메뉴 건너뛰기




Volumn 147, Issue 2, 2004, Pages 129-139

Enzymology of a carbonyl reduction clearance pathway for the HIV integrase inhibitor, S-1360: Role of human liver cytosolic aldo-keto reductases

Author keywords

AKR; Aldo keto reductase; Carbonyl reductase; CR; HIV; HP1; Human immunodeficiency virus; Human plasma metabolite 1; Liquid scintillation counter; LSC; NAD(P)H:quinone oxidoreductase 1; NQO1; NQO2; NRH:quinone oxidoreductase 2; SDR

Indexed keywords

1 [5 (4 FLUOROBENZYL) 2 FURYL] 3 (1,2,4 TRIAZOL 3 YL) 1,3 PROPANEDIONE; ALDEHYDE KETONE REDUCTASE; ALDOKETOREDUCTASE INHIBITOR; CARBONYL DERIVATIVE; CARBONYL REDUCTASE; CARBONYL REDUCTASE INHIBITOR; DIKETONE; DRUG METABOLITE; ENZYME INHIBITOR; FLUFENAMIC ACID; INTEGRASE INHIBITOR; MENADIONE; OXIDOREDUCTASE; PHENOLPHTHALEIN; PROTEIN; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 1542286600     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2003.12.001     Document Type: Article
Times cited : (94)

References (43)
  • 1
    • 0023852121 scopus 로고
    • The human immunodeficiency virus: Infectivity and mechanisms of pathogenesis
    • Fauci A.S. The human immunodeficiency virus: infectivity and mechanisms of pathogenesis. Science. 239:1988;617-622.
    • (1988) Science , vol.239 , pp. 617-622
    • Fauci, A.S.1
  • 2
    • 0022038928 scopus 로고
    • Molecular organization of the AIDS retrovirus
    • Rabson A.B., Martin M.A. Molecular organization of the AIDS retrovirus. Cell. 40:1985;477-480.
    • (1985) Cell , vol.40 , pp. 477-480
    • Rabson, A.B.1    Martin, M.A.2
  • 4
    • 0035160478 scopus 로고    scopus 로고
    • New developments in anti-HIV chemotherapy
    • De Clercq E. New developments in anti-HIV chemotherapy. Curr. Med. Chem. 8:2001;1543-1572.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1543-1572
    • De Clercq, E.1
  • 6
    • 0035428051 scopus 로고    scopus 로고
    • Unexploited viral and host targets for the treatment of human immunodeficiency virus type I infection
    • Garvey E.P. Unexploited viral and host targets for the treatment of human immunodeficiency virus type I infection. Curr. Drug Target. 1:2001;107-123.
    • (2001) Curr. Drug Target. , vol.1 , pp. 107-123
    • Garvey, E.P.1
  • 7
    • 0036107683 scopus 로고    scopus 로고
    • Patented small molecule inhibitors of HIV-1 integrase: A 10-year saga
    • Neamati N. Patented small molecule inhibitors of HIV-1 integrase: a 10-year saga. Expert Opin. Ther. Patents. 12:2002;709-724.
    • (2002) Expert Opin. Ther. Patents , vol.12 , pp. 709-724
    • Neamati, N.1
  • 8
    • 0034600004 scopus 로고    scopus 로고
    • Molecular and structural aspects of xenobiotic carbonyl metabolising enzymes. Role of reductases and dehydrogenases in xenobiotic phase I reactions
    • Oppermann U.C.T., Maser E. Molecular and structural aspects of xenobiotic carbonyl metabolising enzymes. Role of reductases and dehydrogenases in xenobiotic phase I reactions. Toxicology. 144:2000;71-81.
    • (2000) Toxicology , vol.144 , pp. 71-81
    • Oppermann, U.C.T.1    Maser, E.2
  • 9
    • 0037058244 scopus 로고    scopus 로고
    • The metabolic activation of abacavir by human liver cytosol and expressed human alcohol dehydrogenase isozymes
    • Walsh J.S., Reese M.J., Thurmond L.M. The metabolic activation of abacavir by human liver cytosol and expressed human alcohol dehydrogenase isozymes. Chem. Biol. Interact. 142:2002;135-154.
    • (2002) Chem. Biol. Interact. , vol.142 , pp. 135-154
    • Walsh, J.S.1    Reese, M.J.2    Thurmond, L.M.3
  • 10
    • 0033852886 scopus 로고    scopus 로고
    • Purification and characterization of oxidoreductases catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)- 1-butanone (NNK) in human liver cytosol
    • Atalla A., Breyer-Pfaff U., Maser E. Purification and characterization of oxidoreductases catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human liver cytosol. Xenobiotica. 30:2000;755-769.
    • (2000) Xenobiotica , vol.30 , pp. 755-769
    • Atalla, A.1    Breyer-Pfaff, U.2    Maser, E.3
  • 12
    • 0028896435 scopus 로고
    • Kinetic studies of the inhibition of a human liver 3α- hydroxysteroid/dihydrodiol dehydrogenase isozyme by bile acids and anti-inflammatory drugs
    • Miyabe Y., Amano T., Deyashiki Y., Hara A., Tsukada F. Kinetic studies of the inhibition of a human liver 3α-hydroxysteroid/dihydrodiol dehydrogenase isozyme by bile acids and anti-inflammatory drugs. Biol. Pharm. Bull. 18:1995;9-12.
    • (1995) Biol. Pharm. Bull. , vol.18 , pp. 9-12
    • Miyabe, Y.1    Amano, T.2    Deyashiki, Y.3    Hara, A.4    Tsukada, F.5
  • 15
    • 0037324955 scopus 로고    scopus 로고
    • Coenzyme-based functional assignments of short-chain dehydrogenases/ reductases (SDRs)
    • Persson B., Kallberg Y., Oppermann U., Jörnvall H. Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 143-144:2003;271-278.
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 271-278
    • Persson, B.1    Kallberg, Y.2    Oppermann, U.3    Jörnvall, H.4
  • 17
    • 0034531564 scopus 로고    scopus 로고
    • NAD(P)H:quinone oxidoreductase 1 (NQO1): Chemoprotection, bioactivation, gene regulation and genetic polymorphisms
    • Ross D., Kepa J.K., Winski S.L., Beall H.D., Anwar A., Siegel D. NAD(P)H:quinone oxidoreductase 1 (NQO1): chemoprotection, bioactivation, gene regulation and genetic polymorphisms. Chem. Biol. Interact. 129:2000;77-97.
    • (2000) Chem. Biol. Interact. , vol.129 , pp. 77-97
    • Ross, D.1    Kepa, J.K.2    Winski, S.L.3    Beall, H.D.4    Anwar, A.5    Siegel, D.6
  • 19
    • 0034105896 scopus 로고    scopus 로고
    • In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model
    • Houston J.B., Kenworthy K.E. In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model. Drug Metab. Dispos. 28:2000;246-254.
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 246-254
    • Houston, J.B.1    Kenworthy, K.E.2
  • 20
    • 0036201594 scopus 로고    scopus 로고
    • Atypical kinetic profiles in drug metabolism reactions
    • Hutzler J.M., Tracy T.S. Atypical kinetic profiles in drug metabolism reactions. Drug Metab. Dispos. 30:2002;355-362.
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 355-362
    • Hutzler, J.M.1    Tracy, T.S.2
  • 21
    • 0032968065 scopus 로고    scopus 로고
    • Sigmoidal kinetics of CYP3A substrates: An approach for scaling dextromethorphan metabolism in hepatic microsomes and isolated hepatocytes to predict in vivo clearance in rat
    • Witherow L.E., Houston J.B. Sigmoidal kinetics of CYP3A substrates: an approach for scaling dextromethorphan metabolism in hepatic microsomes and isolated hepatocytes to predict in vivo clearance in rat. J. Pharmacol. Exp. Ther. 290:1999;58-65.
    • (1999) J. Pharmacol. Exp. Ther. , vol.290 , pp. 58-65
    • Witherow, L.E.1    Houston, J.B.2
  • 22
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites
    • Korzekwa K.R., Krishnamachary N., Shou M., Ogai A., Parise R.A., Rettie A.E., Gonzales F.J., Tracy T.S. Evaluation of atypical cytochrome P450 kinetics with two-substrate models: evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites. Biochemistry. 37:1998;4137-4147.
    • (1998) Biochemistry , vol.37 , pp. 4137-4147
    • Korzekwa, K.R.1    Krishnamachary, N.2    Shou, M.3    Ogai, A.4    Parise, R.A.5    Rettie, A.E.6    Gonzales, F.J.7    Tracy, T.S.8
  • 23
    • 0033987020 scopus 로고    scopus 로고
    • High-affinity stereoselective reduction of the enantiomers of ketotifen and of ketonic nortriptyline metabolites by aldo-keto reductases from human liver
    • Breyer-Pfaff U., Nill K. High-affinity stereoselective reduction of the enantiomers of ketotifen and of ketonic nortriptyline metabolites by aldo-keto reductases from human liver. Biochem. Pharmacol. 59:2000;249-260.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 249-260
    • Breyer-Pfaff, U.1    Nill, K.2
  • 24
    • 0028998039 scopus 로고
    • Reduction of drug ketones by dihydrodiol dehydrogenases, carbonyl reductase and aldehyde reductase of human liver
    • Ohara H., Miyabe Y., Deyashiki Y., Matsuura K., Hara A. Reduction of drug ketones by dihydrodiol dehydrogenases, carbonyl reductase and aldehyde reductase of human liver. Biochem. Pharmacol. 50:1995;221-227.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 221-227
    • Ohara, H.1    Miyabe, Y.2    Deyashiki, Y.3    Matsuura, K.4    Hara, A.5
  • 25
    • 0033983383 scopus 로고    scopus 로고
    • Carbonyl reduction of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) by cytosolic enzymes in human liver and lung
    • Maser E., Stinner B., Atalla A. Carbonyl reduction of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) by cytosolic enzymes in human liver and lung. Cancer Lett. 148:2000;135-144.
    • (2000) Cancer Lett. , vol.148 , pp. 135-144
    • Maser, E.1    Stinner, B.2    Atalla, A.3
  • 26
    • 0004262303 scopus 로고
    • Academic Press, New York
    • M. Dixon, E.C. Webb, Enzymes, Academic Press, New York, 1979, pp. 332-467.
    • (1979) Enzymes , pp. 332-467
    • Dixon, M.1    Webb, E.C.2
  • 27
    • 0026568286 scopus 로고
    • Stereoselective acetonyl side chain reduction of warfarin and analogs: Partial characterization of two cytosolic carbonyl reductases
    • Hermans J.J.R., Thijssen H.H.W. Stereoselective acetonyl side chain reduction of warfarin and analogs: partial characterization of two cytosolic carbonyl reductases. Drug Metab. Dispos. 20:1992;268-274.
    • (1992) Drug Metab. Dispos. , vol.20 , pp. 268-274
    • Hermans, J.J.R.1    Thijssen, H.H.W.2
  • 28
    • 0032400498 scopus 로고    scopus 로고
    • Roles of C-terminal binding domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: Probing with chimaeric enzymes
    • Matsuura K., Hara A., Deyashiki Y., Iwasa H., Kume T., Ishikura S., Shiraishi H., Katagiri Y. Roles of C-terminal binding domains of human dihydrodiol dehydrogenase isoforms in the binding of substrates and modulators: probing with chimaeric enzymes. Biochem. J. 336:1998;429-436.
    • (1998) Biochem. J. , vol.336 , pp. 429-436
    • Matsuura, K.1    Hara, A.2    Deyashiki, Y.3    Iwasa, H.4    Kume, T.5    Ishikura, S.6    Shiraishi, H.7    Katagiri, Y.8
  • 30
    • 0036547847 scopus 로고    scopus 로고
    • Substrate specificity of human 3(20)α-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines
    • Usami N., Yamamoto T., Shintani S., Higaku Y., Ishikura S., Katagiri Y., Hara A. Substrate specificity of human 3(20)α-hydroxysteroid dehydrogenase for neurosteroids and its inhibition by benzodiazepines. Biol. Pharm. Bull. 25:2002;441-445.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 441-445
    • Usami, N.1    Yamamoto, T.2    Shintani, S.3    Higaku, Y.4    Ishikura, S.5    Katagiri, Y.6    Hara, A.7
  • 31
    • 0026552524 scopus 로고
    • Structural and functional comparison of two human liver dihydrodiol dehydrogenases associated with 3α-hydroxysteroid dehydrogenase activity
    • Deyashiki Y., Taniguchi H., Amano T., Nakayama T., Hara A., Sawada H. Structural and functional comparison of two human liver dihydrodiol dehydrogenases associated with 3α-hydroxysteroid dehydrogenase activity. Biochem. J. 282:1992;741-746.
    • (1992) Biochem. J. , vol.282 , pp. 741-746
    • Deyashiki, Y.1    Taniguchi, H.2    Amano, T.3    Nakayama, T.4    Hara, A.5    Sawada, H.6
  • 33
    • 0345084436 scopus 로고    scopus 로고
    • The multidrug resistance modulator valspodar (PSC 833) is metabolized by human cytochrome P450 3A: Implications for drug-drug interactions and pharmacological activity of the main metabolite
    • Fischer V., Rodríguez-Gascón A., Heitz F., Tynes R., Hauck C., Cohen D., Vickers A.E.M. The multidrug resistance modulator valspodar (PSC 833) is metabolized by human cytochrome P450 3A: implications for drug-drug interactions and pharmacological activity of the main metabolite. Drug Metab. Dispos. 26:1998;802-811.
    • (1998) Drug Metab. Dispos. , vol.26 , pp. 802-811
    • Fischer, V.1    Rodríguez-Gascón, A.2    Heitz, F.3    Tynes, R.4    Hauck, C.5    Cohen, D.6    Vickers, A.E.M.7
  • 34
    • 0017258828 scopus 로고
    • Adriamycin metabolism in man: Evidence from urinary metabolites
    • Takanashi S., Bachur N.R. Adriamycin metabolism in man: evidence from urinary metabolites. Drug Metab. Dispos. 4:1976;79-87.
    • (1976) Drug Metab. Dispos. , vol.4 , pp. 79-87
    • Takanashi, S.1    Bachur, N.R.2
  • 35
    • 0033738822 scopus 로고    scopus 로고
    • Kinetics and inhibition of the formation of 6-naltrexol from naltrexone in human liver cytosol
    • Porter S.J., Somogyi A.A., White J.M. Kinetics and inhibition of the formation of 6-naltrexol from naltrexone in human liver cytosol. Br. J. Clin. Pharmacol. 50:2000;465-471.
    • (2000) Br. J. Clin. Pharmacol. , vol.50 , pp. 465-471
    • Porter, S.J.1    Somogyi, A.A.2    White, J.M.3
  • 39
    • 0037325532 scopus 로고    scopus 로고
    • Purification, characterization and NNK carbonyl reductase activities of 11β-hydroxysteroid dehydrogenase type I from human liver: Enzyme cooperativity and significance in the detoxification of a tobacco-derived carcinogen
    • Maser E., Friebertshäuser J., Völker B. Purification, characterization and NNK carbonyl reductase activities of 11β- hydroxysteroid dehydrogenase type I from human liver: enzyme cooperativity and significance in the detoxification of a tobacco-derived carcinogen. Chem. Biol. Interact. 143-144:2003;435-448.
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 435-448
    • Maser, E.1    Friebertshäuser, J.2    Völker, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.