Natural Product Sciences

The Korean Society of Pharmacognosy (한국생약학회)
권호 표지

Rhus verniciflua Stokes Attenuates Glutamate-induced Neurotoxicity in Primary Cultures of Rat Cortical Cells

  • Jeong, Eun-Ju (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University) ;
  • Sung, Sang-Hyun (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University) ;
  • Kim, Jin-Woong (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University) ;
  • Kim, Seung-Hyun (Institute for Life Science, Elcom Science Co. Ltd.) ;
  • Kim, Young-Choong (College of Pharmacy and Research Institute of Pharmaceutical Science, Seoul National University)
  • Published : 2008.09.30
Download PDF
⟨ Previous Next ⟩

Abstract

The methanolic extract of Rhus verniciflua Stokes (RVS-T) and its fractions (RVS-H, RVS-C, RVS-E and RVS-B) showed significant neuroprotective activity against glutamate-induced toxicity in primary cultures of rat cortical cells. RVS-B, which showed the most potent neuroprotective activity, was further fractionated to yield RVS-B5. Treatment of cortical cells with the RVS-T, RVS-B and RVS-B5 reduced the cellular ROS level and restored the reduced activities of glutathione reductase and SOD induced by glutamate. Although, the activity of glutathione peroxidase was not virtually changed by glutamate, RVS-B5 increased the glutathione peroxidase activity. In addition, these three tested fractions significantly restored the content of GSH which was decreased by glutamate insult in our cultures. Taken together, it could be postulated that RVS extract, in particular its fraction RVS-B5, protected neuronal cells against glutamate-induced neurotoxicity through acting on the antioxidative defense system.

Keywords

References

  1. Albright, T.D., Jessell, T.M., Kandel, E.R., and Poster, M.I., Neural science: a century of progress and the mysteries that remain. Cell 18, 1-55 (2000) https://doi.org/10.1016/0092-8674(79)90348-9
  2. Carlberg, I. and Mannervik, B., Purification and characterization of the flavoenzyme glutathione reductase from rat liver. J. Biol. Chem. 25, 5475-5480 (1975)
  3. Chase, T.N. and Oh, J.D., Striatal mechanisms and pathogenesis of parkinsonian signs and motor complications. Ann. Neurol. 47, 7-14 (2000)
  4. Choi, D.W., Ionic dependence of glutamate neurotoxicity. J. Neurosci 7, 369-379 (1987) https://doi.org/10.1523/JNEUROSCI.07-02-00369.1987
  5. Choi, D.W., Glutamate neurotoxicity and disease of the nervous system. Neuron 1, 623-634 (1988) https://doi.org/10.1016/0896-6273(88)90162-6
  6. Choi, D.W. and Rothman, S.M., The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death. Annu. Rev. Neurosci. 13, 171-182 (1990) https://doi.org/10.1146/annurev.ne.13.030190.001131
  7. Choi, J., Yoon, B.J., Han, Y.N., Lee, K.T., Ha, J., Jung, H.J., and Park, H.J., Antirhematoid arthritis effect of Rhus verniciflua and of the active component, sulfuretin. Planta Med. 69, 899-904 (2003) https://doi.org/10.1055/s-2003-45097
  8. Coyle, J.T. and Puttfarcken P., Oxidative stress, glutamate and neurodegenerative disorders. Science 262, 689-659 (1993) https://doi.org/10.1126/science.7901908
  9. Flohe, L. and Gunzler, W.A., Assays of glutathione peroxidase. Methods Enzymol. 105, 114-121 (1984) https://doi.org/10.1016/S0076-6879(84)05015-1
  10. Goodman, Y. and Mattson, M.P., Selected forms of b-amyloid precursor protein protect hippocampal neurons against amyloid b-peptide induced oxidative injury. Exp. Neurol. 128, 1-12 (1994) https://doi.org/10.1006/exnr.1994.1107
  11. Heintz, N. and Zoghbi, H.Y., Insights from mouse models into the molecular basis of neurodegeneration. Annu. Rev. Physiol. 62, 779-802 (2000) https://doi.org/10.1146/annurev.physiol.62.1.779
  12. Jung, C.H., Jun, C.Y., Lee, S., Park, C.H., Cho, K., and Ko, S.G., Rhus verniciflua Stokes extract: Radical scavenging activities and protective effects on $H_2O_2-induced$ cytotoxicity in macrophage raw 264.7 cell lines. Biol. Pharm. Bull. 29, 1603-1607 (2006) https://doi.org/10.1248/bpb.29.1603
  13. Kim, Y.C., Kim, S.R., Markelonis, G.J., and Oh, T.H., Ginsenosides Rb1 and Rg3 protect cultured rat cortical cells from glutamate-induced neurodegeneration. J. Neurosci. Res. 53, 426-432 (1998) https://doi.org/10.1002/(SICI)1097-4547(19980815)53:4<426::AID-JNR4>3.0.CO;2-8
  14. Kim, T.J., Korea Resource Plants, vol II. Seoul University Press, Seoul, Korea, 292-297, 1996
  15. Lipton, S.A. and Rosenberg, P.A., Excitatory amino acids as a final common pathway for neurologic disorders. N. Engl. J. Med. 330, 613- 622 (1994) https://doi.org/10.1056/NEJM199403033300907
  16. Meldrum, B.S., Implications for neuroprotective treatments. Prog. Brain. Res. 135, 487-495 (2002) https://doi.org/10.1016/S0079-6123(02)35046-5
  17. Muir, K.W. and Lees, K.R., Clinical experience with excitatory amino acid antagonist drugs. Stroke 26, 503-513 (1995) https://doi.org/10.1161/01.STR.26.3.503
  18. Trist, D.G., Excitatory amino acid agonists and antagonists: pharmacology and therapeutic applications. Pharm. Acta. Helv. 74, 221-229 (2000) https://doi.org/10.1016/S0031-6865(99)00053-9
  19. Lee, J.C., Lim, K.T., and Jang, Y.S., Identification of Rhus verniciflua Stokes compounds that exhibit free radical scavenging and antiapoptotic properties. Biochim. Biophys. Acta. 1570, 181-91 (2002) https://doi.org/10.1016/S0304-4165(02)00196-4
  20. Lee, J.M., Zipfel, G.J., and Choi, D.W., The changing landscape of ischemic brain injury mechanisms. Nature (London) 399, 7-14 (1999)
  21. Lim, K.T., Lee, J.C., Jung, H.Y., and Jo, S.K., Effects of Rhus verniciflua Stokes (RVS) on cell-associated detoxificant enzymes, and glucose oxidase-medicated toxicity in cultured mouse hepatocytes. Kor. J. Toxicol. Pub. Health 16, 125-131 (2000)
  22. Lu, S.C., Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J. 13, 1169-1183 (1999) https://doi.org/10.1096/fasebj.13.10.1169
  23. Mates, J.M. and Sanchez-Jimenez, F.M., Role of reactive oxygen species in apoptosis: implications for cancer therapy. IJBCB 32, 157-170 (2000)
  24. McCord, J.M. and Fridovich, I., The utility of superoxide dismutase in studying free radical reactions. . Radicals generated by interaction of sulfite, dimethyl sulfoxide, and oxygen. J. Biol. Chem. 25, 6056-6063 (1969)
  25. Middleton, Jr.E. and Kandaswani, C., Effects of flavonoids on immune and inflammatory cell functions. Biochem. Pharmacol. 43, 1167-1179 (1992) https://doi.org/10.1016/0006-2952(92)90489-6
  26. Park, B.C., Lee, Y.S., Park, H.J., Kwak, M.K., Yoo, B.K., Kim, J.Y., and Kim, J.A., Protective effects of fustin, a flavonoid from Rhus verniciflua Stokes, on 6-hydroxydopamine-induced neuronal cell death. Exp. Mol. Med. 39, 316-326 (2007) https://doi.org/10.1038/emm.2007.35
  27. Park, K.Y., Jung, G.O., Lee, K.T., Choi, J., Choi, M.Y., Kim, G.T., Jung, H.J., and Park, H.J., Antimutagenic activity of flavonoids from the heartwood of Rhus verniflua. J. Ethnopharmacol. 90, 73-79 (2004) https://doi.org/10.1016/j.jep.2003.09.043
  28. Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzano, M.D., Fujimoto, E.K., Goeke, N.M., Olson, B.J., and Klenk, D.C., Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85 (1985) https://doi.org/10.1016/0003-2697(85)90442-7
  29. Tietz, F., Enzymatic method of quantitative determination of nanogram amounts of total and oxidized glutathione. Anal. Biochem. 27, 502- 522 (1969) https://doi.org/10.1016/0003-2697(69)90064-5