Interaction of Anticancer Drugs with Hepatic Monooxygenase Enzymes

References

• Metabolism and action of anti-cancer drugs, G. Powis, R. A. Prough. Taylor & Francis, London 1987; 1–336
   Google Scholar
• Carter S. K., Livingston R. B. Principles of cancer chemotherapy. Principles of Cancer Treatment, S. K. Carter, E. Blatstein, R. B. Livingston. McGraw-Hill, New York 1982; 95–110
   Google Scholar
• Wislocki P. G., Miwa G. T., Lu A. Y. H. Reactions catalysed by the cytochrome P-450 system. Enzymatic Basis of Detoxification, W. B. Jakoby. Academic Press, New York 1980; vol. 1: 135–182
   Google Scholar
• Gelboin H. V. Benzo[a]pyrene metabolism, activation, and carcinogenesis: role and regulation of mixed-function oxidases and related enzymes. Physiol. Rev. 1980; 60: 1107–1166
   PubMed Web of Science ®Google Scholar
• Conney A. H. Induction of microsomal enzymes by foreign chemicals and carcinogenesis by polycyclic aromatic hydrocarbons: G. H. A. Clowes memorial lecture. Cancer Res. 1982; 42: 4875–4917
   PubMed Web of Science ®Google Scholar
• Coon M. J., Koop D. R. P-450 oxygenases in lipid transformation. Enzymes 1983; 16: 645–677
   Google Scholar
• Nebert D. W., Nelson D. R., Adesnik M., Coon M. J., et al. The P450 superfamily: Updated listing of all genes and recommended nomenclature for the chromosomal loci. DNA 1989; 8: 1–13
   PubMedGoogle Scholar
• Waxman D. J. Rat hepatic cytochrome P-450: comparative studies of multiple isozymic forms. Cytochrome P-450: Structure, Mechanism and Biochemistry, P. R. Ortiz de Montellano. Plenum Press, New York 1986; 525–539
   Google Scholar
• Waxman D. J. Interactions of hepatic cytochromes P-450 with steroid hormones. Regioselectivity and stereospecificity of steroid hydroxylation and hormonal regulation of rat P-450 enzyme expression. Biochem. Pharmacol. 1988; 37: 71–84
   PubMed Web of Science ®Google Scholar
• Schwab G. E., Johnson E. F. Enzymology of rabbit cytochromes P-450. Mammalian Cytochromes P-450, F. P. Guengerich. CRC Press, Boca Raton, FL 1987; vol. 1: 55–105
   Google Scholar
• Distlerath L. M., Guengerich F. P. Enzymology of human liver cytochromes P-450. Mammalian Cytochromes P-450, F. P. Guengerich. CRC Press, Boca Raton, FL 1987; vol. 1: 134–198
   Google Scholar
• Guengerich F. P. Enzymology of rat liver P-450 cytochromes. Mammalian Cytochromes P-450. CRC Press, Boca Raton, FL 1987; vol. 1: 1–54
   Google Scholar
• Cytochrome P-450. Structure, mechanism, and biochemistry, P. R. Ortiz de Montellano. Plenum Press, New York 1986; 1–556
   Google Scholar
• Adesnik M., Atchison M. Genes for cytochrome P-450 and their regulation. Critical Rev. Biochem. 1985; 19: 247–305
   Google Scholar
• Ortiz de Montellano P. R., Reich N. O. Inhibition of cytochrome P-450 enzymes, Cytochrome P-450. Structure Mechanism and Biochemistry, P. R. Ortiz de Montellano. Plenum Press, New York 1986; 273–314
   Google Scholar
• Whitlock J. P., Jr. The regulation of cytochrome P-450 gene expression. Ann. Rev. Pharmacol. Toxicol. 1986; 26: 333–369
   PubMed Web of Science ®Google Scholar
• Friedman O. M., Myles A., Colvin M. Cyclophosphamide and phosphoramide mustards. Adv. Cancer Chemother. 1979; 1: 143–204
   Google Scholar
• Cohen J. L., Jao J. Y. Enzymatic basis of cyclophosphamide activation by hepatic microsomes of the rat. J. Pharmacol. Exp. Ther. 1970; 174: 206–210
   PubMed Web of Science ®Google Scholar
• Cox P. J., Farmer P. B., Jarman M. Metabolism and mechanism of action of cyclophosphamide. Cancer Treat. Rep. 1976; 60: 299–525
   Google Scholar
• Gurtoo H. L., Marinello A. J., Struck R. F., Paul B., Dahms R. P. Studies on the mechanism of denaturation of cytochrome P-450 by cyclophosphamide and its metabolites. J. Biol. Chem. 1981; 256: 11691–11701
   PubMed Web of Science ®Google Scholar
• Colvin M., Hilton J. Pharmacology of cyclophosphamide and metabolites. Cancer Treat. Rep. 1981; 65(suppl. 3)89–95
   PubMedGoogle Scholar
• Sladek N. E. Oxazaphosphorines. Metabolism and Action of Anticancer Drugs, G. Powis, R. A. Prough. Taylor & Francis, New York 1987; 48–90
   Google Scholar
• Sladek N. E. Therapeutic efficacy of cyclophosphamide as a function of its metabolism. Cancer Res. 1972; 32: 535–542
   PubMed Web of Science ®Google Scholar
• Jao J. Y., Jusko W. J., Cohen J. L. Phenobarbital effects on cyclophosphamide pharmacokinetics in man. Cancer Res. 1972; 32: 2761–2764
   PubMed Web of Science ®Google Scholar
• Struck R. F., Kari P., Kalin J., Montgomery J. A., Marinello A. J., Love J., Bansal S. K., Gurtoo H. L. Metabolism of cyclophosphamide by purified cytochrome P-450 from microsomes of phenobarbital-treated rats. Biochem. Biophys. Res. Commun. 1984; 120: 390–396
   PubMed Web of Science ®Google Scholar
• Clarke L., Waxman D. J. Oxidative metabolism of cyclophosphamide. Identification of the hepatic monooxygenase catalysts of drug activation. Cancer Res. 1988; 49: 2344–2350
   Web of Science ®Google Scholar
• Cox P. J., Farmer P. B., Jarman M., Kinas R. W., Stec W. J. Stereoselectivity in the metabolism of the enantiomers of cyclophosphamide in mice, rats, and rabbits. Drug Metab. Dispos. 1978; 6: 617–622
   PubMed Web of Science ®Google Scholar
• Farmer P. B. Enantiomers of cyclophosphamide and iphospha-mide. Biochem. Pharmacol. 1988; 37: 145–148
   PubMed Web of Science ®Google Scholar
• Martz G., D'Alessandri A., Keel H. J., Bollag W. Preliminary clinical results with a new antitumor agent RO 4–6467 (NSC-77213). Cancer Chemother. Rep. 1963; 33: 5–15
   PubMedGoogle Scholar
• Spivack S. D. Procarbazine. Ann. Int. Med. 1974; 81: 795–800
   PubMed Web of Science ®Google Scholar
• Baggiolini M., Dewald B., Aebi H. Oxidation of p-(N1-methylhydrazino methyl)-7V-isopropyl benzamide (procarbazine) to the methylazo derivative and oxidative cleavage of the N2–C bond in the isolated perfused rat liver. Biochem. Pharmacol. 1969; 18: 2187–2196
   PubMed Web of Science ®Google Scholar
• Oliverio V. T., Denham Ch., DeVita V. T., Kelly M. G. Some pharmacologic properties of a new antitumor agent, N-iso-propyl-alpha-(2-methylhydrazino)-p-toluamide, hydrochloride (NSC-77213). Cancer Chemother. Rep. 1964; 42: 1–7
   PubMedGoogle Scholar
• Prough R. A., Wittkop J. A., Reed D. J. Further evidence on the nature of microsomal metabolism of procarbazine and related alkylhydrazines. Arch. Biochem. Biophys. 1970; 140: 450–458
   PubMed Web of Science ®Google Scholar
• Weinkam R. J., Shiba D. A. Metabolic activation of procarbazine. Life Sci. 1978; 22: 937–946
   PubMed Web of Science ®Google Scholar
• Dunn D. L., Lubet R. A., Prough R. A. Oxidative metabolism of Ar-isopropyl-alpha-(2-methylhydrazino)-p-toluamide hydrochloride (procarbazine) by rat liver microsomes. Cancer Res. 1979; 39: 4555–4563
   PubMed Web of Science ®Google Scholar
• Wiebkin P., Prough R. A. Oxidative metabolism of N-iso-propyl-alpha-(2-methylazo)-p-toluamide (azoprocarbazine) by rodent liver microsomes. Cancer Res. 1980; 40: 3524–3529
   PubMed Web of Science ®Google Scholar
• Prough R. A., Brown M. I., Dannan G. A., Guengerich F. P. Major isozymes of rat liver microsomal cytochrome P-450 involved in the N-oxidation of N-isopropyl-alpha-(2-methylazo)-p-toluamide, the azo derivative of procarbazine. Cancer Res. 1984; 44: 543–548
   PubMed Web of Science ®Google Scholar
• Prough R. A., Tweedie D. J. Procarbazine. Metabolism and Action of Anticancer Drugs, G. Powis, R. A. Prough. Taylor & Francis, New York 1987; 29–47
   Google Scholar
• Moloney S. J., Wiebkin P., Cummings S. W., Prough R. A. Metabolic activation of the terminal Af-methyl group of AMso-propyl-alpha-(2-methylhydrazino)-p-toluamide hydrochloride (procarbazine). Carcinogenesis 1985; 6: 397–401
   PubMed Web of Science ®Google Scholar
• Rozencweig M., Von Hoff D. D., Henney J. E., Muggia F. M. VM 26 and VP 16–213: A comparative analysis. Cancer 1977; 40: 334–342
   PubMed Web of Science ®Google Scholar
• O'Dwyer P. J., Leyland-Jones B., Alonso M. T., Marsoni S., Wittes R. E. Etoposide (VP-16–213). Current status of an active anticancer drug. N. Engl. J. Med. 1985; 312: 692–700
   PubMed Web of Science ®Google Scholar
• Issell B. F., Rudolph A. R., Lorrie A. C. Etoposide (VP-16), Current Status and New Developments, B. F. Issell, F. M. Muggia, S. K. Carter. Academic Press, Orlando, FL 1984; 6–8
   Google Scholar
• Loike J. D., Horwitz S. B. Effect of VP-16–213 on the intracellular degradation of DNA in HeLa cells. Biochemistry 1976; 15: 5443–5449
   PubMed Web of Science ®Google Scholar
• Chen G. L., Yang L., Rowe T. C, Halligan B. D., Tewey K. M., Liu L. F. Nonintercalative antitumor drugs interfere with the breakage-reunion reaction of mammalian DNA topoiso-merase II. J Biol. Chem. 1984; 259: 13560–13566
   PubMed Web of Science ®Google Scholar
• Wozniak A. J., Glisson B. S., Hande K. R., Ross W. E. Inhibition of etoposide-induced DNA damage and cytotoxicity in L1210 cells by dehydrogenase inhibitors and other agents. Cancer Res. 1984; 44: 626–632
   PubMed Web of Science ®Google Scholar
• Evans W. E., Sinkule J. A., Crom W. R., Dow L., Look A. T., Rivera G. Phamacokinetics of teniposide (VM26) and etoposide (VP16–213) in children with cancer. Cancer Chemother. Pharmacol. 1982; 7: 147–150
   PubMed Web of Science ®Google Scholar
• Colombo T., D'lncalci M., Donelli M. G., Bartock I., Benfenati E., Farina P., Guartani A. Metabolic studies of a podophyllotoxin derivative (VP16) in the isolated perfused liver. Xenobiotica 1985; 15: 343–350
   PubMed Web of Science ®Google Scholar
• Haim N., Nemec J., Roman J., Sinha B. K. In vitro metabolism of etoposide (VP-16–213) by liver microsomes and irreversible binding of reactive intermediates to microsomal proteins. Biochem. Pharmacol. 1987; 36: 527–536
   PubMed Web of Science ®Google Scholar
• Van Maanen J. M. S., de Vries J., Pappie D., van den Akker E., Lafleur M. V. M., Retel J., van der Greef J., Pinedo H. M. Cytochrome P-450-mediated O-demethylation: A route in the metabolic activation of etoposide (VP-16–213). Cancer Res. 1987; 47: 4658–4662
   PubMed Web of Science ®Google Scholar
• Van Maanen J. M. S., de Ruiter C, Kootstra P. R., Lafleur M. V. M., de Vries J., Retel J., Pinedo H. M. Inactivation of Phi Z174 DNA by the orthoquinone derivative or its reduction product of the antitumor agent VP16–213. Eur. J. Cancer Clin. Oncol. 1985; 21: 1215–1218
   PubMedGoogle Scholar
• Long B. H., Musial S. T., Brattain M. G. Comparison of cytotoxicity and DNA breakage activity of congeners of Podophyllotoxin including VP16–213 and VM26: a quantitative structure-activity relationship. Biochemistry 1984; 23: 1183–1188
   PubMed Web of Science ®Google Scholar
• Sinha B. K., Myers C. E. Irreversible binding of etoposide (VP-16–213) to deoxyribonucleic acid and proteins. Biochem. Pharmacol. 1984; 33: 3725–3734
   PubMed Web of Science ®Google Scholar
• Sinha B. K., Eliot H. M., Kalayanaraman B. Iron-dependent hydroxyl radical formation and DNA damage from a novel metabolite of the clinically active antitumor drug VP-16. FEBS Lett. 1988; 227: 240–244
   PubMed Web of Science ®Google Scholar
• Gupta R. S. Genetic, biochemical and cross-resistant studies with mutants of Chinese hamster ovary cells resistant to the anticancer drugs, VM-16 and VP16–213. Cancer Res. 1983; 43: 1568–1574
   PubMed Web of Science ®Google Scholar
• Teicher B. A., Holden S. A., Rose C. M. Effect of oxygen on the cytotoxicity and antitumor activity of etoposide. J. Natl. Cancer Inst. 1985; 75: 1129–1134
   PubMed Web of Science ®Google Scholar
• Schein P. S. Nitrosoureas. Cancer and Chemotherapy, S. T. Crooke, A. W. Prestayko, N. Alder. Academic Press, New York 1981; 37–47
   Google Scholar
• Ali-Osmar F., Giblin J., Berger M., Murphy M. J., Jr., Rosenblum M. L. Chemical structure of carbamoylating groups and their relationship to bone marrow toxicity and antiglioma activity of bifunctionally alkylating and carbamoylating nitrosoureas. Cancer Res. 1985; 45: 4185–4191
   PubMed Web of Science ®Google Scholar
• Reed D. J. Metabolism of nitrosoureas. Nitrosoureas, A. W. Prestayko, L. H. Baker, S. T. Crooke, S. K. Carter, P. S. Schein. Academic Press, New York 1981; 51–66
   Google Scholar
• Reed D J. 2-Chloroethylnitrosoureas. Metabolism and Action of Anticancer Drugs, G. Powis, R. A. Prough. Taylor & Francis, New York 1987; 1–28
   Google Scholar
• May H. E., Boose R., Reed D. J. Hydroxylation of the carcinostatic 1 -(2-chloroethyl)-3-cyclohexyl-1 -nitrosourea (CCNU) by rat liver microsomes. Biochem. Biophys. Res. Com-mun. 1974; 57: 426–433
   PubMed Web of Science ®Google Scholar
• Hill D. L., Kirk M. C, Struck R. F. Microsomal metabolism of nitrosoureas. Cancer Res. 1975; 35: 296–301
   PubMed Web of Science ®Google Scholar
• Yeowell H. N., Waxman D. J., Wadhera A., Goldstein J. A. Suppression of the constitutive, male-specific rat hepatic cytochrome P-450 2c and its mRNA by 3,4,5,3 ',4 ',5 '-hexachlorobi-phenyl and 3-methylcholanthrene. Mol. Pharmacol. 1987; 32: 340–347
   PubMed Web of Science ®Google Scholar
• Potter D. W., Levin W., Ryan D. E., Thomas P. E., Reed D. J. Stereoselective monooxygenation of carcinostatic l-(2-chloroethyl)-3-(cyclohexyl)-l-nitrosourea and l-(2-chloroethyl)-3-(f/wts-4-meth-ylcyclohexyl)-l-nitrosourea by purified cytochrome P-450 isozymes. Biochem. Pharmacol. 1984; 33: 609–613
   PubMed Web of Science ®Google Scholar
• May H. E., Kohlhepp S. J., Boose R. B., Reed D. J. Synthesis and identification of products derived from the metabolism of the carcinostatic l-(2-cnloroethyi)-3-(fraHS-4-methylcyclohex-yl)-l-nitrosourea by rat liver microsomes. Cancer Res. 1979; 39: 762–772
   PubMedGoogle Scholar
• Levin V. A., Stearns J., Byrd A., Finn A., Weinkam R. J. The effect of phenobarbital pretreatment on the antitumor activity of l,3-bis(2-chloroethyl)-l-nitrosourea (BCNU), l-(2-chloro-ethyl)-3-cyclohexyl-l-nitrosourea (CCNU) and l-(2-chloroethyl)-3-(2,6-dioxo)-3-piperidyl-l-nitrosourea (PCNU), and on the plasma pharmacokinetics…. J. Pharmacol. Exp. Ther. 1979; 208: 1–6
   PubMed Web of Science ®Google Scholar
• Potter D. W., Reed D. J. Involvement of FMN and phenobarbital cytochrome P-450 in stimulating a one-electron reductive denitrosation of l-(2-chloroethyl)-3-(cyclohexyl)-l-ni-trosurea catalyzed by NADPH-cytochrome P-450 reductase. J. Biol. Chem. 1983; 258: 6906–6911
   PubMed Web of Science ®Google Scholar
• Potter D. W., Reed D. J. Denitrosation of carcinostatic nitrosoureas by purified NADPH cytochrome P-450 reductase and rat liver microsomes to yield nitric oxide under anaerobic conditions. Arch. Biochem. Biophys. 1982; 216: 158–169
   PubMed Web of Science ®Google Scholar
• High-dose thiotepa and autologous marrow transplantation. Advances in Cancer Chemotherapy, G. P. Herzig. Park Row Publishers. 1987; 1–53
   Google Scholar
• Cohen B. E., Egorin M. J., Kohlhepp E. A., Aisner J., Gutierrez P. L. Human plasma pharmacokinetics and urinary excretion of thiotepa and its metabolites. Cancer Treat. Rep. 1986; 70: 859–864
   PubMedGoogle Scholar
• Egorin M. J., Akman S. R., Gutierrez P. L. Plasma pharmacokinetics and tissue distribution of thiotepa in mice. Cancer Treat. Rep. 1984; 68: 1265–1268
   PubMedGoogle Scholar
• Breau A. P., Field L., Mitchell W. M. Thiono compounds. 4. In vitro mutagenic and antineoplastic activity of tepa and thio-tepa. Cell. Biol. Toxicol. 1984; 1: 21–30
   PubMed Web of Science ®Google Scholar
• Kamataki T., Belcher D. H., Neal R. A. Studies on the metabolism of diethyl p-nitrophenyl-phosphorothionate (parathion) and benzphetamine using an apparently homogeneous preparation of rat liver cytochrome P-450: effect of a cytochrome P-450 antibody preparation. Mol. Pharmacol. 1976; 12: 921–932
   PubMed Web of Science ®Google Scholar
• Teicher B. A., Holden S. A., Cucchi C. A., Cathcart K. N. S., Korbut T. T., Flatow J. L., Frei E., III. Combinations of N,W,W″-triethylenethiophosphoramide and cyclophosphamide in vitro and in vivo. Cancer Res. 1988; 48: 94–100
   PubMed Web of Science ®Google Scholar
• Berrigan M. J., Marinello A. J., Pavelic Z., Williams C. J., Struck R. F., Gurtoo H. L. Protective role of thiols in cyclophosphamide-induced urotoxicity and depression of hepatic drug metabolism. Cancer Res. 1982; 42: 3688–3695
   PubMed Web of Science ®Google Scholar
• Donelli M. G., Franchi G., Rosso R. The effect of cytotoxic agents on drug metabolism. Eur. J. Cancer 1970; 6: 125–126
   PubMed Web of Science ®Google Scholar
• Donelli M. G., Bartosek I., Guaitani A., Martini A., Colombo T., Pacciarini M. A., Modica R. Importance of pharmacokinetic studies on cyclophosphamide (NSC-26271) in understanding its cytotoxic effect. Cancer Treat. Rep. 1976; 60: 395–401
   PubMedGoogle Scholar
• Sladek N. E., Priest J., Doeden D., Mirocha C. J., Pathre S., Krivit W. Plasma half-life and urinary excretion of cyclophosphamide in children. Cancer Treat. Rep. 1980; 64: 1061–1066
   PubMedGoogle Scholar
• Satoh K. Purification, induction, and distribution of placental glutathione transferase: A new marker enzyme for preneoplastic cells in the rat chemical hepatocarcinogenesis. Proc. Natl. Acad. Sci. USA 1985; 82: 3964–3968
   PubMed Web of Science ®Google Scholar
• Tsuda H., Moore M. A., Asamoto M., Inoue T., Fukushima S., Ito N., Satoh K., Amelizad Z., Oesch F. Immuno-histochemically demonstrated altered expression of cytochrome P-450 molecular forms and epoxide hydrolase in N-ethyl-N-hydroxyethylnitrosamine-induced rat kidney and liver lesions. Carcinogenesis 1987; 8: 711–717
   PubMed Web of Science ®Google Scholar
• Marinello A. J., Gurtoo H. L., Struck R. F., Paul B. Denaturation of cytochrome P-450 by cyclophosphamide metabolites. Biochem. Biophys. Res. Commun. 1978; 83: 1347–1353
   PubMed Web of Science ®Google Scholar
• Marinello A. J., Bansal S. K., Paul B., Koser P. L., Love J., Struck R. F., Gurtoo H. L. Metabolism and binding of cyclophosphamide and its metabolite acrolein to rat hepatic microsomal cytochrome P-450. Cancer Res. 1984; 44: 4615–4621
   PubMed Web of Science ®Google Scholar
• LeBlanc G., Waxman D. J. Differential modulation of rat hepatic cytochrome P-450 enzymes upon exposure to cisplatin and cyclophosphamide. Proc. Am. Assoc. Cancer Res. 1987; 28: 314
   Web of Science ®Google Scholar
• Murphy S. D. Mechanism of the effect of acrolein on rat liver enzymes. Toxicol. Appl. Pharmacol. 1965; 7: 833–843
   PubMed Web of Science ®Google Scholar
• Ozols R. F., Young R. C. High dose cisplatin therapy in ovarian cancer. Sem. Oncol. 1985; 12: 21–30
   PubMed Web of Science ®Google Scholar
• Borch R. F. The platinum anti-tumour drugs. Metabolism and Action of Anticancer Drugs, G. Powis, R. A. Prough. Taylor & Francis, New York 1987; 163–193
   Google Scholar
• Pinto A. L., Lippard S. J. Binding of the antitumor drug cJs-diamminedichloroplatinum(II) (cisplatin) to DNA. Biochem. Biophys. Acta 1985; 780: 167–180
   PubMed Web of Science ®Google Scholar
• Litterst C. L., Tong S., Hirokata Y., Siddik Z. H. Stimulation of microsomal drug oxidation in liver and kidney of rats treated with the oncolytic agent os-dichlorodiammineplati-num-II. Pharmacology 1983; 46–53
   PubMed Web of Science ®Google Scholar
• Jollie D. R., Maines M. D. Effect of cis-platinum on kidney cytochrome P-450 and heme metabolism: Evidence for the regulatory role of the pituitary hormones. Arch. Biochem. Biophys. 1985; 240: 51–59
   PubMed Web of Science ®Google Scholar
• Maines M. D. Differential effect of m-platinum (c/s-diammine-dichloroplatinum) on regulation of liver and kidney haem and haemoprotein metabolism. Biochem. J. 1986; 237: 713–721
   PubMed Web of Science ®Google Scholar
• Maines M. D., Mayer R. D. Inhibition of testicular cytochrome P-450-dependent steroid biosynthesis by cis-platinum. J. Biol. Chem. 1985; 260: 6063–6068
   PubMed Web of Science ®Google Scholar
• Waterman M. R., John M. E., Simpson E. R. Regulation of synthesis and activity of cytochrome P-450 enzymes in physiological pathways. Cytochrome P-450: Structure, Mechanism, and Biochemistry, P. R Ortiz de Montellano. Pergamon Press. 1986; 345–386
   Google Scholar
• LeBlanc G. A., Waxman D. J. Feminization of rat hepatic P-450 expression by cisplatin. Evidence for perturbations in the hormonal regulation of steroid-metabolizing enzymes. J. Biol. Chem. 1988; 263: 15732–15739
   PubMed Web of Science ®Google Scholar
• Eiseman J. L., Bernstein A. L., Ferraro T. A. Effects of platinum anticancer agents on murine heme biosynthesis and drug metabolism. Pharmacologist 1985; 27: 152
   Google Scholar
• Donelli M. G., Garattini S. Drug metabolism after repeated treatments with cytotoxic agents. Eur. J. Cancer 1971; 7: 361–364
   PubMed Web of Science ®Google Scholar
• Gooderham N. J., Mannering G. J. Depression of the hepatic cytochrome P-450 monooxygenase system by treatment of mice with the antineoplastic agent 5-azacytidine. Cancer Res. 1985; 45: 1569–1572
   PubMed Web of Science ®Google Scholar
• Reed D. J., May H. E. Cytochrome P-450 interactions with the 2-chloroethylnitrosoureas and procarbazine. Biochimie 1978; 60: 989–995
   Web of Science ®Google Scholar
• Litterst C. L. Prolonged depression of hepatic microsomal drug metabolism and hemoprotein levels following a single dose of l-(2-chloroethyl)-3-cyclohexyl-l-nitrosourea (CCNU). Biochem. Pharmacol. 1981; 30: 1014–1016
   PubMed Web of Science ®Google Scholar
• Buchmann A., Kuhlmann W., Schwarz M., Kunz W., Wolf C. R., Moll E., Friedberg T., Oesch F. Regulation and expression of four cytochrome P-450 isoenzymes, NADPH-cyto-chrome P-450 reductase, the glutathione transferases B and C and microsomal epoxide hydrolase in preneoplastic and neoplastic lesions in rat liver. Carcinogenesis 1985; 6: 513–521
   PubMed Web of Science ®Google Scholar
• Schwarz M., Peres G., Buchmann A., Friedberg T., Waxman D. J., Kunz W. Phenobarbital induction of cytochrome P-450 in normal and preneoplastic rat liver: comparison of enzyme and mRNA expression as detected by immuno histochemistry and in situ hybridization. Carcinogenesis 1987; 8: 1355–1357
   PubMed Web of Science ®Google Scholar
• Giron C. G., Ordonez A., Jalon J. I., Baron M. G. Combination chemotherapy with ifosfamide, mitomycin, and cis-platin in advanced non-small cell lung cancer. Cancer Treat. Rep. 1987; 71: 851–853
   PubMedGoogle Scholar
• Reed E., Litterst C. L., Thill C. C, Yuspa S. H., Poirier M. C. m-Diamminedichloroplatinum(II)-DNA adduct formation in renal, gonadal, and tumor tissues of male and female rats. Cancer Res. 1987; 47: 718–722
   PubMed Web of Science ®Google Scholar
• Guarino A. M., Miller D. S., Arnold S. T., Pritchard J. B., Davis R. D., Urbanek M. A., Miller T. J., Litterst C. L. Platinate toxicity: past, present and prospects. Cancer Treat. Rep. 1979; 63: 1475–1483
   PubMedGoogle Scholar
• Song B-J., Gelboin H. V., Park S. S., Tsokos G. C, Friedman F. K. Monoclonal antibody-directed radioimmunoassay detects cytochrome P-450 in human placenta and lymphocytes. Science 1985; 228: 490–492
   PubMed Web of Science ®Google Scholar
• Waxman D. J. Rat hepatic cytochrome P-450 isoenzyme 2c. Identification as a male-specific, developmental induced steroid 16alpha-hydroxylase and comparison to a female-specific cytochrome P-450 isoenzyme. J. Biol. Chem. 1984; 259: 15481–15490
   PubMed Web of Science ®Google Scholar
• Guengerich F. P., Dannan G. A., Wright S. T., Martin M. V., Kaminsky L. S. Purification and characterization of liver microsomal cytochromes P-450: electrophoretic, spectral, catalytic and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or beta-naphthoflavone. Biochemistry 1982; 21: 6019–6030
   PubMed Web of Science ®Google Scholar
• Waxman D. J., Dannan G. A., Guengerich F. P. Regulation of rat hepatic cytochrome P-450: age-dependent expression, hormonal imprinting and xenobiotic inducibility of sex-specific isoenzymes. Biochemistry 1985; 24: 4409–4417
   PubMed Web of Science ®Google Scholar
• Sladek N. E., Doeden D., Powers J. F., Krivit W. Plasma concentrations of 4-hydroxycyclophosphamide and phosphoramide mustard in patients repeatedly given high doses of cyclophosphamide in preparation for bone marrow transplantation. Cancer Treat. Rep. 1984; 68: 1247–1254
   PubMedGoogle Scholar
• Allen L. M., Creaven P. J., Nelson R. L. Studies on the human pharmacokinetics of isophosphamide (NSC-109724). Cancer Treat. Rep. 1976; 60: 451–458
   PubMedGoogle Scholar
• Colvin M. The comparative pharmacology of cyclophosphamide and ifosphamide. Sent. Oncol. 1982; 9: 2–7
   PubMed Web of Science ®Google Scholar
• Gut J., Catin T., Dayer P., Kronbach T., Zanger U., Meyer U. A. Debrisoquine/sparteine-type polymorphism of drug oxidation: purification and characterization of two functionally different human liver cytochrome P-450 isozymes involved in impaired hydroxylation of the prototype substrate bufuralol. J. Biol. Chem. 1986; 261: 11734–11743
   PubMed Web of Science ®Google Scholar
• Guengerich F. P., Martin M. V., Beaune P. H., Kremers P., Wolff T., Waxman D. J. Characterization of rat and human liver microsomal cytochrome P-450 forms involved in nifedipine oxidation, a prototype for genetic polymorphism in oxidative drug metabolism. J Biol. Chem. 1986; 261: 5051–5060
   PubMed Web of Science ®Google Scholar
• Wrighton S. A., Campanile C, Thomas P. E., Maines S. L., Watkins P. B., Parker G., Mendez-Picon G., Haniu M., Shiveley J. E., Levin W., Guzelian P. S. Identification of a human liver cytochrome P-450 homologous to the major iso-safrole-inducible cytochrome P-450 in the rat. Mol. Pharmacol. 1986; 29: 405–410
   PubMed Web of Science ®Google Scholar
• Waxman D. J., Clarke L., Ng S. Oxidative metabolism of thio-TEPA: Role of hepatic cytochrome P-450. Proc. Am. Assoc. Cancer Res. 1989; 30: 463
   Google Scholar
• Teicher B. A., Waxman D. J., Holden S. A., Wang Y., Clarke L., Alvarez E., Jones S. M., Frei E, Ill. N,N′,N″-Triethylenethiophosphoramide: Evidence for an enzymatic and oxygen involvement in activation. Cancer Res. 1989, submitted for publication
   Web of Science ®Google Scholar
• Aoyama T., Yamano S., Waxman D. J., Lapenson D. P., Meyer U. A., Fischer V., Tyndale R., Inaba T., Kalow W., Gelboin H. V., Gonzalez F. J. Cytochrome P450 hPCN3, a novel P450IIIA gene product that is differentially expressed in adult human liver: cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCNl and hPCN3 for the metabolism of steroid hormones and cyclosporine. J. Biol. Chem. 1989, in press
   Web of Science ®Google Scholar