Korean Journal of Pharmacognosy (생약학회지)

The Korean Society of Pharmacognosy (한국생약학회)
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Screening of the Inhibitory Activity of Korea Local Plant Extracts against Indoleamine 2,3-dioxygenase (IDO)

한국 자생식물 추출물의 Indoleamine 2,3-dioxygenase (IDO) 저해활성 검색

  • Jang, Jun-Pil (Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology(KRIBB)) ;
  • Jang, Jae-Hyuk (Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology(KRIBB)) ;
  • Bae, Eun-Young (Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology(KRIBB)) ;
  • Jeong, Sook-Jung (Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology(KRIBB)) ;
  • Kim, Hye-Min (Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology(KRIBB)) ;
  • Kim, Mee-Ree (Department of Food and Nutrition, Chungnam National University) ;
  • Soung, Nak-Kyun (Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology(KRIBB)) ;
  • Kim, Bo-Yeon (Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology(KRIBB)) ;
  • Ahn, Jong-Seog (Chemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology(KRIBB))
  • 장준필 (한국생명공학연구원 화학생물연구센터) ;
  • 장재혁 (한국생명공학연구원 화학생물연구센터) ;
  • 배은영 (한국생명공학연구원 화학생물연구센터) ;
  • 정숙정 (한국생명공학연구원 화학생물연구센터) ;
  • 김혜민 (한국생명공학연구원 화학생물연구센터) ;
  • 김미리 (충남대학교 식품영양학과) ;
  • 성낙균 (한국생명공학연구원 화학생물연구센터) ;
  • 김보연 (한국생명공학연구원 화학생물연구센터) ;
  • 안종석 (한국생명공학연구원 화학생물연구센터)
  • Received : 2011.11.10
  • Accepted : 2011.12.22
  • Published : 2011.12.31
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Abstract

Indoleamine 2,3-dioxygenase (IDO) is predicted to be therapeutic target for treatment of cancer and immune disease. Thus, we examined methanol extracts prepared from 156 Korean local plants for their inhibitory effects on IDO in vitro. Among them sixteen extracts showed more than 50% inhibition of IDO activity at the concentration of 30 ${\mu}g/ml$. Especially, the extracts of Platycarya strobilacea, Quercus acutissima, Acer ginnala and Alnus japonica were most potent because their $IC_{50}$ value were 6.5, 8.1, 3.9 and 4.2 ${\mu}g/ml$, respectively.

Keywords

References

  1. Takikawa, O. (2005) Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism. Biochem. Biophys. Res. Commun. 338: 12-19. https://doi.org/10.1016/j.bbrc.2005.09.032
  2. Munn, D. H. and Mellor, A. L. (2007) Indoleamine 2,3-dioxygenase and tumor-induced tolerance. J. Clin. Invest. 117: 1147-1154. https://doi.org/10.1172/JCI31178
  3. Mellor, A. L., Munn, D., Chandler, P., Keskin, D., Johnson, T., Marshall, B., Jhaver, K. and Baban, B. (2003) Tryptophan catabolism and T cell responses. Adv. Exp. Med. Biol. 527: 27-35.
  4. Mellor, A. L. and Munn, D. H. (2004) IDO expression by dendritic cells: tolerance and tryptophan catabolism. Nat. Rev. Immunol. 4: 762-774. https://doi.org/10.1038/nri1457
  5. Taylor, M. W. and Feng, G. S. (1991) Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism. FASEB J. 5: 2516-2522.
  6. Uyttenhove, C., Pilotte, L., Theate, I., Stroobant, V., Colau, D., Parmentier, N., Boon, T. and Van den Eynde, B. J. (2003) Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Nat. Med. 9: 1269-1274. https://doi.org/10.1038/nm934
  7. Guillemin, G. J., Brew, B. J., Noonan, C. E., Takikawa, O. and Cullen, K. M. (2005) Indoleamine 2,3 dioxygenase and quinolinic acid immunoreactivity in Alzheimer's disease hippocampus. Neuropathol. Appl. Neurobiol. 31: 395-404. https://doi.org/10.1111/j.1365-2990.2005.00655.x
  8. Fujigaki, Y., Sakakima, M., Sun, Y., Goto, T., Ohashi, N., Fukasawa, H., Tsuji, T., Yamamoto, T. and Hishida, A. (2007) Immunohistochemical study on caveolin-1alpha in regenerating process of tubular cells in gentamicin-induced acute tubular injury in rats. Virchows. Arch. 450: 671-681. https://doi.org/10.1007/s00428-007-0417-4
  9. Potula, R., Poluektova, L., Knipe, B., Chrastil, J., Heilman, D., Dou, H., Takikawa, O., Munn, D. H., Gendelman, H. E. and Persidsky, Y. (2005) Inhibition of indoleamine 2,3-dioxygenase (IDO) enhances elimination of virus-infected macrophages in an animal model of HIV-1 encephalitis. Blood 106: 2382-2390. https://doi.org/10.1182/blood-2005-04-1403
  10. Mellor, A. L., Keskin, D. B., Johnson, T., Chandler, P. and Munn, D. H. (2002) Cells expressing indoleamine 2,3-dioxygenase inhibit T cell responses. J. Immunol. 168: 3771- 3776.
  11. Friberg, M., Jennings, R., Alsarraj, M., Dessureault, S., Cantor, A., Extermann, M., Mellor, A. L., Munn, D. H. and Antonia, S. J. (2002) Indoleamine 2,3-dioxygenase contributes to tumor cell evasion of T cell-mediated rejection. Int. J. Cancer 101: 151-155. https://doi.org/10.1002/ijc.10645
  12. Takikawa, O., Kuroiwa, T., Yamazaki, F. and Kido, R. (1988) Mechanism of interferon-gamma action. Characterization of indoleamine 2,3-dioxygenase in cultured human cells induced by interferon-gamma and evaluation of the enzymemediated tryptophan degradation in its anticellular activity. J. Biol. Chem. 263: 2041-2048.