Natural Product Sciences

  • 제10권4호
  • /
  • Pages.190-195
  • /
  • 2004
  • /
  • 1226-3907(pISSN)
  • /
  • 2288-9027(eISSN)
한국생약학회 (The Korean Society of Pharmacognosy)
권호 표지

Anticancer Potency of Terminalia arjuna Bark on N-nitrosodiethylamine-Induced Hepatocellular Carcinoma in Rats

  • Sivalokanathan, Sarveswaran (Department of Pharmacology and Environmental Toxicology, Dr. ALM Post-Graduate Institute of Basic Medical Sciences, University of Madras) ;
  • Ilayaraja, Muthaiyan (Department of Pharmacology and Environmental Toxicology, Dr. ALM Post-Graduate Institute of Basic Medical Sciences, University of Madras) ;
  • Balasubramanian, Maruthaiveeran Periyasamy (Department of Pharmacology and Environmental Toxicology, Dr. ALM Post-Graduate Institute of Basic Medical Sciences, University of Madras)
  • 발행 : 2004.08.31
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

The anticancer potency of the ethanolic extract of Terminalia arjuna on N-nitrosodiethylamine (DEN) induced hepatocellular carcinoma in Wistar albino rats was studied. Single intraperitoneal injection of DEN was administrated to induce liver cancer. After two weeks, phenobarbital (PB) was given orally for fourteen weeks to promote the cancer. The cancer bearing animals treated with ethanolic extract of T.arjuna (400 mg/kg body weight) for 28 days. Nucleic acids such as deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) were estimated in liver and kidney of control and experimental animals. Certain marker enzymes viz, alanine aminotransaminase (ALT), aspartate aminotransaminase (AST), acid phosphatase (ACP), alkaline phosphatase (ALP), 5'-nucleotidase (5'ND) and lactate dehydrogenase (LDH) were assayed in serum, liver and kidney of control and experimental animals. The levels of DNA and RNA were significantly increased in cancer bearing animals. The activities of ALT, AST, ACP, ALP, 5'ND, and LDH were significantly (P<0.001) increased in serum of cancer bearing animals. On the other hand, the levels of ALT, AST were decreased (P<0.001) and ACP, ALP, 5'ND, and LDH were significantly increased (P<0.001) in liver and kidney. These changes were reversed to near normal in drug treated animals. These observations suggest that the ethanolic extract of T.arjuna possess anticancer activity.

키워드

참고문헌

  1. Bone, K., Clinical applications of Ayurvedic and Chinese herbs, Warwick, Queensland Australia: Phytotherapy Press, pp. 131-3 (1996)
  2. Burton, K., A study of the conditions and mechanisms of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem. J., 62, 315-323 (1956)
  3. Caius, J.F., Mhasker, K.S., and Issac., M., Ind. Med. Res. Memoirs., 16, 51 (1930)
  4. Chopra, R.N. and Ghosh, B.N., Ind. Med. Gaz., 64, 70 (1929)
  5. Chopra, R.N., Chopra, I.C. Handa, K.L., and Kapoor, L.D.,Indigenous Drugs of India, 421,U.N.Dhar and sons Pvt. Ltd., Calcutta, India (1958)
  6. Chopra, R.N., Nagar, S.L., and Chopra, I.C., GIossary of Indian Medicinal Ptants, 241, CSIR Publications. New Delhi, India (1956)
  7. Dao, T.L., IP, C., and Pater, J., Serum sialyl transferase and 5'-nucleotidase as reliable biomarker in women with breast cancer. J. Natl. Cancer. Inst., 65, 529-534 (1980)
  8. Dixit, R. and Gold, B., Inhibition of N-methyl-N-nitrosourea-induced mutagenicity and DNA methylation by ellagic acid., Proc. Natl. Acad. Sci. USA., 83, 8039-8043 (1986) https://doi.org/10.1073/pnas.83.21.8039
  9. Drotman, R.B. and Lawhorn, G.T, Serum enzymes as indicators of chemical induced liver damage. Drug. Chem. Toxicol., 1, 163-171 (1978) https://doi.org/10.3109/01480547809034433
  10. Gupta, M., Mazumder, U.K. and Kumar, R.S., Hepatoprotective effects and antioxidant role of Caesatpinia bonducella on paracetamol-induced hepatic damage in rats. Nat. Prod. Sci., 9, 186-191 (2003)
  11. Hartwell, J.L., Ptants used against cancer, Lawrence (MA): Quarterman Publication, Inc (1982)
  12. Helmes, M.H., Modia, A., Abd, El-Moneim, Moustafe, M.S., Abd EL-Balc, and Safinoz, M.E.L. Clinical value of serum LDH, Ceruloplasmin, cathepsin-D and lipid bound malignant lymphomas. Med. Sci. Res., 26, 613-617 (1998)
  13. Hidvegi, M., Raso, E., Tomoskozi-Farkas, R., Pauk, S., Lapis, K., and Szende, B., Effect of Avemar and Avemar + vitamin C on tumor growth and metastasis in experimental animals. Anticaner. Res., 18, 2353-2358 (1998)
  14. Huang M.T, Wood, A.W., Newmark, H.L, Sayer, J.M., Yagi, H., Jerina, D.M., and Conney, A.H., Inhibition of the mutagenicity of Bay region diol epoxides of polycyclic aromatic hydrocarbons by phenolics plant flavonoids. Carcinogenesis., 4, 1631-8. (1983) https://doi.org/10.1093/carcin/4.12.1631
  15. Kadem, L., Siest, G., and Magdalou, J., Differential toxicity of aflatoxin $B_1$, in male and female rats, relationship with hepatic drug metabolizing enzymes. Biochem. Pharmacol., 31, 3057-62 (1982) https://doi.org/10.1016/0006-2952(82)90080-6
  16. Kapoor, L.D., Handbook of Ayurvedic medicinal plant, Boca Raton (FL): CRC Press, pp. 319-20 (1990)
  17. Kaur, S.J., Grover, I.S., and Kumar, S., Modulatory effects of tannin fraction isolated from Terminalia arjuna on the genotoxicity of mutagens in Salmonella typhimurium. Food. chem. Toxi., 38, 1113-1119 (2000) https://doi.org/10.1016/S0278-6915(00)00104-6
  18. King, J., The transferase-alanine and aspertate transaminase, In: Practical clinical enzymology, Ed. by Van D. Nostrand Co. Ltd., London, pp. 121-138 (1965a)
  19. King, J., The transferase-alanine and aspertate transaminase, In: Practical clinical enzymology, Ed. by Van D. Nostrand Co. Ltd., London, pp. 121-138 (1965a)
  20. King, J., The dehydrogenases or oxido reductase-lactase dehy-drogenase. In: Practical clinical Enzymology Ed. by Van D. Nostand Co. Ltd., London, pp. 83-93 (1965c)
  21. Laconi, S., Pani. P., Pillai, S., Pasciu, D., Sarma, D.S., and Laconi, E.A., A growth constrained environment drives tumor progression in vivo. Proc. NatI. Acad. Sci. U.S.A., 98, 7806-7811 (2001) https://doi.org/10.1073/pnas.131210498
  22. Lippert, M., Papadopoulos, N., and Javadpour, N.R., Role of lactate dehydrogenase isoenzymes in testicular cancer. Uroloey., 18, 50-53 (1981) https://doi.org/10.1016/0090-4295(81)90495-7
  23. Luly, P., Barnabei, 0., and Tria, E., Hormonal control in vitro of plasma membrane bound $Na^+$, $K^+$-ATPase of rat liver. Biochemica. Biophysica. Acta., 282, 447-452 (1972) https://doi.org/10.1016/0005-2736(72)90352-5
  24. Massey, W.H., Dennis, C.L., Flatchen, W.S., and Wood, D.C., Lactic dehydrogenase alterations in malignant disease of the liver. Am. J. Surs., 122, 200 (1971)
  25. Mirmoni, M.H., Suzanger, M., Wise, A., Messripour, M., and Emami, H. Biochemical studies during AFB, induced liver damage in rats fed different levels of dietary protein, Int. J. Cancer, 24, 471-476 (1979)
  26. Moss, D.W. and Butterworth, P.J., Enzymology and Medicine. Pitman Medical, London, pp. 139 (1974)
  27. Nakashimhan, S., Schachter, H., and Rajalakshmi, S., Expression of N-acetylglucosaminyltransferase III in hepatic nodules during rat liver carcinogenesis. The promote by orotic acid. J. Biol. Chem., 263, 1273-1281 (1988)
  28. Pain, V.M., Randall, D.R, and Garlick, P.J., Protein synthesis in liver and skeletal muscle of mice bearing an ascites tumour.Cancer. Res., 44, 1054-1057 (1984)
  29. Rawal, U.M., Patel, U.S., Rao, G.N., and Desai, R.R., Clinical and biochemical studies on cateractous human lens III. Quantitative study of protein, RNA and DNA. Arogya. J. Health. Sci., 3, 69-72 (1977)
  30. Rocken, C. and Carl-Mc Grath, S., Pathology and pathogenesis of hepatocellular carcinoma. Dig. Dis., 19, 269-278 (2001) https://doi.org/10.1159/000050693
  31. Schneider, W.C., Determination of nucleic acid in tissues, In: Methods in enzymology, Colowick, S.P. and Kaplan, N.O (eds) vol III, Academic press, New york, pp. 680-684 (1957)
  32. Starkweather, W.H., Green, R.A., Spencer, H.H., and Schock, H.K., Alterations of serum lactate dehydrogenase isoenzymes during therapy directed at lung cancer. J. Lab. Clin. Med., 68, 314-323 (1966)
  33. Sumitra, M., Manikandan, P, Kumar, D.A, Arutselvan, N., Balaknshna, K., Manohar, B.M., and Puvanaknshnan, R., Experimental myocardial necrosis in rats: Role of arjunolic acid on platelet aggregation, coagulation and antioxidant status. Mol. Cell. Biochem., 224, 135-142 (2001) https://doi.org/10.1023/A:1011927812753
  34. Teo E.K. and Fock, K.M., Hepatocellular carcinoma: An Asian Perspective. Dig. Dis., 19, 263-268 (2001) https://doi.org/10.1159/000050692
  35. Tessitore, L., Bonelli, G., and Baccino, F.M. Early development of protein metabolic perturbations in the liver and skeletal muscle of tumour bearing rats. Biochem. J., 241, 153-159 (1987)
  36. Thabrew, M.I., Joice, P.D.T.M., and Rajatissa, W.A., Comparative study of the efficacy of Paetta indica and Osbeckia octandra in the treatment of liver dysfunction. Planta Medica., 53, 239-241 (1987) https://doi.org/10.1055/s-2006-962691
  37. The Wealth of India, Raw Materials, CSIR, New Delhi, 10 (1976)
  38. Walia, M., Maharajan, M., and Singh, K. Serum adenosine deaminase, 5'-nucleotidase and alkaline phosphatase in breast cancer patients. Ind. J. Med. Res., 101, 247-249 (1995)