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Volumn 59, Issue 7, 1999, Pages 1458-1463

The anticancer prodrug CPT-11 is a potent inhibitor of acetylcholinesterase but is rapidly catalyzed to SN-38 by butyrylcholinesterase

Author keywords

[No Author keywords available]

Indexed keywords

7 ETHYL 10 HYDROXYCAMPTOTHECIN; CHOLINESTERASE; CHOLINESTERASE INHIBITOR; IRINOTECAN;

EID: 0033118471     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (95)

References (29)
  • 1
    • 0028225471 scopus 로고
    • Comparison of topoisomerase I inhibition, DNA damage, and cytotoxicity of camptothecin derivatives presently in clinical trials
    • Bethesda
    • Tanizawa, A., Fujimori, A., Fujimori, Y., and Pommier, Y. Comparison of topoisomerase I inhibition, DNA damage, and cytotoxicity of camptothecin derivatives presently in clinical trials. J. Natl. Cancer Inst. (Bethesda), 86: 836-842, 1994.
    • (1994) J. Natl. Cancer Inst. , vol.86 , pp. 836-842
    • Tanizawa, A.1    Fujimori, A.2    Fujimori, Y.3    Pommier, Y.4
  • 2
    • 0029116438 scopus 로고
    • Efficacy of topoisomerase I inhibitors, topotecan and irinotecan, administered at low dose levels in protracted schedules to mice bearing xenografts of human tumors
    • Houghton, P. J., Cheshire, P. J., Hallman, J. D., II, Lutz, L., Friedman, H. S., Danks, M. K., and Houghton, J. A. Efficacy of topoisomerase I inhibitors, topotecan and irinotecan, administered at low dose levels in protracted schedules to mice bearing xenografts of human tumors. Cancer Chemother. Pharmacol., 36: 393-403, 1995.
    • (1995) Cancer Chemother. Pharmacol. , vol.36 , pp. 393-403
    • Houghton, P.J.1    Cheshire, P.J.2    Hallman J.D. II3    Lutz, L.4    Friedman, H.S.5    Danks, M.K.6    Houghton, J.A.7
  • 3
    • 0030856521 scopus 로고    scopus 로고
    • Pharmacokinetic interrelationships of irinotecan (CPT-11) and its three major plasma metabolites in patients enrolled in phase I/II trials
    • Rivory, L. P., Haaz, M-C., Canal, P., Lokiec, F., Armand, J-P., and Robert, J. Pharmacokinetic interrelationships of irinotecan (CPT-11) and its three major plasma metabolites in patients enrolled in Phase I/II trials. Clin. Cancer Res., 3: 1261-1266. 1997.
    • (1997) Clin. Cancer Res. , vol.3 , pp. 1261-1266
    • Rivory, L.P.1    Haaz, M.-C.2    Canal, P.3    Lokiec, F.4    Armand, J.-P.5    Robert, J.6
  • 5
    • 0029609624 scopus 로고
    • Molecular aspects of carboxylesterase isoforms in comparison with other esterases
    • Satoh, T., and Hosokawa, M. Molecular aspects of carboxylesterase isoforms in comparison with other esterases. Toxicol. Lett., 82-83: 439-445, 1995.
    • (1995) Toxicol. Lett. , vol.82-83 , pp. 439-445
    • Satoh, T.1    Hosokawa, M.2
  • 6
    • 0028364014 scopus 로고
    • Metabolic activation of CPT-11, 7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyl-oxycamplothecin, a novel antitumor agent, by carboxylesterase
    • Satoh, T., Hosokawa, M., Atsumi, R., Suzuki, W., Hakusui, H., and Nagai, E. Metabolic activation of CPT-11, 7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyl-oxycamplothecin, a novel antitumor agent, by carboxylesterase. Biol. Pharmacol. Bull. 17: 662-664, 1994.
    • (1994) Biol. Pharmacol. Bull. , vol.17 , pp. 662-664
    • Satoh, T.1    Hosokawa, M.2    Atsumi, R.3    Suzuki, W.4    Hakusui, H.5    Nagai, E.6
  • 7
    • 0030790137 scopus 로고    scopus 로고
    • The transformation of irinotecan (CPT-11) to its active metabolite SN-38 by human liver microsomes. Differential hydrolysis for the lactone and carboxylate forms
    • Haaz, M. C., Rivory, L. P., Riche, C., and Robert, J. The transformation of irinotecan (CPT-11) to its active metabolite SN-38 by human liver microsomes. Differential hydrolysis for the lactone and carboxylate forms. Naunyn-Schmiedebergs Arch. Pharmacol., 356: 257-262, 1997.
    • (1997) Naunyn-Schmiedebergs Arch. Pharmacol. , vol.356 , pp. 257-262
    • Haaz, M.C.1    Rivory, L.P.2    Riche, C.3    Robert, J.4
  • 8
    • 0002221497 scopus 로고
    • Cholinesterase
    • L. Beckman (ed.), Basel: Karger
    • Whittaker, M. Cholinesterase. In: L. Beckman (ed.), Monographs in Human Genetics, Vol. 11, pp. 1-132. Basel: Karger, 1986.
    • (1986) Monographs in Human Genetics , vol.11 , pp. 1-132
    • Whittaker, M.1
  • 9
    • 0024352019 scopus 로고
    • Comparison of butyrylcholinesterase and acetylcholinesterase
    • Chatonnet, A., and Lockridge, O. Comparison of butyrylcholinesterase and acetylcholinesterase. Biochem. J., 260: 625-634, 1989.
    • (1989) Biochem. J. , vol.260 , pp. 625-634
    • Chatonnet, A.1    Lockridge, O.2
  • 10
    • 0025294717 scopus 로고
    • Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine
    • Lockridge, O. Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol. Ther., 47: 35-60, 1990.
    • (1990) Pharmacol. Ther. , vol.47 , pp. 35-60
    • Lockridge, O.1
  • 11
    • 0002803601 scopus 로고
    • Genetic variants of human serum butyrylcholinesterase influence the metabolism of the muscle relaxant succinylcholine
    • W. Kalow (ed.), New York: Pergamon Press, Inc.
    • Lockridge, O. Genetic variants of human serum butyrylcholinesterase influence the metabolism of the muscle relaxant succinylcholine. In: W. Kalow (ed.), Pharmacogenetics of Drug Metabolism, pp. 15-50. New York: Pergamon Press, Inc., 1992.
    • (1992) Pharmacogenetics of Drug Metabolism , pp. 15-50
    • Lockridge, O.1
  • 13
    • 0029760995 scopus 로고    scopus 로고
    • Identification and properties of a major plasma metabolite of irinotecan (CPT-11) isolated from the plasma of patients
    • Rivory, L. P., Riou, J. F., Haaz, M. C., Sable, S., Vuilhorgne, M., Commercon, A., Pond, S. M., and Robert, J. Identification and properties of a major plasma metabolite of irinotecan (CPT-11) isolated from the plasma of patients. Cancer Res., 56: 3689-3694, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 3689-3694
    • Rivory, L.P.1    Riou, J.F.2    Haaz, M.C.3    Sable, S.4    Vuilhorgne, M.5    Commercon, A.6    Pond, S.M.7    Robert, J.8
  • 14
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Washington DC
    • Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., and Silman, I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science (Washington DC), 253: 872-879, 1991.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 15
    • 24444468650 scopus 로고
    • Ground states of molecules. 38. The MNDO method. Approximations and parameters
    • Dewar, M. J. S., and Thiel, W. Ground states of molecules. 38. The MNDO method. Approximations and parameters. J. Am. Chem. Soc., 99: 4899-4907, 1977.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 4899-4907
    • Dewar, M.J.S.1    Thiel, W.2
  • 16
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethorpim, a drug receptor system
    • Dauber-Osguthorpe, P., Roberts, V. A., Osguthorpe, D. J., Wolff, J., Genest, M., and Hagler, A. T. Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethorpim, a drug receptor system. Proteins, 4: 31-47, 1988.
    • (1988) Proteins , vol.4 , pp. 31-47
    • Dauber-Osguthorpe, P.1    Roberts, V.A.2    Osguthorpe, D.J.3    Wolff, J.4    Genest, M.5    Hagler, A.T.6
  • 17
    • 0024519351 scopus 로고
    • Treatment of electrostatic effects in macromolecular modeling
    • Harvey, S. C. Treatment of electrostatic effects in macromolecular modeling. Proteins, 5: 78-92, 1989.
    • (1989) Proteins , vol.5 , pp. 78-92
    • Harvey, S.C.1
  • 19
    • 0032526239 scopus 로고    scopus 로고
    • Isolation and partial characterization of a cDNA encoding a rabbit liver carboxylesterase that activates the prodrug irinotecan (CPT-11)
    • Potter, P. M., Pawlik, C. A., Morton, C. L., Naeve, C. W., and Danks, M. K. Isolation and partial characterization of a cDNA encoding a rabbit liver carboxylesterase that activates the prodrug irinotecan (CPT-11). Cancer Res., 52: 2646-2651, 1998.
    • (1998) Cancer Res. , vol.52 , pp. 2646-2651
    • Potter, P.M.1    Pawlik, C.A.2    Morton, C.L.3    Naeve, C.W.4    Danks, M.K.5
  • 20
    • 0015909845 scopus 로고
    • Colorimetric determination of serum cholinesterase and its genetic variants by the propionyl-thiocholine-dithiobis [nitrobenzoic acid] procedure
    • Dietz, A. A., Rubinstein, H. M., and Lubrano, T. Colorimetric determination of serum cholinesterase and its genetic variants by the propionyl-thiocholine-dithiobis [nitrobenzoic acid] procedure. Clin. Chem., 19: 1309-1313, 1973.
    • (1973) Clin. Chem. , vol.19 , pp. 1309-1313
    • Dietz, A.A.1    Rubinstein, H.M.2    Lubrano, T.3
  • 21
    • 0018079419 scopus 로고
    • A new approach to determining cholinesterase activities in samples of whole blood
    • Augustinsson, K. B., Eriksson, H., and Faijersson, Y. A new approach to determining cholinesterase activities in samples of whole blood. Clin. Chim. Acta. 89: 239-252, 1978.
    • (1978) Clin. Chim. Acta , vol.89 , pp. 239-252
    • Augustinsson, K.B.1    Eriksson, H.2    Faijersson, Y.3
  • 22
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholinesterase activity
    • Ellman, G. L., Courtney, K. D., Anders, V., and Featherstone, R. M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol., 7: 88-95, 1961.
    • (1961) Biochem. Pharmacol. , vol.7 , pp. 88-95
    • Ellman, G.L.1    Courtney, K.D.2    Anders, V.3    Featherstone, R.M.4
  • 23
    • 0023513281 scopus 로고
    • Microtiter assay for acetylcholinesterase
    • Doctor, B. P., Toker, L., Roth, B., and Silman, I. Microtiter assay for acetylcholinesterase. Anal. Biochem., 166: 399-403, 1987.
    • (1987) Anal. Biochem. , vol.166 , pp. 399-403
    • Doctor, B.P.1    Toker, L.2    Roth, B.3    Silman, I.4
  • 25
    • 0031975059 scopus 로고    scopus 로고
    • Overexpression of a rabbit liver carboxylesterase sensitizes human tumor tells to CPT-11
    • Danks, M. K., Morton, C. L., Pawlik, C. A., and Potter, P. M. Overexpression of a rabbit liver carboxylesterase sensitizes human tumor tells to CPT-11. Cancer Res., 58: 20-22, 1998.
    • (1998) Cancer Res. , vol.58 , pp. 20-22
    • Danks, M.K.1    Morton, C.L.2    Pawlik, C.A.3    Potter, P.M.4
  • 27
    • 0032529642 scopus 로고    scopus 로고
    • Cellular localization domains of a rahhit and a human carboxylesterase: Influence on irinotecan (CPT-11) metabolism by the rabbit enzyme
    • Potter, P. M., Wolverton, J. S., Morton, C. L., Wierdl, M., and Danks, M. K. Cellular localization domains of a rahhit and a human carboxylesterase: influence on irinotecan (CPT-11) metabolism by the rabbit enzyme. Cancer Res., 58: 3627-3632, 1998.
    • (1998) Cancer Res. , vol.58 , pp. 3627-3632
    • Potter, P.M.1    Wolverton, J.S.2    Morton, C.L.3    Wierdl, M.4    Danks, M.K.5
  • 28
    • 0008419366 scopus 로고    scopus 로고
    • Responses of neuroblastoma (Nb) xenografts to systemic administration of irinotecan
    • Thompson, J., Houghton, J. A., and Houghton, P. J. Responses of neuroblastoma (Nb) xenografts to systemic administration of irinotecan. Proc. Am. Assoc. Cancer Res., 37: A2976, 1996.
    • (1996) Proc. Am. Assoc. Cancer Res. , vol.37
    • Thompson, J.1    Houghton, J.A.2    Houghton, P.J.3
  • 29
    • 0023758710 scopus 로고
    • Butyrylcholinesterase in human brain and acetylcholinesterase in human plasma: Trace enzymes measured by two-site immunoassay
    • Brimijoin, S., and Hammond, P. Butyrylcholinesterase in human brain and acetylcholinesterase in human plasma: trace enzymes measured by two-site immunoassay. J. Neurochem. 51: 1227-1231, 1988.
    • (1988) J. Neurochem. , vol.51 , pp. 1227-1231
    • Brimijoin, S.1    Hammond, P.2


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