메뉴 건너뛰기




Volumn 27, Issue 3, 2004, Pages 319-323

High-level expression of human cytochrome P450 3A4 by co-expression with human molecular chaperone HDJ-1 (Hsp40)

Author keywords

Chaperone; Co expresion; CYP3A4; HDJ 1

Indexed keywords

CHAPERONE; CYP3A PROTEIN, HUMAN; CYP3A4 PROTEIN, HUMAN; CYTOCHROME P450; DNAJB1 PROTEIN, HUMAN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40;

EID: 7044231916     PISSN: 02536269     EISSN: 02536269     Source Type: Journal    
DOI: 10.1007/BF02980067     Document Type: Article
Times cited : (14)

References (18)
  • 1
    • 0026324283 scopus 로고
    • Measurement of steroid hydroxylation reactions by high-performance liquid chromatography as indicator of P450 identity and function
    • Arlotto, M. P., Trant, J. M., and Estabrook, R. W., Measurement of steroid hydroxylation reactions by high-performance liquid chromatography as indicator of P450 identity and function. Methods Enzymol., 206, 454-462 (1991).
    • (1991) Methods Enzymol. , vol.206 , pp. 454-462
    • Arlotto, M.P.1    Trant, J.M.2    Estabrook, R.W.3
  • 2
    • 0037023781 scopus 로고    scopus 로고
    • Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy
    • Bao, Y. P., Cook, L. J., ODonovan, D., Uyama, E., and Rubinsztein, D. C., Mammalian, yeast, bacterial, and chemical chaperones reduce aggregate formation and death in a cell model of oculopharyngeal muscular dystrophy. J. Biol. Chem., 277, 12263-12269 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12263-12269
    • Bao, Y.P.1    Cook, L.J.2    Odonovan, D.3    Uyama, E.4    Rubinsztein, D.C.5
  • 3
    • 0022263133 scopus 로고
    • Purification and characterization of the human liver cytochromes P-450 involved in debrisoquine 4-hydroxylation and phenacetin O-deethylation, two prototypes for genetic polymorphism in oxidative drug metabolism
    • Distlerath, L. M., Reilly, P. E., Martin, M. V., Davis, G. G., Wilkinson, G. R., and Guengerich, F. P., Purification and characterization of the human liver cytochromes P-450 involved in debrisoquine 4-hydroxylation and phenacetin O-deethylation, two prototypes for genetic polymorphism in oxidative drug metabolism. J. Biol. Chem., 260, 9057-9067 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 9057-9067
    • Distlerath, L.M.1    Reilly, P.E.2    Martin, M.V.3    Davis, G.G.4    Wilkinson, G.R.5    Guengerich, F.P.6
  • 4
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman, B. C. and Morimoto, R. I., The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J., 15, 2969-2979 (1996).
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 5
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillam, E. M., Baba, T., Kim, B. R., Ohmori, S., and Guengerich, F. P. Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys., 305, 123-131 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 123-131
    • Gillam, E.M.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5
  • 6
    • 0030660647 scopus 로고    scopus 로고
    • Expression of drug-metabolizing enzymes
    • Guengerich, F. P. and Parikh, A., Expression of drug-metabolizing enzymes. Curr. Opin. Biotechnol., 8, 623-628 (1997).
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 623-628
    • Guengerich, F.P.1    Parikh, A.2
  • 7
    • 0002888510 scopus 로고
    • Human cytochrome P450 enzymes
    • Oritiz de Montelano, P. R. (Ed.). Plenum Press, New York
    • nd ed. Plenum Press, New York, pp.473-535 (1995).
    • (1995) nd Ed. , pp. 473-535
    • Guengerich, F.P.1
  • 8
    • 0031822496 scopus 로고    scopus 로고
    • Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities
    • Hanna, I. H., Teiber, J. F., Kokones, K. L., and Hollenberg, P. F., Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities. Arch. Biochem. Biophys., 350, 324-332 (1998).
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 324-332
    • Hanna, I.H.1    Teiber, J.F.2    Kokones, K.L.3    Hollenberg, P.F.4
  • 9
    • 0034673581 scopus 로고    scopus 로고
    • Development of bacterial expression system with high yield of CYP3A7, a human fetus-specific form of cytochrome P450
    • Inoue, E., Takahashi, Y., Imai, Y., and Kamataki, T., Development of bacterial expression system with high yield of CYP3A7, a human fetus-specific form of cytochrome P450. Biochem. Biophys. Res. Commun., 269, 623-627 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 623-627
    • Inoue, E.1    Takahashi, Y.2    Imai, Y.3    Kamataki, T.4
  • 10
    • 0032522904 scopus 로고    scopus 로고
    • High catalytic activity of human cytochrome P450 co-expressed with human NADPH-cytochrome P450 reductase in Escherichia coli
    • Iwata, H., Fujita, K-I., Kushida, H., Suzuki, A., Konno, Y., Nakamura, K., Fujino, A., and Kamataki, T., High catalytic activity of human cytochrome P450 co-expressed with human NADPH-cytochrome P450 reductase in Escherichia coli. Biochem. Pharmacol., 55, 1315-1325 (1998).
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1315-1325
    • Iwata, H.1    Fujita, K.-I.2    Kushida, H.3    Suzuki, A.4    Konno, Y.5    Nakamura, K.6    Fujino, A.7    Kamataki, T.8
  • 11
    • 0032510812 scopus 로고    scopus 로고
    • Mammalian cytosolic DnaJ homologues affect the hsp70 chaperone-substrate reaction cycle, but do not interact directly with nascent or newly synthesized proteins
    • Nagata, H., Hansen, W. J., Freeman, B., and Welch, W. J., Mammalian cytosolic DnaJ homologues affect the hsp70 chaperone-substrate reaction cycle, but do not interact directly with nascent or newly synthesized proteins. Biochemistry, 37, 6924-6938 (1998).
    • (1998) Biochemistry , vol.37 , pp. 6924-6938
    • Nagata, H.1    Hansen, W.J.2    Freeman, B.3    Welch, W.J.4
  • 12
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T. and Sato, R., The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem., 239, 2370-2378 (1964).
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 13
    • 0031127850 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a catalytically active human cytochrome P450 3A4: Rat NADPH-cytochrome P450 fusion protein
    • Parikh, A. and Guengerich, F. P., Expression, purification, and characterization of a catalytically active human cytochrome P450 3A4: Rat NADPH-cytochrome P450 fusion protein. Protein Expr. Purif., 9, 346-354 (1997).
    • (1997) Protein Expr. Purif. , vol.9 , pp. 346-354
    • Parikh, A.1    Guengerich, F.P.2
  • 14
    • 0031572185 scopus 로고    scopus 로고
    • A general strategy for the expression of recombinant human cytochrome P450s in Escherichia coli using bacterial signal peptides: Expression of CYP3A4, CYP2A6, and CYP2E1
    • Pritchard, M. P., Ossentian, R., Li, D. N., Henderson, C. J., Burchell, B., Wolf, R., and Friedberg, T., A general strategy for the expression of recombinant human cytochrome P450s in Escherichia coli using bacterial signal peptides: Expression of CYP3A4, CYP2A6, and CYP2E1. Arch. Biochem. Biophys., 345, 342-354 (1997).
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 342-354
    • Pritchard, M.P.1    Ossentian, R.2    Li, D.N.3    Henderson, C.J.4    Burchell, B.5    Wolf, R.6    Friedberg, T.7
  • 15
    • 0027420580 scopus 로고
    • Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity
    • Sandhu, P., Baba, T., and Guengerich, F. P., Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity. Arch. Biochem. Biophys., 306, 443-450 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 443-450
    • Sandhu, P.1    Baba, T.2    Guengerich, F.P.3
  • 16
    • 0019162146 scopus 로고
    • Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing
    • Sanger, F., Coulson, A. R., Barrell, B. G., Smith, A. J., and Roe, B. A., Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing. J. Mol. Biol., 143, 161-178 (1980).
    • (1980) J. Mol. Biol. , vol.143 , pp. 161-178
    • Sanger, F.1    Coulson, A.R.2    Barrell, B.G.3    Smith, A.J.4    Roe, B.A.5
  • 17
    • 0034976635 scopus 로고    scopus 로고
    • Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions
    • Tang, W. and Stearns, R. A., Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions. Curr. Drug Metab., 2, 185-198 (2001)
    • (2001) Curr. Drug Metab. , vol.2 , pp. 185-198
    • Tang, W.1    Stearns, R.A.2
  • 18
    • 0026750647 scopus 로고
    • The human hepatic cytochromes P450 involved in drug metabolism
    • Wrighton, S. A. and Stevens, J. C., The human hepatic cytochromes P450 involved in drug metabolism. Crit. Rev. Toxcol., 22, 1-21 (1992).
    • (1992) Crit. Rev. Toxcol. , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.