Cancer Letters
Volume 224, Issue 1 , Pages 67-80 , 16 June 2005

Remission of hepatocellular carcinoma with arginine depletion induced by systemic release of endogenous hepatic arginase due to transhepatic arterial embolisation, augmented by high-dose insulin: arginase as a potential drug candidate for hepatocellular carcinoma

  • P.N.M. Cheng

      Affiliations

    • Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, China
    • The Hong Kong Sanatorium and Hospital, Happy Valley, Hong Kong, China
    • Corresponding Author InformationCorresponding author. Address: Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, China. Tel.: +852 28686813; fax: +852 28453906.
    • ,
  • Y.C. Leung

      Affiliations

    • Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, China
    • ,
  • W.H. Lo

      Affiliations

    • Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, China
    • ,
  • S.M. Tsui

      Affiliations

    • Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, China
    • ,
  • K.C. Lam

      Affiliations

    • The Hong Kong Sanatorium and Hospital, Happy Valley, Hong Kong, China

Received 2 September 2004 ,Accepted 20 October 2004.

References 

  1. Wheatley DN, Campbell E. Arginine catabolism, liver extracts and cancer. Pathol. Oncol. Res. 2002;8:18–25
  2. Barbul A. Arginine: biochemistry, physiology, and therapeutic implications. JPEN J. Parenter. Enteral. Nutr. 1986;10:227–238
  3. Wu G, Morris SM. Arginine metabolism: nitric oxide and beyond. Biochem. J. 1998;15:1–17
  4. Hoogenraad N, Totino N, Elmer H, Wraight C, Alewood P, Johns RB. Inhibition of intestinal citrulline synthesis causes severe growth retardation in rats. Am. J. Physiol. 1985;249:G792–G799
  5. Schimke RT. Enzymes of arginine metabolism in mammalian cell culture. I. Repression of argininosuccinate synthetase and argininosuccinase. J. Biol. Chem. 1964;239:136–145
  6. Scott L, Lamb J, Smith S, Wheatley DN. Single amino acid (arginine) deprivation: rapid and selective death of cultured transformed and malignant cells. Br. J. Cancer. 2000;83:800–810
  7. Storr JM, Burton AF. The effects of arginine deficiency on lymphoma cells. Br. J. Cancer. 1974;30:50–59
  8. Savoca KV, Davis FF, van Es T, McCoy JR, Palczuk NC. Cancer therapy with chemically modified enzymes. II. The therapeutic effectiveness of arginase, and arginase modified by the covalent attachment of polyethylene glycol, on the taper liver tumor and the L5178Y murine leukemia. Cancer Biochem. Biophys. 1984;7:261–268
  9. Harris JM, Martin NE, Modi M. Pegylation: a novel process for modifying pharmacokinetics. Clin. Pharmacokinet. 2001;40:539–551
  10. Harris JM, Chess RB. Effect of pegylation on pharmaceuticals. Nat. Rev. Drug Discov. 2003;2:214–221
  11. Lieberman I, Ove P. Inhibition of growth of cultured mammalian cells by liver extracts. Biochim. Biophys. Acta. 1960;38:153
  12. Bach SJ, Swaine D. The effect of arginase on the retardation of tumour growth. Br. J. Cancer. 1965;19:379–386
  13. Holley RW. Evidence that a rat liver ‘inhibitor’ of the synthesis of DNA in cultured mammalian cells is arginase. Biochim. Biophys. Acta. 1967;145:525–527
  14. Nelson JA, Carpenter JW, Morris HP. Growth inhibitory and arginase activities in liver and hepatoma extracts. Proc. Soc. Exp. Biol. Med. 1975;149:900–902
  15. Terayama H, Koji T, Kontani M, Okumoto T. Arginase as an inhibitory principle in liver plasma membranes arresting the growth of various mammalian cells in vitro. Biochim. Biophys. Acta. 1982;720:188–192
  16. Dillon BJ, Holtsberg FW, Ensor CM, Bomalaski JS, Clark MA. Biochemical characterization of the arginine degrading enzymes arginase and arginine deiminase and their effect on nitric oxide production. Med. Sci. Monit. 2002;8:BR248–BR253
  17. Ikemoto M, Tsunekawa S, Awane M, Fukuda Y, Murayama H, Igarashi M, et al. A useful ELISA system for human liver-type arginase, and its utility in diagnosis of liver diseases. Clin. Biochem. 2001;34:455–461
  18. Ikemoto M, Tsunekawa S, Toda Y, Totani M. Liver-type arginase is a highly sensitive marker for hepatocellular damage in rats. Clin. Chem. 2001;47:946–948
  19. Kimura M, Tatsumi KI, Tada H, Ikemoto M, Fukuda Y, Kaneko A, et al. Amino N, enzyme immunoassay for autoantibodies to human liver-type arginase and its clinical application. Clin. Chem. 2000;46:112–117
  20. Ikemoto M, Tsunekawa S, Tanaka K, Tanaka A, Yamaoka Y, Ozawa K, et al. Liver-type arginase in serum during and after liver transplantation: a novel index in monitoring conditions of the liver graft and its clinical significance. Clin. Chim. Acta. 1998;271:11–23
  21. Wakabayashi H, Ushiyama T, Ishimura K, Izuishi K, Karasawa Y, Masaki T, et al. Significance of reduction surgery in multidisciplinary treatment of advanced hepatocellular carcinoma with multiple intrahepatic lesions. J. Surg. Oncol. 2003;82:98–103
  22. Ryu M, Shimamura Y, Kinoshita T, Konishi M, Kawano N, Iwasaki M, et al. Therapeutic results of resection, transcatheter arterial embolization and percutaneous transhepatic ethanol injection in 3225 patients with hepatocellular carcinoma: a retrospective multicenter study. Jpn. J. Clin. Oncol. 1997;27:251–257
  23. Pisters PW, Cersosimo E, Rogatko A, Brennan MF. Insulin action on glucose and branched-chain amino acid metabolism in cancer cachexia: differential effects of insulin. Surgery. 1992;111:301–310
  24. S. Tepic, P. Pyk, Therapeutic compositions for treatment of cancer, PCT Patent, No. WO 98/06421, 19 Feb 1998.
  25. Takaku H, Takase M, Abe S, Hayashi H, Miyazaki K. In vivo anti-tumor activity of arginine deiminase purified from Mycoplasma arginini. Int. J. Cancer. 1992;51:244–249
  26. Sugimura K, Fukuda S, Wada Y, Taniai M, Suzuki M, Kimura T, et al. Identification and purification of arginine deiminase that originated from Mycoplasma arginini. Infect. Immun. 1990;58:2510–2515
  27. Izzo F, Marra P, Beneduce G, Castello G, Vallone P, de Rosa V, et al. Pegylated arginine deiminase treatment of patients with unresectable hepatocellular carcinoma: results from phase I/II studies. J. Clin. Oncol. 2004;22:1815–1822
  28. Curley SA, Bomalaski JS, Ensor CM, Holtsberg FW, Clark MA. Regression of hepatocellular cancer in a patient treated with arginine deiminase. Hepatogastroenterology. 2003;50:1214–1216
  29. Takaku H, Misawa S, Hayashi H, Miyazaki K. Chemical modification by polyethylene glycol of the anti-tumor enzyme arginine deiminase from Mycoplasma arginini. Jpn. J. Cancer Res. 1993;84:1195–1200
  30. Takaku H, Matsumoto M, Misawa S, Miyazaki K. Anti-tumor activity of arginine deiminase from Mycoplasma argini and its growth-inhibitory mechanism. Jpn. J. Cancer Res. 1995;86:840–846
  31. Philip R, Campbell E, Wheatley DN. Arginine deprivation, growth inhibition and tumour cell death: 2. Enzymatic degradation of arginine in normal and malignant cell cultures. Br. J. Cancer. 2003;88:613–623
  32. Ensor CM, Holtsberg FW, Bomalaski JS, Clark MA. Pegylated arginine deiminase (ADI-SS PEG20,000 mw) inhibits human melanomas and hepatocellular carcinomas in vitro and in vivo. Cancer Res. 2002;62:5443–5450

PII: S0304-3835(04)00879-1

doi: 10.1016/j.canlet.2004.10.050

Cancer Letters
Volume 224, Issue 1 , Pages 67-80 , 16 June 2005

Article Tools

* Image Usage & Resolution