메뉴 건너뛰기




Volumn 75, Issue 5, 2008, Pages 1161-1169

Molecular basis for the interaction of four different classes of substrates and inhibitors with human aromatase

Author keywords

Aromatase inhibitor; Cytochrome P450; Estrogen; Mutagenesis; Structural model

Indexed keywords

AROMATASE; COUMESTROL; DIBENZYLFLUORESCEIN; ESTRADIOL; FLUORESCEIN DERIVATIVE; HEME; METHYLTESTOSTERONE; UNCLASSIFIED DRUG;

EID: 38949101404     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2007.11.010     Document Type: Article
Times cited : (45)

References (35)
  • 2
    • 0028943384 scopus 로고
    • Letrozole (CGS 20267). A phase I study of a new potent oral aromatase inhibitor of breast cancer
    • Lipton A., Demers L.M., Harvey H.A., Kambic K.B., Grossberg H., Brady C., et al. Letrozole (CGS 20267). A phase I study of a new potent oral aromatase inhibitor of breast cancer. Cancer 75 8 (1995) 2132-2138
    • (1995) Cancer , vol.75 , Issue.8 , pp. 2132-2138
    • Lipton, A.1    Demers, L.M.2    Harvey, H.A.3    Kambic, K.B.4    Grossberg, H.5    Brady, C.6
  • 3
    • 0026446844 scopus 로고
    • Phase I and endocrine study of exemestane (FCE 24304), a new aromatase inhibitor, in postmenopausal women
    • Evans T.R., Di Salle E., Ornati G., Lassus M., Benedetti M.S., Pianezzola E., et al. Phase I and endocrine study of exemestane (FCE 24304), a new aromatase inhibitor, in postmenopausal women. Cancer Res 52 21 (1992) 5933-5939
    • (1992) Cancer Res , vol.52 , Issue.21 , pp. 5933-5939
    • Evans, T.R.1    Di Salle, E.2    Ornati, G.3    Lassus, M.4    Benedetti, M.S.5    Pianezzola, E.6
  • 4
    • 7444259675 scopus 로고    scopus 로고
    • A randomized trial of letrozole in postmenopausal women after five years of tamoxifen therapy for early-stage breast cancer
    • Goss P.E., Ingle J.N., Martino S., Robert N.J., Muss H.B., Piccart M.J., et al. A randomized trial of letrozole in postmenopausal women after five years of tamoxifen therapy for early-stage breast cancer. N Engl J Med 349 19 (2003) 1793-1802
    • (2003) N Engl J Med , vol.349 , Issue.19 , pp. 1793-1802
    • Goss, P.E.1    Ingle, J.N.2    Martino, S.3    Robert, N.J.4    Muss, H.B.5    Piccart, M.J.6
  • 5
    • 10744223655 scopus 로고    scopus 로고
    • A randomized trial of exemestane after two to three years of tamoxifen therapy in postmenopausal women with primary breast cancer
    • Coombes R.C., Hall E., Gibson L.J., Paridaens R., Jassem J., Delozier T., et al. A randomized trial of exemestane after two to three years of tamoxifen therapy in postmenopausal women with primary breast cancer. N Engl J Med 350 11 (2004) 1081-1092
    • (2004) N Engl J Med , vol.350 , Issue.11 , pp. 1081-1092
    • Coombes, R.C.1    Hall, E.2    Gibson, L.J.3    Paridaens, R.4    Jassem, J.5    Delozier, T.6
  • 6
    • 0037157603 scopus 로고    scopus 로고
    • Anastrozole alone or in combination with tamoxifen versus tamoxifen alone for adjuvant treatment of postmenopausal women with early breast cancer: first results of the ATAC randomised trial
    • Baum M., Budzar A.U., Cuzick J., Forbes J., Houghton J.H., Klijn J.G., et al. Anastrozole alone or in combination with tamoxifen versus tamoxifen alone for adjuvant treatment of postmenopausal women with early breast cancer: first results of the ATAC randomised trial. Lancet 359 9324 (2002) 2131-2139
    • (2002) Lancet , vol.359 , Issue.9324 , pp. 2131-2139
    • Baum, M.1    Budzar, A.U.2    Cuzick, J.3    Forbes, J.4    Houghton, J.H.5    Klijn, J.G.6
  • 7
    • 0034669484 scopus 로고    scopus 로고
    • Anastrozole is superior to tamoxifen as first-line therapy for advanced breast cancer in postmenopausal women: results of a North American multicenter randomized trial. Arimidex Study Group
    • Nabholtz J.M., Buzdar A., Pollak M., Harwin W., Burton G., Mangalik A., et al. Anastrozole is superior to tamoxifen as first-line therapy for advanced breast cancer in postmenopausal women: results of a North American multicenter randomized trial. Arimidex Study Group. J Clin Oncol 18 22 (2000) 3758-3767
    • (2000) J Clin Oncol , vol.18 , Issue.22 , pp. 3758-3767
    • Nabholtz, J.M.1    Buzdar, A.2    Pollak, M.3    Harwin, W.4    Burton, G.5    Mangalik, A.6
  • 10
    • 10744231992 scopus 로고    scopus 로고
    • Structure-function studies of aromatase and its inhibitors: a progress report
    • Chen S., Zhang F., Sherman M.A., Kijima I., Cho M., Yuan Y.C., et al. Structure-function studies of aromatase and its inhibitors: a progress report. J Steroid Biochem Mol Biol 86 3-5 (2003) 231-237
    • (2003) J Steroid Biochem Mol Biol , vol.86 , Issue.3-5 , pp. 231-237
    • Chen, S.1    Zhang, F.2    Sherman, M.A.3    Kijima, I.4    Cho, M.5    Yuan, Y.C.6
  • 11
    • 0034819384 scopus 로고    scopus 로고
    • Evaluation of the mechanism of aromatase cytochrome P450. A site-directed mutagenesis study
    • Kao Y.C., Korzekwa K.R., Laughton C.A., and Chen S. Evaluation of the mechanism of aromatase cytochrome P450. A site-directed mutagenesis study. Eur J Biochem 268 2 (2001) 243-251
    • (2001) Eur J Biochem , vol.268 , Issue.2 , pp. 243-251
    • Kao, Y.C.1    Korzekwa, K.R.2    Laughton, C.A.3    Chen, S.4
  • 12
    • 0031124888 scopus 로고    scopus 로고
    • Binding characteristics of aromatase inhibitors and phytoestrogens to human aromatase
    • Chen S., Kao Y.C., and Laughton C.A. Binding characteristics of aromatase inhibitors and phytoestrogens to human aromatase. J Steroid Biochem Mol Biol 61 3-6 (1997) 107-115
    • (1997) J Steroid Biochem Mol Biol , vol.61 , Issue.3-6 , pp. 107-115
    • Chen, S.1    Kao, Y.C.2    Laughton, C.A.3
  • 13
    • 0030013560 scopus 로고    scopus 로고
    • Binding characteristics of seven inhibitors of human aromatase: a site-directed mutagenesis study
    • Kao Y.C., Cam L.L., Laughton C.A., Zhou D., and Chen S. Binding characteristics of seven inhibitors of human aromatase: a site-directed mutagenesis study. Cancer Res 56 15 (1996) 3451-3460
    • (1996) Cancer Res , vol.56 , Issue.15 , pp. 3451-3460
    • Kao, Y.C.1    Cam, L.L.2    Laughton, C.A.3    Zhou, D.4    Chen, S.5
  • 14
    • 33644836657 scopus 로고    scopus 로고
    • Three-dimensional model of the human aromatase enzyme and density functional parameterization of the iron-containing protoporphyrin IX for a molecular dynamics study of heme-cysteinato cytochromes
    • Favia A.D., Cavalli A., Masetti M., Carotti A., and Recanatini M. Three-dimensional model of the human aromatase enzyme and density functional parameterization of the iron-containing protoporphyrin IX for a molecular dynamics study of heme-cysteinato cytochromes. Proteins 62 4 (2006) 1074-1087
    • (2006) Proteins , vol.62 , Issue.4 , pp. 1074-1087
    • Favia, A.D.1    Cavalli, A.2    Masetti, M.3    Carotti, A.4    Recanatini, M.5
  • 15
    • 33846619697 scopus 로고    scopus 로고
    • Molecular basis for the aromatization reaction and exemestane-mediated irreversible inhibition of human aromatase
    • Hong Y., Yu B., Sherman M., Yuan Y.C., Zhou D., and Chen S. Molecular basis for the aromatization reaction and exemestane-mediated irreversible inhibition of human aromatase. Mol Endocrinol 21 2 (2007) 401-414
    • (2007) Mol Endocrinol , vol.21 , Issue.2 , pp. 401-414
    • Hong, Y.1    Yu, B.2    Sherman, M.3    Yuan, Y.C.4    Zhou, D.5    Chen, S.6
  • 16
    • 0347479344 scopus 로고    scopus 로고
    • Mechanistic basis for estrogenic effects in fathead minnow (Pimephales promelas) following exposure to the androgen 17alpha-methyltestosterone: conversion of 17alpha-methyltestosterone to 17alpha-methylestradiol
    • Hornung M.W., Jensen K.M., Korte J.J., Kahl M.D., Durhan E.J., Denny J.S., et al. Mechanistic basis for estrogenic effects in fathead minnow (Pimephales promelas) following exposure to the androgen 17alpha-methyltestosterone: conversion of 17alpha-methyltestosterone to 17alpha-methylestradiol. Aquat Toxicol 66 1 (2004) 15-23
    • (2004) Aquat Toxicol , vol.66 , Issue.1 , pp. 15-23
    • Hornung, M.W.1    Jensen, K.M.2    Korte, J.J.3    Kahl, M.D.4    Durhan, E.J.5    Denny, J.S.6
  • 17
    • 38949167509 scopus 로고    scopus 로고
    • Miller VP, Streser D, Crespi CL. Use of fluorescein aryl ethers in high throughput cytochrome P450 inhibition assays. United States Patent US 6,420,131 B1; 2002.
    • Miller VP, Streser D, Crespi CL. Use of fluorescein aryl ethers in high throughput cytochrome P450 inhibition assays. United States Patent US 6,420,131 B1; 2002.
  • 19
    • 0025089197 scopus 로고
    • Stable expression of human aromatase complementary DNA in mammalian cells: a useful system for aromatase inhibitor screening
    • Zhou D.P.D., and Chen S. Stable expression of human aromatase complementary DNA in mammalian cells: a useful system for aromatase inhibitor screening. Cancer Res 50 (1990) 6949-6954
    • (1990) Cancer Res , vol.50 , pp. 6949-6954
    • Zhou, D.P.D.1    Chen, S.2
  • 20
    • 0025089197 scopus 로고
    • Stable expression of human aromatase complementary DNA in mammalian cells: a useful system for aromatase inhibitor screening
    • Zhou D.J., Pompon D., and Chen S.A. Stable expression of human aromatase complementary DNA in mammalian cells: a useful system for aromatase inhibitor screening. Cancer Res 50 21 (1990) 6949-6954
    • (1990) Cancer Res , vol.50 , Issue.21 , pp. 6949-6954
    • Zhou, D.J.1    Pompon, D.2    Chen, S.A.3
  • 21
    • 0036829928 scopus 로고    scopus 로고
    • Expression and purification of a recombinant form of human aromatase from Escherichia coli
    • Zhang F., Zhou D., Kao Y.C., Ye J., and Chen S. Expression and purification of a recombinant form of human aromatase from Escherichia coli. Biochem Pharmacol 64 9 (2002) 1317-1324
    • (2002) Biochem Pharmacol , vol.64 , Issue.9 , pp. 1317-1324
    • Zhang, F.1    Zhou, D.2    Kao, Y.C.3    Ye, J.4    Chen, S.5
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0031915796 scopus 로고    scopus 로고
    • Molecular basis of the inhibition of human aromatase (estrogen synthetase) by flavone and isoflavone phytoestrogens: A site-directed mutagenesis study
    • Kao Y.C., Zhou C., Sherman M., Laughton C.A., and Chen S. Molecular basis of the inhibition of human aromatase (estrogen synthetase) by flavone and isoflavone phytoestrogens: A site-directed mutagenesis study. Environ Health Perspect 106 2 (1998) 85-92
    • (1998) Environ Health Perspect , vol.106 , Issue.2 , pp. 85-92
    • Kao, Y.C.1    Zhou, C.2    Sherman, M.3    Laughton, C.A.4    Chen, S.5
  • 24
    • 0015337522 scopus 로고
    • Differences in the cytochrome P-450S from resistant and susceptible house flies
    • Philpot R.M., and Hodgson E. Differences in the cytochrome P-450S from resistant and susceptible house flies. Chem Biol Interact 4 6 (1972) 399-408
    • (1972) Chem Biol Interact , vol.4 , Issue.6 , pp. 399-408
    • Philpot, R.M.1    Hodgson, E.2
  • 25
    • 0015605693 scopus 로고
    • Cytochrome P-450 difference spectra of microsomes from several insecticide-resistant and -susceptible strains of the housefly, Musca domestica L.
    • Tate L.G., Plapp F.W., and Hodgson E. Cytochrome P-450 difference spectra of microsomes from several insecticide-resistant and -susceptible strains of the housefly, Musca domestica L. Chem Biol Interact 6 4 (1973) 237-247
    • (1973) Chem Biol Interact , vol.6 , Issue.4 , pp. 237-247
    • Tate, L.G.1    Plapp, F.W.2    Hodgson, E.3
  • 26
    • 0035544730 scopus 로고    scopus 로고
    • 17alpha-methyl testosterone is a competitive inhibitor of aromatase activity in Jar choriocarcinoma cells and macrophage-like THP-1 cells in culture
    • Mor G., Eliza M., Song J., Wiita B., Chen S., and Naftolin F. 17alpha-methyl testosterone is a competitive inhibitor of aromatase activity in Jar choriocarcinoma cells and macrophage-like THP-1 cells in culture. J Steroid Biochem Mol Biol 79 1-5 (2001) 239-246
    • (2001) J Steroid Biochem Mol Biol , vol.79 , Issue.1-5 , pp. 239-246
    • Mor, G.1    Eliza, M.2    Song, J.3    Wiita, B.4    Chen, S.5    Naftolin, F.6
  • 27
    • 31044449968 scopus 로고    scopus 로고
    • Inhibition of human CYP19 by azoles used as antifungal agents and aromatase inhibitors, using a new LC-MS/MS method for the analysis of estradiol product formation
    • Trosken E.R., Fischer K., Volkel W., and Lutz W.K. Inhibition of human CYP19 by azoles used as antifungal agents and aromatase inhibitors, using a new LC-MS/MS method for the analysis of estradiol product formation. Toxicology 219 1-3 (2006) 33-40
    • (2006) Toxicology , vol.219 , Issue.1-3 , pp. 33-40
    • Trosken, E.R.1    Fischer, K.2    Volkel, W.3    Lutz, W.K.4
  • 29
    • 0018533128 scopus 로고
    • The interaction of aliphatic analogs of methylene-dioxyphenyl compounds with cytochromes P-450 and P-420
    • Dahl A.R., and Hodgson E. The interaction of aliphatic analogs of methylene-dioxyphenyl compounds with cytochromes P-450 and P-420. Chem Biol Interact 27 2-3 (1979) 163-175
    • (1979) Chem Biol Interact , vol.27 , Issue.2-3 , pp. 163-175
    • Dahl, A.R.1    Hodgson, E.2
  • 30
    • 0002892893 scopus 로고    scopus 로고
    • Piperonylic acid, a selective, mechanism-based inactivator of the trans-cinnamate 4-hydroxylase: a new tool to control the flux of metabolites in the phenylpropanoid pathway
    • Schalk M., Cabello-Hurtado F., Pierrel M.A., Atanossova R., Saindrenan P., and Werck-Reichhart D. Piperonylic acid, a selective, mechanism-based inactivator of the trans-cinnamate 4-hydroxylase: a new tool to control the flux of metabolites in the phenylpropanoid pathway. Plant Physiol 118 1 (1998) 209-218
    • (1998) Plant Physiol , vol.118 , Issue.1 , pp. 209-218
    • Schalk, M.1    Cabello-Hurtado, F.2    Pierrel, M.A.3    Atanossova, R.4    Saindrenan, P.5    Werck-Reichhart, D.6
  • 31
    • 0021871058 scopus 로고
    • Spectral and inhibitory interactions of methylenedioxyphenyl and related compounds with purified isozymes of cytochrome P-450
    • Marcus C.B., Murray M., and Wilkinson C.F. Spectral and inhibitory interactions of methylenedioxyphenyl and related compounds with purified isozymes of cytochrome P-450. Xenobiotica 15 4 (1985) 351-362
    • (1985) Xenobiotica , vol.15 , Issue.4 , pp. 351-362
    • Marcus, C.B.1    Murray, M.2    Wilkinson, C.F.3
  • 32
    • 0031466805 scopus 로고    scopus 로고
    • In vitro and in vivo effects of the arylamine human immunodeficiency virus protease inhibitor 4R-(4alpha,5alpha,6beta, 7beta)-1-[(3-(1-imidazoylcarbamoyl)phenyl)methyl]-3-[(3-aminophenyl)methyl]hexahydro-5,6-dihydroxy-4,7-bis(phenylmethyl)-2H-1,3-diazepin-2-one (SD894) on rat hepatic cytochrome P450 2B and 3A
    • Grubb M.F., Diamond S., and Christ D.D. In vitro and in vivo effects of the arylamine human immunodeficiency virus protease inhibitor 4R-(4alpha,5alpha,6beta, 7beta)-1-[(3-(1-imidazoylcarbamoyl)phenyl)methyl]-3-[(3-aminophenyl)methyl]hexahydro-5,6-dihydroxy-4,7-bis(phenylmethyl)-2H-1,3-diazepin-2-one (SD894) on rat hepatic cytochrome P450 2B and 3A. Drug Metab Dispos 25 12 (1997) 1424-1428
    • (1997) Drug Metab Dispos , vol.25 , Issue.12 , pp. 1424-1428
    • Grubb, M.F.1    Diamond, S.2    Christ, D.D.3
  • 33
    • 0017101722 scopus 로고
    • Methylenedioxyphenyl insecticide synergists as potential human health hazards
    • Franklin M.R. Methylenedioxyphenyl insecticide synergists as potential human health hazards. Environ Health Perspect 14 (1976) 29-37
    • (1976) Environ Health Perspect , vol.14 , pp. 29-37
    • Franklin, M.R.1
  • 34
    • 0019412167 scopus 로고
    • Self-induction by triacetyloleandomycin of its own transformation into a metabolite forming a stable 456 nm-absorbing complex with cytochrome P-450
    • Pessayre D., Descatoire V., Konstantinova-Mitcheva M., Wandscheer J.C., Cobert B., Level R., et al. Self-induction by triacetyloleandomycin of its own transformation into a metabolite forming a stable 456 nm-absorbing complex with cytochrome P-450. Biochem Pharmacol 30 6 (1981) 553-558
    • (1981) Biochem Pharmacol , vol.30 , Issue.6 , pp. 553-558
    • Pessayre, D.1    Descatoire, V.2    Konstantinova-Mitcheva, M.3    Wandscheer, J.C.4    Cobert, B.5    Level, R.6
  • 35
    • 9144269994 scopus 로고    scopus 로고
    • Biochemical and biological characterization of a novel anti-aromatase coumarin derivative
    • Chen S., Cho M., Karlsberg K., Zhou D., and Yuan Y.C. Biochemical and biological characterization of a novel anti-aromatase coumarin derivative. J Biol Chem 279 46 (2004) 48071-48078
    • (2004) J Biol Chem , vol.279 , Issue.46 , pp. 48071-48078
    • Chen, S.1    Cho, M.2    Karlsberg, K.3    Zhou, D.4    Yuan, Y.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.