The Chemopreventive Effects of Antioxidant Enzyme

항산화효소의 암 예방 효과 및 발암 억제 기전

  • Jung Hwa-Jin (Department of Pharmacology, Institute for Research of Medical Science (IRMS), School of Medicine, Kyung Hee University) ;
  • Choi Yoon-Joo (Department of Pharmacology, Institute for Research of Medical Science (IRMS), School of Medicine, Kyung Hee University) ;
  • Won Chang-Won (Department of Family Medicine, School of Medicine, Kyung Hee University) ;
  • Seo Young-Rok (Department of Pharmacology, Institute for Research of Medical Science (IRMS), School of Medicine, Kyung Hee University)
  • 정화진 (경희대학교 의과대학 약리학교실 및 기초의과학연구소) ;
  • 조윤주 (경희대학교 의과대학 약리학교실 및 기초의과학연구소) ;
  • 원장원 (경희대학교 의과대학 가정의학과) ;
  • 서영록 (경희대학교 의과대학 약리학교실 및 기초의과학연구소)
  • Published : 2006.06.01

Abstract

The reactive oxygen species (ROS) caused the damage of macro molecules, many degenerative disease and cancer, which was produced in process of the aerotropic metabolic pathway as well as in response to the various genotoxic stresses. Recently, redox systems including the number of antioxidant proteins such as catalase, glutathione peroxidase, heam-containing peroxidase, peroxiredoxin and superoxide dismutase (SOD) has been reported to have chemopreventive effects. Antioxidant proteins has been known to have the activity directly removing ROS and affecting the protein-protein interaction and cell signaling to induce the cellular responses. We need to understand the mechanism of antioxidants prevent DNA damage from oxidative stresses for researching the cancer prevention and providing the development of cancer therapeutic drug.

Keywords

References

  1. Moss, R.W. PhD. (2002) Antioxidants against cancer. State College, PA, Equinox Press, pp. 7-121
  2. Powis, G. and Montfort, W.R. (2001) Properties and biological activities of thioredoxins. Annu. Rev. Pharmacol. Toxicol. 41, 261-295 https://doi.org/10.1146/annurev.pharmtox.41.1.261
  3. Chae, H.Z., Kang, S.W. and Rhee, S.G. (1999) Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin. Methods Enzymol. 300, 219-226 https://doi.org/10.1016/S0076-6879(99)00128-7
  4. Nordberg, J. and Arner, E.S.J. (2001) Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic. Biol. 31, 1287-1312 https://doi.org/10.1016/S0891-5849(01)00724-9
  5. Holmgren, A. Glutaredoxin. Aslund F. (1995) Methods Enzymol 252, 283-292 https://doi.org/10.1016/0076-6879(95)52031-7
  6. Holmgren, A. (1976) Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc. Natl. Acad. Sci. USA. 73, 2275-2279
  7. Bushweller, J.H.J., Billeter, M., Holmgren, A. and Wuthrich, K. (1994) The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin (C14S) and glutathione. Mol. Biol. 235, 1585-1597
  8. Kirsch, M., Groot, H.D. (2001) NAD(P)H, a directly operating antioxidant? FASEB J. 15, 1569-1574 https://doi.org/10.1096/fj.00-0823hyp
  9. Chae, H.Z., Chung, S.J. and Rhee, S.G. (1994) Thioredoxindependent peroxide reductase from yeast. J. Biol. Chem. 296, 27670-27678