Skip to main content
SpringerLink
Log in
Book cover

Chemotherapy pp 457–487Cite as

Enzyme Therapy

  • Chapter

Part of the book series: Cancer ((C,volume 5))

Abstract

Most chemotherapeutic agents function either by depriving cells of an adequate quantity of metabolic precursors, e.g., purine, pyrimidine, and folate antagonists, or by modifying the structures of existing cellular components, e.g., alkylating and intercalating agents. Enzymes have been used in experimental therapeutic trials following these same mechanistic principles. Asparaginase, glutaminase, arginase, methioninase, ß-tyrosinease, phenylalanine ammonia lyase, xanthine oxidase, and a folic-acid-degrading enzyme (carboxypeptidase G) have been used to deprive cells of metabolic precursors, while DNase, RNase, neuraminidase, proteolytic enzymes, abrin, ricin, and diphtheria toxin have been used to modify existing cellular components. Enzymes differ from other chemotherapeutic agents, however, in that their macromolecular nature probably restricts their cellular permeability and consequently their accessibility to substrates. This very macromolecular nature enables enzymes to demonstrate a high degree of substrate specificity that can be very useful in restricting their cytotoxicity toward specific tissues, e.g., asparaginase therapy of asparagine-dependent leukemia cells.

This is a preview of subscription content, log in via an institution.

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   39.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Abell, C. W., Stith, W. J., and Hodgkins, D. S., 1972, The effects of phenylalanine ammonia-lyase on leukemic lymphocytes in vitro, Cancer Res. 32: 285.

    PubMed  CAS  Google Scholar 

  • Abell, C. W., Hodgkins, D. S., and Stith, W. J., 1973, An in vivo evaluation of the chemotherapeutic potency of phenylalanine ammonia-lyase, Cancer Res. 33: 2529.

    PubMed  CAS  Google Scholar 

  • Adamson, R. H., and Fabro, S., 1968, Antitumor activity and other biologic properties of L-asparaginase (NSC-109229)—a review, Cancer Chemother. Rep. 52 (6): 617.

    PubMed  CAS  Google Scholar 

  • Arnon, R., and Neurath, H., 1970, Immunochemical studies on bovine trypsin and trypsinogen derivatives, Immunochemistry 7: 241.

    Article  PubMed  CAS  Google Scholar 

  • Ashworth, L. A. E., and Maclennan, A. P., 1974, Comparison of the L-asparaginases from Escherichia coli and carotovora as immunosuppressants, Cancer Res. 34: 1353.

    PubMed  CAS  Google Scholar 

  • Astaldi, G., 1972, Is L-asparaginase an antiblastic agent? Haematologia 6: 433.

    PubMed  CAS  Google Scholar 

  • Astaldi, G., Burgio, G. R., Krc, J., Genova, R., and Astaldi, A. A., Jr., 1969, L-Asparaginase and blastogensis, Lancet 1: 423.

    Article  PubMed  CAS  Google Scholar 

  • Baechtel, F. S., Gregg, D. E., and Prager, M. D., 1976, The influence of glutamine, its decomposition products, and glutaminase on the transformation of human and mouse lymphocytes, Biochim. Biophys. Acta 421: 33.

    Article  PubMed  CAS  Google Scholar 

  • Bartholeyns, J., and Baudhuin, P., 1976, Inhibition of tumor cell proliferation by dimerized ribonuclease, Proc. Natl. Acad. Sci. U.S.A. 73: 573.

    Article  PubMed  CAS  Google Scholar 

  • Becker, F. F., and Broome, J. D., 1967, L-Asparaginase: Inhibition of early mitosis in regenerating rat liver, Science 156: 1602.

    Article  PubMed  CAS  Google Scholar 

  • Beerman, T. A., and Goldberg, I. H., 1974, DNA strand scission by the antitumor protein neocarzinostatin, Biochem. Biophys. Res. Commun. 59: 1254.

    Article  PubMed  CAS  Google Scholar 

  • Bekesi, J. G., Holland, J. F., Cuttner, J., Silver, R., Coleman, M., Jarowski, C., and Vinceguerra, V., 1976, Immunotherapy in acute myelocytic leukemia (AML) with neuraminidase (N’ASE) treated allogenic myeloblasts with or without MER, Proc. Amer. Assoc. Cancer Res. 35: 184.

    Google Scholar 

  • Bergel,-F., 1961, Chemistry of Enzymes in Cancer, pp. 65–70, Charles C Thomas, Springfield, Illinois.

    Google Scholar 

  • Bernard, J., Boiron, M., Jacquillat, C., Weil, M., and Levy D. (eds.), 1970, La L-Asparaginase, Editions du Centre National de la Recherche Scientifique, Paris.

    Google Scholar 

  • Bertino, J. R., Skeel, R., Makulu, D., Mcintosh, S., Uhoch, J., and Chabner, B., 1974, Initial clinical studies with carboxypeptidase G, (CPG,): A folate depleting enzyme, Clin. Res. 22: 483a.

    Google Scholar 

  • Bettigole, R. E., Himelstein, E. S., Oettgen, H. F., and Clifford, G. O., 1970, Hypofibrinogenemia due to L-asparaginase: Studies of fibrinogen survival using autologous “’I-fibrinogen, Blood 35: 195.

    PubMed  CAS  Google Scholar 

  • Betz, J. L., Brown, P. R., Smyth, M. J., and Clarke, P. H., 1974, Evolution in action, Nature (London) 247: 261.

    Article  CAS  Google Scholar 

  • Blumberg, N., 1974, Tumor angiogenesis factor: Speculations on an approach to cancer chemotherapy, Yale J. Biol. Med. 47: 71.

    PubMed  CAS  Google Scholar 

  • Bosmann, H. B., 1972, Antineoplastic drug activity in the mitotic cycle—effects of six agents on macromolecular synthesis in synchronous mammalian leukemic cells, Biochem. Pharmacol. 21: 1977.

    Google Scholar 

  • Boyer,H. W., 1974, Restriction and modification of DNA: Enzymes and substrates, Fed. Proc. Fed. Amer. Soc. Exp. Biol.33:1125.

    Google Scholar 

  • Broome, J. D., 1963a, Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. I. Properties of the L-asparaginase of guinea pig serum in relation to those of the antilymphoma substance, J. Exp. Med. 118: 99.

    Article  PubMed  CAS  Google Scholar 

  • Broome, J. D., 1963b, Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. II. Lymphoma 6C3HED cells cultured in a medium devoid of L-asparagine lose their susceptibility to the effects of guinea pig serum in vivo, J. Exp. Med. 118: 121.

    Article  PubMed  CAS  Google Scholar 

  • Burchenal, J. H., Clarkson, B. D., Dowling, M. D., Gee, T., Haghbin, M., and Tan, C. T. C., 1970, Experimental and clinical studies of L-asparaginase in combination therapy, in: La L-Asparaginase ( J. Bernard, M. Boiron, C. Jacquillat, M. Weil, and D. Levy, eds.), pp. 243–248, Editions de Centre National de la Recherche Scientifique, Paris.

    Google Scholar 

  • Burns, R. 0., 1971, L-Threonine deaminase—biosynthetic (Salmonella typhimurium), in: Methods in Enzymology (H. Tabor and C. W. Tabor, eds.), Vol. 17B, pp. 555–560, Academic Press, New York.

    Google Scholar 

  • Buzzi, S., and Maistrello, I., 1973, Inhibition of growth of Ehrlich tumors in Swiss mice by diphtheria toxin, Cancer Res. 33: 2349.

    PubMed  CAS  Google Scholar 

  • Capizzi, R. L., 1975, Improvement in the therapeutic index of L-asparaginase by methotrexate, Cancer Chemother. Rep. 6 (3): 37.

    CAS  Google Scholar 

  • Capizzi, R. L., Bertino, J. R., and Handschumacher, R. E., 1970, L-Asparaginase, Annu. Rev. Med. 21: 433.

    Article  PubMed  CAS  Google Scholar 

  • Capizzi, R. L., Summers, W. P., and Bertino, J. R., 1971, L-Asparaginase induced alteration of methotrexate activity in mouse leukemia L5178Y, Ann. N. Y. Acad. Sci. 186: 302.

    Article  PubMed  CAS  Google Scholar 

  • Capizzi, R., Castro, 0., Aspnes, G., Bobrow, S., Bertino, J., Finch, S., and Pearson, H., 1974, Treatment of acute lymphocytic leukemia (ALL) with intermittent high dose methotrexate (MTX) and asparaginase, Proc. Amer. Assoc. Cancer Res. 15: 182.

    Google Scholar 

  • Chabner, B. A., Chello, P. L., and Bertino, J. R., 1972a, Antitumor activity of a folate-cleaving enzyme, carboxypeptidase G1, Cancer Res. 32: 2114.

    PubMed  CAS  Google Scholar 

  • Chabner, B. A., Johns, D. G., and Bertino, J. R., 1972b, Enzymic cleavage of methotrexate provides a method for prevention of drug toxicity, Nature (London) 239: 395.

    Article  CAS  Google Scholar 

  • Chang, P. K., 1976, O-L-Homoserine-5’-adenylate (USAMP). Esterification of 5’-adenylic acid with the gamma-hydroxyl group of L-homoserine, in: Synthetic Procedures in Nucleic Acid Chemistry, Vol. III ( L. Townsend, ed.), John Wiley and Sons, New York.

    Google Scholar 

  • Chang, T. M. S., 1971, The in vivo effects of semipermeable microcapsules containing L-asparaginase on 6C3HED lymphosarcoma, Nature (London) 229: 117.

    Article  CAS  Google Scholar 

  • Chen, L. F., and Richardson, T., 1974, Enzyme derivatives containing reactive groups. Immobilization of alpha-amylase on human erythrocytes, Pharmacol. Res. Commun. 6: 273.

    Article  PubMed  CAS  Google Scholar 

  • Chong, E. O. S., and Chang, T. M. S., 1974, In vivo effects of intraperitoneally injected Lasparaginase solution and L-asparaginase immobilized within semipermeable nylon microcapsules with emphasis on blood L-asparaginase, “body” L-asparaginase, and plasma L-asparagine levels, Enzyme 18: 218.

    CAS  Google Scholar 

  • Chou, T. C., and Handschumacher, R. E., 1972, Production of L-asparagine by tumor cells and the effect of asparagine analogs, Biochem. Pharmacol. 21: 39.

    Article  PubMed  CAS  Google Scholar 

  • Cooney, D. A., and Handschumacher, R. E., 1970, L-Asparaginase and L-asparagine metabolism, Annu. Rev. Pharmacol. 10: 421.

    Article  CAS  Google Scholar 

  • Cooney, D. A., and Rosenbluth, R. J., 1975, Enzymes as therapeutic agents, Adv. Pharmacol. Chemother. 12: 185.

    Article  PubMed  CAS  Google Scholar 

  • Cooney, D. A., Capizzi, R. L., and Handschumacher, R. E., 1970, Evaluation of L-asparagine metabolism in animals and man, Cancer Res. 30: 929.

    PubMed  CAS  Google Scholar 

  • Demopoulos, H. B., 1966a, Effects of low phenylalanine–tyrosine diets on S91 mouse melanomas, J. Natl. Cancer Inst. 37: 185.

    PubMed  CAS  Google Scholar 

  • Demopoulos, H. B., 1966b, Effects of reducing the phenylalanine–tyrosine intake of patients with advanced malignant melanoma, Cancer 19: 657.

    Article  PubMed  CAS  Google Scholar 

  • Deodhar, S. D., 1973, Enhancement of metastases by L-asparaginase in allogeneic and isogeneic mouse tumor systems, Adv. Exp. Med. Biol. 29: 519.

    PubMed  CAS  Google Scholar 

  • Distasio, J. A., and Niederman, R. A., 1976, Purification and characterization of L-asparaginase with antilymphoma activity from Vibrio succinogenes, J. Biol. Chem. 251: 6929.

    PubMed  CAS  Google Scholar 

  • Ellison, R. R., Karnofsky, D. A., Sternberg, S. S., Murphy, M. L., and Burchenal, J. H., 1954, Clinical trials of O-diazoacetyl-L-serine (azaserine) in neoplastic disease, Cancer 7: 801.

    Google Scholar 

  • Engasser, J.-M., and Horvath, C., 1976, Diffusion and kinetics with immobilized enzymes, in: Applied Biochemistry and Bioengineering, Vol. I (L. B. Wingard, Jr., E. Katzir-Katchalski, and L. Goldstein, eds.), pp. 127–220, Academic Press, New York.

    Google Scholar 

  • Feinstein, G., Bodlaender, P., and Shaw, E., 1969, The modification of essential carboxylic acid side chains of trypsin, Biochemistry 8: 4949.

    Article  PubMed  CAS  Google Scholar 

  • Foley, G. E., Barell, E. F., Adams, R. A., and Lazarus, H., 1969, Nutritional requirements of human leukemic cells. Cystine requirements of diploid cell lines and their heteroploid variants, Exp. Cell Res. 57: 129.

    Article  PubMed  CAS  Google Scholar 

  • Gerhart, J. C., and Schachman, H. K., 1965, Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase, Biochemistry 4: 1054.

    Article  PubMed  CAS  Google Scholar 

  • Gill, D. M., Pappenheimer, A. M., and Uchida, T., 1973, Diphtheria toxin, protein synthesis, and the cell, Fed. Proc. Fed. Amer. Soc. Exp. Biol. 32: 1508.

    CAS  Google Scholar 

  • Goldberg, A. I., Cooney, D. A., Glynn, J. P., Homan, E. R., Gaston, M. R., and Milman, H. A., 1973, The effects of immunization to L-asparaginase on antitumor and enzymatic activity, Cancer Res. 33: 256.

    PubMed  CAS  Google Scholar 

  • Goldstein, A., Aronow, L., and Kalman, S., 1974, Principles of Drug Action: The Basis of Pharmacology, p. 166, John Wiley and Sons, New York.

    Google Scholar 

  • Greenberg, D. M., and Sassenrath, E. N., 1953, Lack of effect of high potency arginase on tumor growth, Cancer Res. 13: 709.

    CAS  Google Scholar 

  • Grundmann, E., and Oettgen, H. F. (eds.), 1970, Experimental and Clinical Effects of L-Asparaginase, Springer-Verlag, New York—Heidelberg-Berlin.

    Google Scholar 

  • Gumprecht, J. G., and Wriston, J. C., 1973, Purification and partial sequencing of cyanogen bromide peptides from L-asparaginase of Escherichia coli, Biochemistry 12: 4869.

    Article  PubMed  CAS  Google Scholar 

  • Haddow, A., Lamirande, G. P., Bergel, F., Bray, R. C., and Gilbert, D. A., 1958, Antitumor and biochemical effects of purified bovine xanthine oxidase in C3H and C mice, Nature (London) 182: 1144.

    Article  CAS  Google Scholar 

  • Haley, E. E., Fischer, G. A., and Welch, A. D., 1961, The requirement for L-asparagine of mouse leukemia cells L5178Y in culture, Cancer Res. 21: 532.

    PubMed  CAS  Google Scholar 

  • Halpern, B. C., Clark, B. R., Hardy, D. N., Halpern, R. M., and Smith, R. A., 1974, The effect of replacement of methionine by homocystine on survival of malignant and normal adult mammalian cells in culture, Proc. Natl. Acad. Sci. U.S.A. 71: 1133.

    Article  PubMed  CAS  Google Scholar 

  • Han, T., and Ohnuma, T., 1972, L-Asparaginase: In vitro inhibition of blastogenesis by enzyme from Erwinia catotovora, Nature (London) New Biol. 239: 50.

    Article  CAS  Google Scholar 

  • Hare, L. E., and Handschumacher, R. E., 1973, Physical and biological properties of acetamidino-, f3dimethylaminopropionamidino-, and maleyl-L-asparaginase, Mol. Pharmacol. 9: 534.

    PubMed  CAS  Google Scholar 

  • Haskell, C. M., and Canellos, G. P., 1969, L-Asparaginase resistance in human leukemia—asparagine synthetase, Biochem. Pharmacol. 18: 2578.

    Article  PubMed  CAS  Google Scholar 

  • Haskell, C. M., Canellos, G. P., Leventhal, B. G., Carbone, P. P., Block, J. B., Serpick, A. A., and Selawry, O. S., 1969, L-Asparaginase: Effects in patients with neoplastic disease, N. Engl. J. Med. 281: 1028.

    Article  PubMed  CAS  Google Scholar 

  • Hayashi, O., 1955, Special techniques for bacterial enzymes. Enrichment culture and adaptive enzymes, in: Methods in Enzymology ( S. P. Colowick and N. O. Kaplan, eds.), Vol. 1, pp. 126–137, Academic Press, New York.

    Chapter  Google Scholar 

  • Hegeman, G. D., and Rosenberg, S. L., 1970, The evolution of bacterial enzyme systems, Annu. Rev. Microbiol. 24: 429.

    Article  CAS  Google Scholar 

  • Hersh, E. M., 1971, L-Glutaminase: Suppression of lymphocyte blastogenic responses in vitro, Science 172: 736.

    Article  PubMed  CAS  Google Scholar 

  • Hersh, E. M., 1973, Immunosuppressive enzymes, Transplant. Proc. 5: 1211.

    PubMed  CAS  Google Scholar 

  • Herter, F. P., Weissman, S. G., Thompson, H. G., Hyman, G., and Martin, D. S., 1961, Clinical experience with 6-amino nicotinamide, Cancer Res. 21: 31.

    PubMed  CAS  Google Scholar 

  • Ho, P. H. W., Thetford, B., Carter, C. J. K., and Frei, E., 1970, Clinical pharmacologic studies of L-asparaginase, Clin. Pharmacol. Ther. 11: 408.

    PubMed  CAS  Google Scholar 

  • Ho, P. P. K., and Millikin, E. B., 1970, Multiple forms of L-asparaginase, Biochim. Biophys. Acta 206: 196.

    PubMed  CAS  Google Scholar 

  • HOLCENBERG, J. S., AND ROBERTS, J., 1977, Enzymes as drugs, Annu. Rev. Pharmacol. 17.

    Google Scholar 

  • Holcenberg, J. S., Roberts, J., and Dolowy, W. C., 1973, Glutaminases as antineoplastic agents, in: The Enzymes of Glutamine Metabolism ( S. Prusiner and G. Stadtman, eds.), pp. 277–292, Academic Press, New York and London.

    Google Scholar 

  • Holcenberg, J. S., Schimer, G., Teller, D. C., and Roberts, J., 1975a, Biologic and physical properties of succinylated and glycosylated Acinetobacter glutaminase-asparaginase, J. Biol. Chem. 250: 4165.

    PubMed  CAS  Google Scholar 

  • Holcenberg, J. S., Tang, E., and Dolowy, W. C., 1975b, Effect of Acinetobacter glutaminase-asparaginase treatment on free amino acids in mouse tissues, Cancer Re. 35: 1320.

    CAS  Google Scholar 

  • Horowitz, B., and Meister, A., 1972, Glutamine-dependent asparagine synthetase from leukemia cells, J. Biol. Chem.247:6708.

    Google Scholar 

  • Horowitz, B., Madras, B. K., Meister, A., Old, L. S., Boyce, E. A., and Stockert, E., 1968, Asparagine synthetase activity of mouse leukemias, Science 160: 533.

    Article  PubMed  CAS  Google Scholar 

  • Howard, J. B., and Carpenter, F. H., 1972, L-Asparaginase from Erwinia carotovora. Substrate specificity and enzymatic properties, J. Biol. Chem. 247: 1020.

    PubMed  CAS  Google Scholar 

  • Ihler, G. M., Glew, R. H., and Schnure, F. W., 1973, Enzyme loading of erythrocytes, Proc. Natl. Acad. Sci. U.S.A. 70: 2663.

    Article  PubMed  CAS  Google Scholar 

  • Ihler, G. M., Lantzy, A., Purpura, J., and Glew, R. H., 1975, Enzymatic degradation of uric acid by urease-loaded human erythrocytes, J. Clin. Invest. 56: 595.

    Article  PubMed  CAS  Google Scholar 

  • Jackson, R. C., and Handschumacher, R. E., 1970, Escherichia coli L-asparaginase. Catalytic activity and subunit nature, Biochemistry 9: 3585.

    CAS  Google Scholar 

  • Jose, D. G., and Good, R. A., 1973, Quantitative effects of nutritional essential amino acid deficiency upon immune responses to tumors in mice, J. Exp. Med. 137: 1.

    Article  PubMed  CAS  Google Scholar 

  • Kendall, P. A., 1972, Antibody labelling for electron microscopy: Immunochemical properties of immunoglobulin G heavily labeled with methylmercury after thiolation by homocysteine thiolactone, Biochim. Biophys. Acta 257: 101.

    PubMed  CAS  Google Scholar 

  • kidd, J. D., 1953, Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum, J. Exp. Med. 98: 565.

    Article  PubMed  CAS  Google Scholar 

  • Kolata, G. B., 1975, Intracellular bacterial toxins: Origins and effects, Science 190: 969.

    Google Scholar 

  • Kreis, W., and Hession, C., 1973a, Isolation and purification of L-methionine-a-deamino-y-mercaptomethane-lyase (L-methionase) from Clostridium sporogenes, Cancer Res. 33: 1862.

    PubMed  CAS  Google Scholar 

  • Kreis, W., and Hession, C., 1973b, Biological effects of enzymatic deprivation of L-methionine in cell culture and an experimental tumor, Cancer Res. 33: 1866.

    PubMed  CAS  Google Scholar 

  • Laboureur, P., Langlois, C., Labrousse, M., Boudon, M., Emeraud, J., Samain, J. F., Ageron, M., and Dumesnil, Y., 1971, L-Asparaginases d’Escherichia coli. II. Pluralite et origine des formes moleculaires. Relations avec l’activite biologique, Biochimie 53: 1157.

    Article  PubMed  CAS  Google Scholar 

  • Lamirande, G. D., 1961, Action of deoxyribonuclease and ribonuclease on the growth of Ehrlich ascites carcinoma in mice, Nature (London) 192: 52.

    Article  Google Scholar 

  • Land, V. J., Sutow, W. W., Fernbach, D. J., Lane, D. M., and Williams, T. E., 1972, Toxicity of L-asparaginase in children with advanced leukemia, Cancer 30: 339.

    Article  PubMed  CAS  Google Scholar 

  • Lane, M., and Smith, F. E., 1971, Induced riboflavin deficiency in treatment of patients with lymphomas and polycythemia vera, Proc. Amer. Assoc. Cancer Res. 12: 85.

    Google Scholar 

  • Lane, M., Alfrey, C. P., Mengel, C. E., Doherty, M. A., and Doherty, J., 1964, The rapid induction of human riboflavin deficiency with galactoflavin, J. Clin. Invest. 43: 357.

    Article  PubMed  CAS  Google Scholar 

  • Lazarus, H., Barell, E. F., Oppenheim, S., and Krishan, A., 1974, Divergent properties of two human lymphocytic cell lines isolated from a single specimen of peripheral blood, In Vitro 9: 303.

    Article  Google Scholar 

  • Levin, B., and Merrill, J. P., 1972, Immunosuppressive effects of cyclophosphamide and Lasparaginase in the inbred rat renal transplant model, Transplantation 13: 160.

    Article  PubMed  CAS  Google Scholar 

  • Lin, J. Y., Tserng, K. Y., Chen, C. L., Lin, L. T., and Tung, T. C., 1970, Abrin and ricin: New antitumor substances, Nature (London) 227: 292.

    Article  CAS  Google Scholar 

  • Ltu, Y. P., and Handschumacher, R. E., 1972, Nitroasparaginase: Subunit cross-linkage and altered substrate specificity, J. Biol. Chem. 247: 66.

    Google Scholar 

  • Livingston, D. M., Ferguson, C., Gallogly, R., and Lazarus, H., 1976, Accumulation of cystine auxotrophic thymocytes accompanying Type C viral leukemogenesis in the mouse, Cell 7: 41.

    Article  PubMed  CAS  Google Scholar 

  • Lorincz, A. B., Kuttner, R. E., and Brandt, M. B., 1969, Tumor response to phenylalanine-tyrosine limited diets, J. Amer. Diet. Assoc. 54: 198.

    CAS  Google Scholar 

  • Malta, T., Morokuma, K., and Matsuda, G., 1974, Amino acid sequence of L-asparaginase from Escherichia coli, J. Biochem. 76: 1351.

    Google Scholar 

  • Makino, H., Satoh, H., Kuroiwa, Y., Yanazaki, S., Tamaura, Y., and Inada, Y., 1975, Immunochemical properties of asparaginase modified by chemical substitutions, Immunochemistry 12: 183.

    Article  CAS  Google Scholar 

  • Manning, J. M., Cerami, A., Gillette, P. N., Defuria, F. G., and Miller, D. R., 1974, Biochemical and physiological properties of carbamylated hemoglobin S, Adv. Enzymol. 40: 1.

    PubMed  CAS  Google Scholar 

  • Marsh, J. W., Denis, I., and Wriston, J. C., 1976, Effect of glycosylation on clearance of E. coli asparaginase in mice, Fed. Proc. 35: 1371.

    Google Scholar 

  • Mashburn, L. T., and Wriston, J. C., 1964, Tumor inhibitory effect of L-asparaginase from Escherichia coli, Arch. Biochem. Biophys. 105: 450.

    Article  CAS  Google Scholar 

  • Mccoll, J. D., Rice, W. B., and Adamkiewicz, V. W., 1957, Inhibition of Walker carcinoma 256 by 6-amino nicotinamide, Can. J. Biochem. 35: 795.

    PubMed  CAS  Google Scholar 

  • Mccullough, J. L., Chabner, B. A., and Bertino, J. R., 1971, Purification and properties of carboxypeptidase G,, J. Biol. Chem. 246: 7207.

    PubMed  CAS  Google Scholar 

  • Meadows, G. G., Digiovanni, J., Minor, J., and Elmer, G. W., 1976, Some biological properties and an in vivo evaluation of tyrosine phenol-lyase on growth of B-16 melanoma, Cancer Res. 36: 167.

    PubMed  CAS  Google Scholar 

  • Mihich, E., and Nichol, A. A., 1965, Antitumor effects of methylglyoxal-bis-(N4methylthiosemicarbazone) and their potentiation in pyridoxine-deficient animals, Cancer Res. 25: 794.

    PubMed  CAS  Google Scholar 

  • Mikami, T., Ohuma, M., and Hayashi, T. T. A., 1974, Requirement of arginine for the replication of Marek’s disease herpes virus, J. Gen. Virol. 22: 115.

    Article  PubMed  CAS  Google Scholar 

  • Miller, H. K., Salser, J. S., and Balis, M. E., 1969, Amino acid levels following L-asparagine amidohydrolase (EC.3.5.1.1) therapy, Cancer Res. 29: 183.

    PubMed  CAS  Google Scholar 

  • Morell, A. G., Gregoriadis, G., Scheinberg, I. H. Hickman, J., and Ashwell, G., 1971. The role of sialic acid in determining the survival of glycoproteins in the circulation, J. Biol. Chem. 246: 1461.

    PubMed  CAS  Google Scholar 

  • Morino, Y., and Snell, E. E., 1970, Tryptophanase (Escherichia coli B), in: Methods in Enzymology ( H. Tabor and C. W. Tabor, eds.), Vol. 17A, pp. 439–446, Academic Press, New York.

    Google Scholar 

  • Morris, H. P., 1947, Effects on the genesis and growth of tumors associated with vitamin intake, Ann. N. Y. Acad. Sci. 49: 119.

    Article  CAS  Google Scholar 

  • Nesbitt, M., Chard, R., Evans, A., Karon, M., and Hammond, D., 1970, Intermittent L-asparaginase therapy for acute childhood leukemia, Proceedings of the 10th International Cancer Congress, p. 447.

    Google Scholar 

  • Neukomm, S., Thompson, C. B., and Biossonnaz, M., 1949, Action de l’arginase pure sur la croissance du cancer greffe de la souris, Expezientia 5: 239.

    Article  CAS  Google Scholar 

  • Newman, R. E., and Mccoy, T. A., 1956, Dual requirement of Walker carcinosarcoma 256 in vitro for asparagine and glutamine, Science 124: 124.

    Article  Google Scholar 

  • Newcomb, E., and Minocha, H. C., 1973, Amino acid requirement for fibroma virus replication in rabbit kidney cells, Amer. J. Vet. Res. 34: 261.

    CAS  Google Scholar 

  • Newton, W. A., Ertel, I. J., Nesbit, M., Thatcher, L. G., Karon, M., and Hammond, G. B., 1973, Effective dose of L-asparaginase in acute leukemia, Proc. Amer. Assoc. Cancer Res. 14: 78.

    Google Scholar 

  • Ohno, R., and Hersh, E. M., 1970, Immunosuppressive effects of L-asparaginase, Cancer Res.30:1605.

    Google Scholar 

  • Ohnuma, T., Holland, J. F., Nagel, G., and ST. Arneault, G., 1969, Effects of L-asparaginase in acute myelocytic leukemia, J. Amer. Med. Assoc. 210: 1919.

    Article  CAS  Google Scholar 

  • Ohnuma, T., Waligunda, J., and Holland, J. F., 1971, Amino acid requirements in vitro of human leukemic cells, Cancer Res. 31: 1640.

    CAS  Google Scholar 

  • Ohnuma, T., Holland, J. F., and Meyer, P., 1972, Erwinia carotovora asparaginase in patients with prior anaphylaxis to asparaginase from E. coli, Cancer 30: 376.

    CAS  Google Scholar 

  • Oki, T., Shirai, M., Ohshima, M., Yamamoto, T., and Soda, K., 1973, Antitumor activities of bacterial leucine dehydrogenase and glutaminase A, FEBS Lett. 33: 286.

    Google Scholar 

  • Old, L. J., Boyse, E. A., Campbell, H. A., Brodey, R. S., Fidler, J., and Teller, J. D., 1967, Treatment of lymphosarcoma in the dog with L-asparaginase, Cancer 20: 1066.

    Google Scholar 

  • Olsnes, S., Refsnes, K., and Pijl, A., 1974, Mechanism of action of the toxic lectins abrin and ricin, Nature (London) 249: 627.

    Article  CAS  Google Scholar 

  • Ortega, J., Nesbit, M., Donaldson, M., Weiner, J., Hittle, R., and Karon M., 1975, LAsparaginase, vincristine and prednisone for induction of first remission in acute lymphocytic leukemia (ALL), Proc. Amer. Assoc. Cancer Res. 16: 140.

    Google Scholar 

  • Patterson, M. K., JR., and Orr, G. R., 1969, Regeneration, tumor, dietary and L-asparaginase effects on asparagine biosynthesis in rat liver, Cancer Res. 29: 1179.

    PubMed  CAS  Google Scholar 

  • Pearsall, N. N., and Weiser, R. S., 1970, The Macrophage, p. 65, Lea and Febiger, Philadelphia. Peterson, R. G., Handschumacher, R. E., and Mitchell, M. S., 1971, Immunological responses to L-asparaginase, J. Clin. Invest. 50: 1080.

    Google Scholar 

  • Potter, V. R., 1958, The biochemical approach to the cancer problem, Fed. Proc. Fed. Amer. Soc. Exp. Biol. 17: 691.

    CAS  Google Scholar 

  • Prager, M. D., and Bachynsky, N., 1968, Asparagine synthetase in normal and malignant tissues: Correlation with tumor sensitivity to asparaginase, Arch. Biochem. Biophys. 127: 645.

    Article  PubMed  CAS  Google Scholar 

  • Recsei, P. A., and Snell, E. E., 1970, Histidine decarboxylase of Lactobacillus 30a. VI. Mechanism of action and kinetic properties, Biochemistry 9: 1492.

    Article  PubMed  CAS  Google Scholar 

  • Regan, J. D., Vodopick, H., Takeda, S., Lee, W. H., and Faulcon, F. M., 1969, Serine requirement in leukemic and normal blood cells, Science 163: 1452.

    Google Scholar 

  • Rigby, P. W. J., Burleigh, B. D., and Hartley, B. S., 1974, Gene duplication in experimental enzyme evolution, Nature (London) 251: 200.

    Article  CAS  Google Scholar 

  • Riley, V., 1968, Role of the LDH-elevating virus in leukemia therapy by asparaginase, Nature (London) 220: 1245.

    Article  CAS  Google Scholar 

  • Riley, V., Campbell, H. A., and Stock, C. C., 1970, Asparaginase clearance: Influence of the LDH-elevating virus, Proc. Soc. Exp. Biol. Med. 133: 3.

    Google Scholar 

  • Rivlin, R. S., 1973, Riboflavin and cancer: A review, Cancer Res. 33: 1977.

    Google Scholar 

  • Rivlin, R. S., Hornibrook, R., and Osnos, M., 1973, Effects of riboflavin deficiency upon concentrations of riboflavin mononucleotide and flavin adenine dinucleotide in Novikoff hepatoma in rats, Cancer Res. 33: 3019.

    PubMed  CAS  Google Scholar 

  • Roberts, J., 1976, Purification and properties of highly potent antitumor glutaminase—asparaginase from Pseudomonas 7a, J. Biol. Chem. 251: 2119.

    PubMed  CAS  Google Scholar 

  • Roberts, J., and Schmid, F. A., 1976, Biological and antineoplastic properties of a novel Pseudomonas glutaminase—asparaginase with high therapeutic efficacy, Proc. Amer. Assoc. Cancer Res. 17: 26.

    Google Scholar 

  • Roberts, J., Schmid, F. A., and Takai, K., 1974, The in vivo effects of leucine dehydrogenase from Bacillus sphaericus, FEBS Letters 43: 56.

    Article  PubMed  CAS  Google Scholar 

  • Roberts, J., Schmid, F. A., and Takai, K., 1976, In vivo effects of phenylalanine ammonia lyase, Cancer Treatment Rep. 60: 261.

    CAS  Google Scholar 

  • Rogers, J. C., and Kornfeld, S., 1971, Hepatic uptake of proteins coupled to feteuin glycopeptide, Biochem. Biophys. Res. Commun. 45: 622.

    Article  PubMed  CAS  Google Scholar 

  • Roholt, O. A., and Greenberg, D. M., 1956, Liver arginase. IV. Effects of pH on kinetics of manganese-activated enzyme, Arch. Biochem. Biophys. 62: 454.

    Article  PubMed  CAS  Google Scholar 

  • Rubens, R. D., 1974, Antibodies as carriers of anticancer agents, Lancet 1974: 498.

    Article  Google Scholar 

  • Rutter, D. A., and Wade, H. E., 1971, The influence of the iso-electric point of L-asparaginase upon its persistence in the blood, Br. J. Exp. Pathol. 52: 610.

    PubMed  CAS  Google Scholar 

  • Ryan, W. L., and Curtis, G. L., 1973, Immunity and asparaginase suppression of tumor growth, J. Natl. Cancer Inst. 51: 147.

    PubMed  CAS  Google Scholar 

  • Sachs, D. H., Schechter, A. N., Eastlake, A., and Anfinsen, C. B., 1974, Immunological distinction between the possible origins of enzymatic activity in a polypeptide fragment of staphylococcal nuclease, Nature (London) 251: 242.

    Article  CAS  Google Scholar 

  • Sagers, R. D., and Carter, J. E., 1971, L-Serine dehydratase (Clostridium acidiurici), in: Methods in Enzymology ( H. Tabor and C. W. Tabor, eds.), Vol. 17B, pp. 351–356, Academic Press, New York.

    Google Scholar 

  • Sartorelli, A. C., 1964, Combination chemotherapy with actinomycin D and ribonuclease: An example of complementary inhibition, Nature (London) 203:877.

    Google Scholar 

  • Saunders, E. F., 1972, The effect of L-asparaginase on the nucleic acid metabolism and cell cycle of human leukemia cells, Blood 39: 575.

    PubMed  CAS  Google Scholar 

  • Schmid, F. A., and Roberts, J., 1974, Antineoplastic and toxic effects of Acinetobacter and Pseudomonas glutaminase-asparaginase, Cancer Chemother. Rep. 58: 829.

    PubMed  CAS  Google Scholar 

  • Schwartz, R. S., 1969, L-Asparaginase acts as an immunosuppressant in mice, Nature (London) 224: 275.

    Article  CAS  Google Scholar 

  • Sedlacek, H. H., Meesmann, H., and Seiler, F. R., 1975, Regression of spontaneous mammary tumors in dogs after injection of neuraminidase-treated tumor cells, Int. J. Cancer 15: 409.

    Article  PubMed  CAS  Google Scholar 

  • Seigler, H. F., Shingleton, W. W., and Pickrell, K. L., 1974, Intralesional BCG, intravenous immuno lymphocytes, and immunization with neuraminidase-treated tumor cells to manage melanoma, Plast. Reconstr. Surg. 55: 294.

    Article  Google Scholar 

  • Sethi, K. K., and Brandis, H., 1973, Neuraminidase induced loss in the transplantability of murine leukemia L1210, induction of immunoprotection and the transfer of induced immunity to normal DBA/2 mice by serum and peritoneal cells, Br. J. Cancer 27: 106.

    Article  PubMed  CAS  Google Scholar 

  • Shapiro, D. M., Dietrich, L. S., and Shils, M. E., 1957, Quantitative biochemical differences between tumor and host as a basis for cancer chemotherapy, V. Niacin and nicotinamide, Cancer Res. 17: 600.

    PubMed  CAS  Google Scholar 

  • Shifrin, S., and Grochowski, B. J., 1972, L-Asparaginase from Escherichia coli B. Succinylation and subunit interaction, J. Biol. Chem. 247: 1048.

    PubMed  CAS  Google Scholar 

  • Shifrin, S., Luborsky, S. W., and Grochowski, B. J., 1971, L-Asparaginase from Escherichia coli B. Physiocochemical studies of the dissociation process, J. Biol. Chem. 246: 7708.

    PubMed  CAS  Google Scholar 

  • Shingleton, W. W., Seigler, H. F., Stocks, L. H., and Downs, R. W., 1975, Management of recurrent melanoma of the extremity, Cancer 35: 574.

    Article  PubMed  CAS  Google Scholar 

  • Shizuta, Y., and Tokushige, M., 1971, Threonine deaminase—degradative (Escherichia coli), in: Methods in Enzymology ( H. Tabor and C. W. Tabor, eds.), Vol. 17B, pp. 575–580, Academic Press, New York.

    Google Scholar 

  • Simmons, R. L., and Rios, A., 1973a, Differential effect of neuraminidase on the immunogenicity of viral associated and private antigens of mammary carcinomas, J. Immunol. 111: 1820.

    PubMed  CAS  Google Scholar 

  • Simmons, R. L., and Rios, A., 1973b, Neuraminase treated cells and their role in cancer immunotherapy, in: Birth Defects: Original Article Series ( D. Bergsma, ed.), Vol. 9, pp. 223–228, Williams and Wilkins, Baltimore.

    Google Scholar 

  • Simmons, R. L., Rios, A., Landgren, G., RAY, P. K., Mckhann, C. F., and Haywood, G. R., 1971, Immunospecific regression of methylcholanthrene fibrosarcoma with the use of neuraminidase, Surgery 70: 38.

    PubMed  CAS  Google Scholar 

  • Skipper, H. E., and Thomson, J. R., 1958, A preliminary study of the influence of amino acid deficiencies on experimental cancer chemotherapy, in: Ciba Found. Symp.: Amino Acids and Peptides with Antimetabolic Activity ( G. E. W. Wolstonholme and C. M. O’Connor, eds.), pp. 38–61, Little, Brown and Co., Boston.

    Google Scholar 

  • Spiers, A. S. D., and Wade, H. E., 1976, Bacterial glutaminase in treatment of acute leukaemia, Br. Med. J. 1: 1317.

    Article  PubMed  CAS  Google Scholar 

  • Storr, J. M., and Burton, A. F., 1974, The effects of arginine deficiency on lymphoma cells, Br. J. Cancer 30: 50.

    Article  PubMed  CAS  Google Scholar 

  • Sugimura, T., Birnbaum, S. M., Winitx, M., and Greenstein, J. P., 1959, Quantitative nutritional studies with water-soluble, chemically defined diets. VIII. The forced feeding of diets each lacking in one essential amino acid, Arch. Biochem. Biophys. 81: 448.

    Article  PubMed  CAS  Google Scholar 

  • Summers, W. P., and Handschumacher, R. E., 1971, L5178Y asparagine-dependent cells and independent clonal sublines: Toxicity of 5-diazo-4-oxo-L-norvaline, Biochem. Pharmacol. 20: 2213.

    Article  PubMed  CAS  Google Scholar 

  • Summers, W. P., and Handschumacher, R. E., 1973, The rate of mutation of L5178Y asparagine-independence and its biological consequences, Cancer Res. 33: 1775.

    PubMed  CAS  Google Scholar 

  • Theuer, R. C., 1971, Effect of essential amino acid restriction on the growth of female C57BL mice and their implanted BW10232 adenocarcinomas, J. Nutr. 101: 223.

    PubMed  CAS  Google Scholar 

  • Thorbecke, G. J., Maurer, P. H., and Benaceraff, B., 1960, The affinity of the reticulo-endothelial system for various modified serum proteins, Br. J. Exp. Pathol. 41: 190.

    PubMed  CAS  Google Scholar 

  • Thornes, R. D., Deasy, P. F., Carroll, R., Reen, D. C., and Macdonell, J. D., 1972, The use of the proteolytic enzyme brinase to produce autocytoxicity in patients with acute leukemia and its possible role in immunotherapy, Cancer Res. 32: 280.

    PubMed  CAS  Google Scholar 

  • Tryfiates, G. P., and Morris, H. P., 1974, Effect of pyridoxine deficiency on tyrosine transaminase activity and growth of four Morris hepatomas, J. Natl. Cancer Inst. 52: 1259.

    PubMed  CAS  Google Scholar 

  • Uren, J. R., and Handschumacher, R. E., 1974, Evaluation of asparagine analogs as cancer chemotherapeutic agents, Proc. Amer. Assoc. Cancer Res. 15: 124.

    Google Scholar 

  • Uren, J. R., and Lazarus, H., 1975, Enzymatic approaches to cyst(e)ine depletion therapy, Proc. Amer. Assoc. Cancer Res. 16: 144.

    Google Scholar 

  • Uren, J. R., Summers, W. P., and Handschumacher, R. E., 1974, Enzymatic and nutritional evidence for two-stage expression of the asparagine synthetase locus in L5178Y murine leukemia mutants, Cancer Res. 34: 2940.

    PubMed  CAS  Google Scholar 

  • Vadlamudi, S., Padarathsingh, M., Waravdekar, V. S., and Goldin, A., 1970, Factors influencing the therapeutic activity of L-asparaginase (NSC 109229) in leukemic (L5178Y) mice, Cancer Res. 30: 1467.

    PubMed  CAS  Google Scholar 

  • Vrat; V. A., 1951, Inhibitory effects of arginase on mammary adenocarcinoma transplants in strain A mice, Permanente Found. (Oakland, Calif.) Med. Bull. 9: 49.

    Google Scholar 

  • Weigelt, 0., 1974, Die Wirkung intratumoral applizierter proteolytischer Enzyme auf spontane Mamma-adenome bei weiblichen Sprague-Dawley Ratten, Arzneim. Forsch. 24: 549.

    Google Scholar 

  • Whitecar, J. P., Bodey, G. P., Harris, J. E., and Freireich, E. J., 1970, L-Asparaginase, N. Engl. J. Med. 282: 732.

    Article  PubMed  Google Scholar 

  • Wolf, M., and Ransberger, K., 1972, Enzyme Therapy, Vantage Press, New York.

    Google Scholar 

  • Woods, J. S., and Handschumacher, R. E., 1973, Hepatic regulation of plasma L-asparagine, Amer. J. Physiol. 224: 740.

    PubMed  CAS  Google Scholar 

  • Wriston, J. C., and Yellin, T. 0., 1973, L-Asparaginase: A review, Adv. Enzymol. 39: 185.

    PubMed  CAS  Google Scholar 

  • Wu, T. T., Lin, E. C. C., and Tanaka, S., 1968, Mutants of Aerobacter aerogenes capable of utilizing xylitol as a novel carbon source, J. Bacteriol. 96: 447.

    PubMed  CAS  Google Scholar 

  • Wu, W. H., and Morris, D. R., 1973, Biosynthetic arginine decarboxylase from Escherichia coli: Purification and properties, J. Biol. Chem. 248: 1687.

    PubMed  CAS  Google Scholar 

  • Zyk, N., 1973, Modification of L-asparaginase EC-2 by homologous antibodies, Biochim. Biophys. Acta 302: 420.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Sidney Farber Cancer Institute, Harvard University, Boston, Massachusetts, USA

    Jack R. Uren

  2. Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut, USA

    Robert E. Handschumacher

Authors
  1. Jack R. Uren
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Robert E. Handschumacher
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. M.D. Anderson Hospital and Tumor Institute, University of Texas System Cancer Center, Houston, Texas, USA

    Frederick F. Becker

Rights and permissions

Reprints and permissions

Copyright information

© 1977 Plenum Press, New York

About this chapter

Cite this chapter

Uren, J.R., Handschumacher, R.E. (1977). Enzyme Therapy. In: Becker, F.F. (eds) Chemotherapy. Cancer, vol 5. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6628-1_16

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-6628-1_16

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-6630-4

  • Online ISBN: 978-1-4615-6628-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation