Archives of Pharmacal Research

  • 제27권8호
  • /
  • Pages.867-872
  • /
  • 2004
  • /
  • 0253-6269(pISSN)
  • /
  • 1976-3786(eISSN)
대한약학회 (The Pharmaceutical Society of Korea)
권호 표지

Oxidative Stress in Ovariectomy Menopause and Role of Chondroitin Sulfate

  • Ha, Bae-Jin (Department of Bioscience and Biotechnology, Silla University)
  • 발행 : 2004.08.01
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Oxidative stress due to reactive oxygen species (ROS) can cause oxidative damage to cells. Cells have a number of defense mechanisms to protect themselves from the toxicity of ROS. Mitochondria are especially important in the oxidative stress as ROS have been found to be constantly generated as an endogen threat. Mitochondrial defense depends mainly on super-oxide dismutase (SOD) and glutathione peroxidase (GPx), whereas microsomal defense depends on catalase (CAT), which is an enzyme abundant in microsomes. SOD removes superoxide anions by converting them to $H_2O$$_2$, which can be rapidly converted to water by CAT and GPx. Also, GPx converts hydroperoxide (ROOH) into oxidized-glutathione (GSSG). Ovariectomized (OVX) rats are used as an oxidative stress model. An ovariectomy increased the levels of MDA, one of the end-products in the lipid peroxidative process, and decreased levels of the antioxidative enzymes； SOD, CAT and GPx. However, Chondroitin sulfate (CS) decreased the levels of MDA, but increased the levels of SOD, CAT and GPx in a dose-depen-dent manner. Moreover, inflammation and cirrhosis of liver tissue in CS- treated rats were sig-nificantly decreased. These results suggest that CS might be a potential candidate as an anti oxidative reagent.

키워드

참고문헌

  1. Aebi, H., Catalase in vitro. Methods in Enzymol., 105, 121-126 (1984) https://doi.org/10.1016/S0076-6879(84)05016-3
  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) https://doi.org/10.1016/0014-5793(96)00253-0
  3. 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)
  4. Cand, F. and Verdetti, J., Superoxide dismutase, glutathione peroxidase, catalase, and lipid peroxidation in the major organs of the aging rats. Free Rad. Biol. Med., 7, 59-63 (1989) https://doi.org/10.1016/0891-5849(89)90101-9
  5. Cutler, R. G., Urate and ascorbate: their possible role as antioxidants in determining longevity of mammalian species. Arch. Gerontol. Geriatr., 3, 321-348 (1985)
  6. Esterbauer, H. and Cheeseman, K. H., Determination of aldehydic lipid peroxidation products: malonaldehyde and 4-hydroxynonenal. Methods in Enzymol., 186, 407-421 (1990) https://doi.org/10.1016/0076-6879(90)86134-H
  7. Esterbauer, H., Schaur, R. J., and Zollner, H., Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Rad. Biol. Med., 11, 81-128 (1991) https://doi.org/10.1016/0891-5849(91)90192-6
  8. Fridovich, I. and Beauchamp, C., Superoxide dismutase : Improved assays and an assay applicable to acrylamide gals. Anal. Biochem., 44, 276-278 (1971) https://doi.org/10.1016/0003-2697(71)90370-8
  9. Ha, B. J. and Lee, J. Y., The Effect of Chondroitin Sulfate against$CCI_{4}$-lnduced Hepatotoxicity. Biol. Pharm. Bull., 26, 622-626 (2003) https://doi.org/10.1248/bpb.26.622
  10. 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)
  11. Jira, W., Spiteller, G., and Schramm, A., Increase in hydroxy fatty acids in human low density lipoproteins with age. Chem. Phys. Lipids, 84, 165-173 (1996) https://doi.org/10.1016/S0009-3084(96)02635-7
  12. Lawrence, R. A. and Burk, R. F., Glutathione peroxidase activity in selenium-deficiency rat liver. Biochem. Res. Commom., 71, 952-958 (1976) https://doi.org/10.1016/0006-291X(76)90747-6
  13. Lee, J. Y., Lee, S. H., Kim, H. J., Ha, J. M., Lee, S. H., Lee, J. H., and Ha, B. J., The Preventive inhibition of Chondroitin Sulfate Against the $CCI_{4}$-lnduced Oxidative Stress of Subcellular Level. Arch. Pharm. Res., 27, 340-345 (2004) https://doi.org/10.1007/BF02980070
  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 foline phegent. J. Biol. Chem., 193, 265-275 (1951)
  16. Matsuo, M., Gomi, F., and Sagai, M., Suppression of an age-dependent increase in the respiration rate of pentane by food restriction. Recent Adv. Aging Sci., 15th Proc. Congr. Int. Assoc. Gerontol., 1, 239-244 (1993)
  17. Mattson, M. P., Waeg, W., Fu, G., and Uchida, K., 4Hydroxynonenal, a product of lipid peroxidation, inhibits dephosphorylation of the microtubule-associated protein tau. NeuroReport, 8, 2275-2281 (1997) https://doi.org/10.1097/00001756-199707070-00036
  18. Ohkawa, H., Ohishi, N., and Yagi, K., Assay for lipid peroxides in animal tissues by thiobarbituric acid. Anal. Biochem., 95, 351-358 (1979) https://doi.org/10.1016/0003-2697(79)90738-3
  19. Player, T. J., Mills, D. J., and Horton, A. A., Age-dependent change in rat liver microsomal and Mitochondrial NADPH-dependent lipid peroxidation. Biochem. Biophys. Res. Commun., 78, 1397-1402 (1997) https://doi.org/10.1016/0006-291X(77)91447-4
  20. 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)
  21. Tomalsoff, J. M., Ono, T., and Cutler, R. G., Superoxide dismutase: correlation with lifespan and specific metabolic rate in primate species. Proc. Natl. Acad. Sci. U.S.A., 77, 2777-2781 (1980) https://doi.org/10.1073/pnas.77.5.2777
  22. Waeg, G., Dimsity, G., and Esterbauer, H., Monoclonal antibodies for detection of 4-hydroxynonenal modified proteins. Free Rad. Res., 25, 149-159 (1996) https://doi.org/10.3109/10715769609149920
  23. Yu, B. P., Cellular defenses against damages from reactive oxygen species. Physiol. Rev., 74, 139-162 (1994)
  24. Zarling, E. J., Mobarhan, S., Bowen, P., and Kamath, S., Pulmonary pentane excretion increases with age in healthy subjects. Mech.Ageing Dev., 67, 141-147 (1993) https://doi.org/10.1016/0047-6374(93)90118-B