Browse > Article

Protective Effect of Curcumin and Aqueous Extract of Onchengyeum on CCI4-induced Hepatotoxicity  

SEUNG Keum Ran (Duksung Women's University)
JUNG Ki Hwa (Duksung Women's University)
Publication Information
Biomolecules & Therapeutics / v.13, no.4, 2005 , pp. 232-239 More about this Journal
Abstract
An aqueous extract of oriental herbal composition named Onchengyeum and curcumin, an antioxidant isolated from turmeric (Curcuma Zonga L.) reduced hepatotoxicity induced by carbon tetrachloride ($CCI_4$). Improved liver function was observed by measuring the activities of aspartate aminotransferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP), blood urea nitrogen (BUN), creatinine (CRE), total cholesterol (T-CHO), triglyceride (TG), low density lipoprotein cholesterol (LDL-CHO), high density lipoprotein cholesterol (HDL-CHO), total protein (TP), albumin (ALB) and total bilirubin (BIL) in serum. Hepatic parameters monitored were levels of cholesterol (CHO), triglyceride (TG), and malondialdehyde (MDA) and activities of cytochrome P450 (CYP), NADPH-CYP reductase, superoxide dismutase (SOD), catalase (CAT), glutathione (GSH), glutathione S-transferase (GST), glutathione reductase (GR), and glutathione peroxidase (GPx). The histopathological examination showed that the treatment of Onchengyeum and curcumin relieved the ballooning degeneration of hepatocytes which had been generated by $CCI_4$. The results suggested that hepatoprotective effects of Onchengyeum and curcumin possibly are due to their promising antioxidative activity.
Keywords
Onchengyeum, curcumin; free radical; lipid peroxidation; hepatotoxicity;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Aebi, H. (1974). Catalase Methods of Enzymatic analysis. 3rd ed, Verlag. Chemie. 2, 673-684
2 Ahmed, R.S., Seth, V., Banerjee, B.D. (2000). Influence of dietary ginger (Zingiber officinales Rose) on antioxidant defense system in rat: comparison with ascorbic acid. Indian J Exp BioI 38, 604-606
3 Antebi, H., Ribiere, C., Sinaceur, J., Abu-Murad, C., Nordmann, R. (1984). Involvement of oxygen radicals in ethanol oxidation and in the ethanol-induced decrease in liver glutathion. in : Bors, W., Saranm, M., Tait, D., eds. Oxygen Tadicals in Chemistry and Biology. New york., p.757-760
4 Carlberg, I., Mannervik, B. (1985). Glutathione reductase. Methods Enzymol. 113, 484-490   DOI
5 Comporti, M. (1993). Lipid peroxidation : An overview. In : Free Radicals: From Basic Science to Medicine(Molecular and cell biology updates), Poli, G, Albano, E., Dianzani, M.U. eds. Birkhause Verlag, Basel. Switzerland. p.65-79
6 Freidovich, I. (1999). Fundamental aspects of reactive oxygen species, or what's the matter with oxygen? Ann. NY. Acad. Sci. 893, 13-18   DOI
7 Fridovich, I. (1995). Xanthine Oxidase, CRC handbook of methods for oxygen radical research. CRC Press. New york
8 Habig, W.H., Pabst, M.J., Jakoby, W.B. (1974). Glutathione Stransferases. The first enzymatic step in mercapturic acid formation. J. BioI. Chem. 249, 7130-7139
9 Ho, Y.S., Crapo, J.D. (1988). Isolation and characterization of complementary DNAs encoding human manganese-containing superoxide dismutase. FEBS Lett. 229, 256-260   DOI   ScienceOn
10 James, J.L., Moody, D.E., Chan, C.H., Smuckler, E.A. (1982). The phospholipids of the hepatic endoplasmic reticulum. Structural change in liver injury. Biochem. J. 206, 203-210   DOI
11 Koner, B.C., Banerjee, B.D., Ray, A. (1998). Organochlorine pesticide-induced oxidative stress and immune suppression in rats. Indian J. Exp. BioI. 36, 395-398
12 Koo, B.H. (1997). Lexicologic Doneuibogam. Korean dictionary research p.187, 192
13 Leu, T.H., Su, S.L., Chuang, Y.C., Maa, M.C. (2002). Direct .inhibitoryeffect -of curcumin on Src and focal adhesion kinase activity. Biochem. Pharmacol. 66, 2323-2331   DOI   ScienceOn
14 Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951) Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265-275
15 McCay, P.B., Lai, E.K., Poyer, J. L. (1984). Oxygen-and carboncentered free radical formation during carbon tetrachloride metabolism. J. Biochem. 254, 2135-2143
16 Poli, G, Albano, E., Dianzani, M.U. (1987). The role of lipid peroxidation in liver damage. Chem. Phys. Lipids. 45, 117-142   DOI   ScienceOn
17 Omura, T., Sato, R. (1964). The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature., II. Solubilization, purification, and properties. J. Biol. Chem. 239, 2370-2378
18 Oruc, E.O., Uner, N. (2000) Combined effects of 2,4-D and azinphosmethyl on antioxidant enzymes and lipid peroxidation in liver of Oreochromis niloticus. Comp Biochem Physiol C Toxicol Pharmacol. 127, 291-296
19 Park, S.S., Yeom, T.H., (1984). lecture of today's chinese(herb) medicine. Seoul Hanglim publishing company. p.185, 186, 204,507,518
20 Ray, A, Banerjee, B.D. (1998). Stress, free radicals and the immune response: modulation by drugs. Arch. Pharmacol. 358 (Suppl. 2), 739-744
21 Recknagel, R.O, Glende, Jr, E.A, Dolak, J.A, Waller, R.L. (1989) Mechanisms of carbon tetrachloride toxicity. Pharmacol. Ther. 43, 139-154   DOI   ScienceOn
22 Sies, H., Akerboom, T.P. (1984). Glutathione disulfide (GSSG) efflux from cells and tissues. Methods Enzymol 105, 445-451   DOI
23 Song, H.J. (1984). The effect of Hwangryonhaedoktang on the immune response to sheep red blood cells. Wonkwang Univ. Oriental Med. J. 2, 195-206
24 Strobel, H.W., Digman, J.D. (1978). Biological oxidations, microsomal, cytochrome P-450, and other hemoprotein systems, Methods in Enzymology: biomembrames, II. Academic press. New york p.89-96
25 David, R.M., Nerland, D.E. (1983). Induction of mouse liver glutathione S-transferase by ethanol. Biochem. Pharmacol. 32, 2809-2811   DOI   ScienceOn
26 Recknagel, R.O. (1967). Carbon tetrachloride hepatotoxicity. Pharmacol Rev. 19, 145-208
27 Ellman, G.L. (1959). Tissue sulfhydryl groups. Arch. Biochem. Biophys, 82, 70-77   DOI   ScienceOn
28 Piper J.T., Singhal S.S., Salameh M.S., Torman R.T., Awasthi Y.C., Awasthi S. (1998) Mechanisms of anticarcinogenic properties of curcumin: the effect of curcumin on glutathione linked detoxification enzymes in tat liver. Int. J. Biochem. Cell Biol. 30, 445-456   DOI   ScienceOn
29 Kaynar, H., Meral, M., Turhan, H., Keles, M., Celik, G., Akcay, F. (2005). Glutathione peroxidase, glutathione-S-transferase, catalase, xanthine oxidase, Cu-Zn superoxide dis mutase activities, total glutathione, nitric oxide, and malondialdehyde levels in erythrocytes of patients with small cell and non-small cell lung cancer. Cancer Lett. 227, 133-139   DOI   ScienceOn
30 Uchiyama, M., Mihara, M. (1978). Determination of malonaldehyde precursor in tissues by thiobarbituric acid test. Analytical Biochemistry. 86, 271-278   DOI   ScienceOn
31 McCord, J.M. (2000). The evolution of free radicals and oxidative stress. Am. J. Med. 108, 652-659   DOI   ScienceOn
32 Y. Sun. L. W. Oberley. (1996). Redox regulation of transcriptional activators. Free Rad. BioI. Med. 21, 335-348   DOI   ScienceOn
33 Niki, E. (1993). Antioxidant defenses in eukariotic cells: An Overview. In: Free radicals: From Basic Science to Medicine (Molecular and cell biology update), Poli, G, Albano, E., Dianzani, M.U. eds. Birkhauser Verlag, Vasel. Switzerland., p. 365-368
34 Nong, J.H. (1986). Reprinting with additions of manbunghoychun. Jungkukkukwonsukongsa. last volume p.83
35 Svingen, B.A, Buege, J.A, O'Neal, F.O., Aust, S.D. (1979). The mechanism of NADPH-dependent lipid peroxidation. The propagation of lipid peroxidation. J Biol. Chem. 254, 5892-5899
36 Tappel, A.L. (1978). Glutathione peroxidase and hydroperoxides. Methods Enrymol. 52, 506-513   DOI