Journal of Pharmacopuncture (대한약침학회지)

KOREAN PHARMACOPUNCTURE INSTITUTE (대한약침학회)
권호 표지
DOI QR코드

DOI QR Code

HepG2 세포의 산화적 손상에 대한 산삼 추출물의 보호효과 - DNA chip을 이용하여 -

  • Kim, Hyung-Seok (Dept. of Acup & Moxibustion, College of Oriental Medicine, Sangji University) ;
  • Park, Hee-Soo (Dept. of Acup & Moxibustion, College of Oriental Medicine, Sangji University) ;
  • Kwon, Ki-Rok (Dept. of Acup & Moxibustion, College of Oriental Medicine, Sangji University)
  • 김형석 (상지대학교 한의과대학 침구학교실) ;
  • 박희수 (상지대학교 한의과대학 침구학교실) ;
  • 권기록 (상지대학교 한의과대학 침구학교실)
  • Published : 2007.02.28
Download PDF
⟨ Previous Next ⟩

Abstract

Objectives : This study was carried out to examine protective effect of wild ginseng extract on HepG2 human hepatoma cell line against tert-Butyl hydroperoxide (t-BHP)-induced oxidative damage. Methods : To evaluate protective effect of wild ginseng extract against t-BHP induced cytotoxicity, LDH level and activity of glutathione peroxidase and reductase were measured. Gene expression was also measured using DNA microarray. Results : Wild ginseng extract showed a significant protective effect against t-BHP-induced cytotoxicity in HepG2 cell line. It is not, however, related with the activities of glutathione peroxidase and glutathione reductase. Analysis of gene expression using DNA chip, demonstrated that 28 genes were up-regulated in t-BHP only group. Five genes - selenoprotein P, glutathione peroxidase 3, sirtuin 2, peroxiredoxin 2, serfiredoxin 1 homolog - may be related with the protective effect of wild ginseng extract. Conclusions : Based on the results, a protective effect of wild ginseng extract against t-BHP-induced oxidative damage in HepG2 cell line is not associated with the activities of glutathione peroxidase and glutathione reductase, but with the expression of selenoprotein P, glutathione peroxidase 3, sirtuin 2, peroxiredoxin 2, and serfiredoxin 1 homolog.

Keywords

References

  1. 전국한의과대학 본초학교수 공편저. 본초학. 서울, 영림사. 1985; 531
  2. 중약대사전편찬위원회. 완역중약대사전 권7. 서울, 정담. 1997; 3473-3479
  3. 신순식. 산삼 감정 기준의 객관성. 동의 한의연 제 5집. 2001; 107-114
  4. 최진호, 인삼의 신비, 서울, 교문사, p13-14, 1984
  5. 권기록, 위종성, 김성욱. 산삼에 대한 문헌적 고찰. 대한약침학회지. 2003; 6(2):67-76 https://doi.org/10.3831/KPI.2003.6.2.067
  6. 朝鮮總督府專賣局, 人蔘史. 서울, 法人文化社, 1960; 3-4
  7. 하대유. 인삼에 대한 세포학 및 면역학적 연구. 대한 면역학회지. 1979; 1(1): 45-52
  8. 山田昌之. 朝鮮人蔘의 硏究. 日本藥理學會誌. 1955; 51: 390
  9. Brekhman. I.I, Panax ginseng, Gosudarst Isdat et Med, Lit. Leningard, 1957; 1
  10. Kim, MJ., Jung, NP. The effect of ginseng saponin on the mouse immune system. Korean J. Ginseng Sci. 11: 1987; 130-135
  11. 남기열. 최신 고려인삼. 경기도, 천일인쇄소. 1996; 56
  12. Takagi, K, Proceedings International Ginseng Symposium, The Central Research Institute, Office of Monopoly, Seoul, Korea, 1974; 119
  13. 김승환, 장명제, 이성규, 장완성, 최현희, 성종환. 인삼복용시 과산화지질과 총항산화능에 미치는 영향. 한국체육학회지. 2003; 42(3): 661-668
  14. Choi, KJ., Kim, MW., Hong, SK., Kim, DH. Effect of solvents on the yield, brown color intensity, UV absorbance, reducing and antioxident activities of extracts from white and red ginseng. J. Korean Agric. Chem. Soc. 1983; 26: 8-18
  15. 이승은, 이성우, 방진기, 유영주, 성낙슬. 인삼의 부위별 항산화활성. Korean J. Medicinal Crop. Sci. 2004; 12(3): 237-242
  16. 김성진, 신순식, 서부일, 지선영. 산삼, 장뇌삼, 인삼의 항암효과 비교연구. 대한본초학회지. 2004; 19(2); 41-50
  17. Se Na Yun, Sang Jung Moon, Sung Kwon Ko, Byung Ok Im, Sung Hyun Chung. Wild Ginseng Prevents the Onset of High-Fat Diet Induced Hyperglycemia and Obesity in ICR mice. Arch Pham Res. 2004; 27(7): 790-796 https://doi.org/10.1007/BF02980150
  18. Davies, M.J. Detection of peroxyl and alkoxyl radicals produced by reaction of hydroperoxydase with rat liver microsomal fractions. Biochem. J. 1989; 257: 603-606
  19. Lee HU, Bae EA, Han MJ, Kim DH. Hepatoprotective effect of 20(S)-ginsenosides Rg3 and its metabolite 20(S)-ginsenoside Rh2 on tert-butyl hydroperoxide-induced liver injury. Biol Pharm Bull. 2005; 28: 1992-1994 https://doi.org/10.1248/bpb.28.1992
  20. Burk RF, Hill KE. Selenoprotein P: an extracellular protein with unique physical characteristics and a role in seleniμM homeostasis. Annu Rev Nutr. 2005; 25: 215-235 https://doi.org/10.1146/annurev.nutr.24.012003.132120
  21. Carlson BA, Novoselov SV, KμMaraswamy E, Lee BJ, Anver MR, Gladyshev VN, Hatfield DL. Specific excision of the selenocysteine tRNA[Ser]Sec (Trsp) gene in mouse liver demonstrates an essential role of selenoproteins in liver function. J Biol Chem. 2004; 279: 8011-8017 https://doi.org/10.1074/jbc.M310470200
  22. Burk RF, Hill KE, Read R, Bellew T. Response of rat selenoprotein P to selenium administration and fate of its selenium. Am J Physiol. 1991; 261: E26-30
  23. Flohe L, Brigelius-Flohe R, Maiorino M, Roveri A, Wissing J, Ursini F. Selenium and male reproduction. 2001; 157-178
  24. Takahashi K, Avissar N, Whitin J, Cohen H. Purification and characterization of hμMan plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme. Arch Biochem Biophys. 1987; 256: 677-686 https://doi.org/10.1016/0003-9861(87)90624-2
  25. Takebe G, Yarimizu J, Saito Y, Hayashi T, Nakamura H, Yodoi J, Nagasawa S, Takahashi K. A comparative study on the hydroperoxide and thiol specificity of the glutathione peroxidase family and selenoprotein P. J Biol Chem. 2002; 277: 41254-41258 https://doi.org/10.1074/jbc.M202773200
  26. Avissar N, Ornt DB, Yagil Y, Horowitz S, Watkins RH, Kerl EA, Takahashi K, Palmer IS, Cohen HJ. HuMan kidney proximal tubules are the main source of plasma glutathione peroxidase. Am J Physiol. 1994; 266: C367-375
  27. Chu FF, Esworthy RS, Doroshow JH, Doan K, Liu XF. Expression of plasma glutathione peroxidase in hμMan liver in addition to kidney, heart, lung, and breast in hμMans and rodents. Blood. 1992; 79: 3233-3238
  28. Whitin JC, Bhamre S, Tham DM, Cohen HJ. Extracellular glutathione peroxidase is secreted basolaterally by hμMan renal proximal tubule cells. Am J Physiol Renal Physiol. 2002; 283: F20-28
  29. Burk RF, Early DS, Hill KE, Palmer IS, Boeglin ME. Plasma seleniμM in patients with cirrhosis. Hepatology. 1998. 27: 794-798 https://doi.org/10.1002/hep.510270322
  30. Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J Biol Chem. 2000. 275: 20346-20354 https://doi.org/10.1074/jbc.M001943200
  31. Rhee SG, Kang SW, Chang TS, Jeong W, Kim K. Peroxiredoxin, a novel family of peroxidases. IUBMB Life. 2001. 52: 35-41 https://doi.org/10.1080/15216540252774748
  32. Kang SW, Chae HZ, Seo MS, Kim K, Baines IC, Rhee SG. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem. 1998. 273: 6297-6302 https://doi.org/10.1074/jbc.273.11.6297
  33. Ishii T, Yamada M, Sato H, Matsue M, Taketani S, Nakayama K, Sugita Y, Bannai S. Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein. J Biol Chem. 1993. 268: 18633-18636
  34. Findlay VJ, Tapiero H, Townsend DM. Sulfiredoxin: a potential therapeutic agent? Biomed Pharmacother. 2005. 59: 374-379 https://doi.org/10.1016/j.biopha.2005.07.003
  35. Denu JM. Vitamin B3 and sirtuin function. Trends Biochem Sci. 2005. 30: 479-483 https://doi.org/10.1016/j.tibs.2005.07.004
  36. Bell SD, Botting CH, Wardleworth BN, Jackson SP, White MF. The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation. Science. 2002. 296: 148-151 https://doi.org/10.1126/science.1070506
  37. Borra MT, O'Neill FJ, Jackson MD, Marshall B, Verdin E, Foltz KR, Denu JM. Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases. J Biol Chem. 2002. 277: 12632-12641 https://doi.org/10.1074/jbc.M111830200