventive manner. Our study suggests that CS might be a potential scavenger of free radicals in the oxidative stress originated from the lipid peroxidation of the liver cells of $CCl_4$-treated rats.

참고문헌 (20)

  1. Aebi, H., A Catalase in vitro. Methods Enzymol., 105, 121-126 (1984) 
  2. Albertini, R., Rindi, S., Passi, A., Pallavicini, G., and De Luca, G., Heparin protection against $Fe^{2+}$-and $Cu^{2+}$-mediated oxidation of liposome. FEBS Lett., 383, 155-158 (1996) 
  3. Ha, B. J. and Lee, J. Y., The Effect of Chondroitin Sulfate against $CCI_{4}$-lnduced Hepatotoxidcity. Biol. Pharm. Bull., 26, 622-626 (2003) 
  4. Baldwin, D. A., Jenny E. R., and Aisen, P., The effect of human serum transferrin and milk lactoferrin on hydroxyl radical formation from superoxide and hydrogen peroxide. J. Biol. Chem., 259, 13391-13394 (1984) 
  5. Beauchamp, C. and Fridovich, I., Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem., 44, 276-287 (1971) 
  6. Bird, R. P. and Draper, H. H., Effect of malonaldehyde and acetaldehyde on cultured mammalian cells: Growth, morphology, and synthesis of macromolecules. J. Environ. Health, 6, 811-823 (1980) 
  7. Elman, G. L., Tissue sulphydryl groups. Arch. Biochem. Biophys., 82, 70-77 (1959) 
  8. Hagihara, M., Nishigaki, I., Maseki, M., and Yagi, K., Agedependent changes in lipid peroxide levels in the lipoprotein fractions of human serum. J. Gerontol., 39, 269-272 (1984) 
  9. Halliwell, B., Gutteridge, J. M., and Cross, C. E., Free radicals, antioxidants, and human disease: where are we now? J. Lab. Clin. Med., 119, 598-620 (1992) 
  10. Kurata, M., Suzuki, M., and Agar, N. S., Antioxidant systems and erythrocyte life-span in mammals. Compo. Biochem. Physiol. B., 106, 477-487 (1993) 
  11. Lai, E. K., McCay, P. B., Noguchi, T., and Fong, K. L., In vivo spin-trapping of trichloromethyl radicals formed from $CCI_{4}$, Biochem. Pharmacol., 28, 2231-2235 (1979) 
  12. Laila, G., Yues, A., Bernard, H., Claude, J., Gerard, C., and Gerard, S., Biological variability of superoxide dismutase, glutathione peroxidase, and catalase in blood. Clin. Chem. B., 37(11), 1932-1937 (1991) 
  13. Lawrence, R. A. and Burk, R. F., Glutathione peroxidase activity in selenium-deficient rat liver. Blochem. Biophys. Res. Common., 71, 952-958 (1976) 
  14. Lin, C. Q. and Bissel, M. J., Multi-faceted regulation of cell differentiation by extracellular matrix. FASEM J. 7, 737-743 (1993) 
  15. Lowry, O. H. and Rosenbrough, N. J., Protein measurement with folin reagent. J. Biol. Chem., 193, 265-275 (1951) 
  16. Okhawa, H, Ohishi, N., and Vagi, K., Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem., 95, 351-358 (1979) 
  17. Puglia, C. D. and Powell, S. R., Inhibition of cellular antioxidants: a possible mechanism of toxic cell injury. Environ. Health Perspect., 57, 307-311 (1984) 
  18. Ross, M. A., Long, W. F., and Williamson, F. B., Inhibition by heparin of Fe(II)-catalysed free-radical peroxidation of linoleic acid. Biochem. J., 286, 717-720 (1992) 
  19. Salminen, A., Kainulainen, H., Arstila, A. U., and Vihko, v., Vitamin E deficiency and the susceptibility to lipid peroxidation of mouse cardiac and skeletal muscles. Acta. physiol. Scand., 122,565-570 (1984) 
  20. Yu, B. P., Cellular defenses against damage from reactive oxygen species. Physiol. Rev., 74, 139-162 (1994) 

이 논문을 인용한 문헌 (4)

  1. 2004. "" Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea, 27(8): 867~872 
  2. 2008. "" Biotechnology and bioprocess engineering, 13(2): 168~173 
  3. 2008. "" Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea, 31(5): 622~627 
  4. 2011. "" Archives of pharmacal research : a publication of the Pharmaceutical Society of Korea, 34(5): 801~810 


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