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Molecular and Cellular Biochemistry

, Volume 125, Issue 1, pp 59–63 | Cite as

Effect of plumbagin on some glucose metabolising enzymes studied in rats in experimental hepatoma

  • R. Parimala
  • P. Sachdanandam
Article

Abstract

Plumbagin (5-hydroxy-2-methyl-1, 4-naphthoquinone) isolated from Plumbago zeylanica Linn, when administered orally, at a dosage of 4 mg/kg body weight induces tumour regression in 3-methyl-4-dimethyl aminoazobenzene (3Me-DAB) induced hepatoma in Wistar male rats. The purpose of this investigation was to identify the changes in the rate of glycolysis and gluconeogenesis in tumour-bearing rats and the effects of treatment with Plumbagin. The levels of certain glycolytic enzymes, namely, hexokinase; phosphoglucoisomerase; and aldolase levels increased (p<0.001) in hepatoma bearing rats, whereas they decreased in Plumbagin administered rats to near normal levels. Certain gluconeogenic enzymes, namely, glucose-6-phosphatase and fructose-1,6-diphosphatase decreased (p<0.001) in tumour hosts, whereas Plumbagin administration increased the gluconeogenic enzyme levels in the treated animals. These investigations indicate the molecular basis of the different biological behaviour of 3MeDAB induced hepatoma and the anticarcinogenic property of Plumbagin against hepatoma studied in rats.

Key Words

Plumbagin glycolysis gluconeogenesis hepatoma 

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References

  1. 1.
    Mohana K, Purushothaman KK: Plumbagin: A study of its anticancer, antibacterial and antifungal properties. Indian J Exp Biol 18:876–877, 1980Google Scholar
  2. 2.
    Namboodiri CNT: Natural products for the treatment of cancer. Abstract presented in National Cancer Congress, Trivandrum, 1992Google Scholar
  3. 3.
    Dieterle H: A constituent ofDrosera rotundifolia. Scientia Pharm 9:121–122, 1938Google Scholar
  4. 4.
    Bygrave FL: Mitochondrial calcium transport and the regulation of metabolism by calcium in tumour cells. In: Criss WE, Ono T, Sabine JR (eds). Control mechanisms in cancer. New York, Raven Press, 411–423, 1976Google Scholar
  5. 5.
    Criss WE, Pradhan TK: Regulation of tumour cell metabolism by the adenylate and guanylate energy changes. In: Criss WE, Ono T, Sabine JR (ed). Control mechanisms in cancer. New York, Raven Press, 401–410, 1970Google Scholar
  6. 6.
    Gold J: Cancer cachexia and gluconeogenesis. Ann NY Acad Sci 230:103–110, 1974Google Scholar
  7. 7.
    Stein TP: Cachexia, gluconeogenesis and progressive weight loss in cancer patients. J Theor Biol 73:51–59, 1978Google Scholar
  8. 8.
    Waterhouse C, Jeanpetre N, Keilson, J: Gluconeogenesis from alanine in patients with progressive malignant disease. Cancer Res 39, 1968Google Scholar
  9. 9.
    Lundholm K, Edstrom S, Karlberg I, Ekman L, Schersten T: Glucose turnover, gluconeogenesis from glycerol and estimation of net glucose cycling in cancer patients. Cancer 50:1142–1146, 1982Google Scholar
  10. 10.
    Holroyde CP, Reichard GA: Carbohydrate metabolism in cancer cachexia. Cancer Treat Rep (Suppl 5) 65:55–60, 1981Google Scholar
  11. 11.
    Harris Busch: An Introduction to the biochemistry of the cancer cell. Academic Press, New York, pp 313–346, 1962Google Scholar
  12. 12.
    Shatton J, Donnelly AJ, Weinhouse S: Metabolism of neoplastic tissues XVI. Glucokinase activity and glycogen levels during hepatocarcinogenesis by azo dyes. Cancer Res 22:1372–1380, 1962Google Scholar
  13. 13.
    Lowry OH, Rosenbrough NJ, Farr AI, Randall RJ: Protein determination using Folin ciocalteau reagent. J Biol Chem 193:265–275, 1951Google Scholar
  14. 14.
    King J. In: ‘Practical clinical enzymology’; D Van Nostrand Co, London, pp 363, 1965Google Scholar
  15. 15.
    Fiske CH, Subbarow Y: The colorimetric determination of phosphorus. J Biol Chem 66:375–400, 1925Google Scholar
  16. 16.
    Gancedo JM, Gancedo C: Fructose 1,6-diphosphatase, phosphofructokinase and glucose-6-phosphate dehydrogenase from fermenting and non-fermenting yeasts. Arch Microbiol 76:132–138, 1971Google Scholar
  17. 17.
    Branstrup N, Kirk JE, Bruni C: Hexokinase and phosphoglucoisomerase activities of aortic and pulmonary artery tissue in individuals of various ages. J Greontol 12:166–170, 1957Google Scholar
  18. 18.
    Sasaki T, Matsui S, Sanae A: Effect of acetic acid concentration on the color reaction in the o-toluidine boric acid method for blood glucose estimation. Rinsho Kagaku 1:346–353, 1972Google Scholar
  19. 19.
    Horrocks JE, Ward J, King J: A routine method for the determination of phosphoglucoisomerase activity in body fluid. J Clin Pathol 16:248–252, 1963Google Scholar
  20. 20.
    Weber G, Lea MA: The molecular correlation concept of neoplasia. Advances in Enzyme Regulation 4:115–145, 1966Google Scholar
  21. 21.
    Weinhouse S: Glycolysis, respiration and enzyme deletions in slow-growing hepatic tumours. In: Gann Monograph 1, Japanese Cancer Association. pp 99–116, 1966Google Scholar
  22. 22.
    Ashmore J, Sweeney MJ, Morris MP, Weber G: Change from liver — type to muscle — type fructose metabolism in hepotamas. Biochim Biophys Acta 71:451–453, 1963Google Scholar
  23. 23.
    Weber G, Morris HP, Love WC, Ashmore J: Hepatomas (II) isotope studies of carbohydrate metabolism in Morris hepatoma 5123. Cancer Res 21:1406–1411, 1961Google Scholar
  24. 24.
    Sweeney MJ, Ashmore J, Morris HP, Weber G: Change from liver — type to muscle — type fructose metabolism in hepatomas. Cancer Res 23:995–1002, 1963Google Scholar
  25. 25.
    Weber G: Behaviour of liver enzymes during hepatocarcinogenesis. Advances in Cancer Research 6:403–494, Academic Press, New York, 1961Google Scholar
  26. 26.
    Weber G, Banerjee G, MorrisHP: Comparative biochemistry of hepatomas (I) carbohydrate enzymes in Morris hepatoma 5123. Cancer Res 21:933–937, 1961Google Scholar
  27. 27.
    Weber G, Morris HP: Comparative biochemistry of hepatomas III. Carbohydrate enzymes in liver tumours of different growth rates. Cancer Res 23:987–994, 1963Google Scholar
  28. 28.
    Takafumi MD, Toshio Kitagawa MC: Anticancer drug screening test with LDH in Nude mouse bearing bone and soft part sarcoma. Cancer 56:1112–1116, 1985Google Scholar

Copyright information

© Kluwer Academic Publishers 1993

Authors and Affiliations

  • R. Parimala
    • 1
  • P. Sachdanandam
    • 1
  1. 1.Department of Medical Biochemistry, Dr.A.L.M.P-G.I.B.M.S.University of MadrasMadrasIndia

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