메뉴 건너뛰기




Volumn 461, Issue 1, 2007, Pages 76-84

Hepatic cytochrome P450 reductase-null mice reveal a second microsomal reductase for squalene monooxygenase

Author keywords

Cholesterol synthesis; HMG CoA reductase; Lanosterol; Supernatant protein factor

Indexed keywords

ANTIBODY; CYTOCHROME P450 REDUCTASE; DIHYDROLANOSTEROL; SQUALENE MONOOXYGENASE; STEROL 14ALPHA DEMETHYLASE;

EID: 34247270767     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2007.02.010     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 0028839090 scopus 로고
    • Molecular cloning and expression of rat squalene epoxidase
    • Sakakibara J., Watanabe R., Kanai Y., and Ono T. Molecular cloning and expression of rat squalene epoxidase. J. Biol. Chem. 270 (1995) 17-20
    • (1995) J. Biol. Chem. , vol.270 , pp. 17-20
    • Sakakibara, J.1    Watanabe, R.2    Kanai, Y.3    Ono, T.4
  • 2
    • 0014939325 scopus 로고
    • Studies on squalene epoxidase of rat liver
    • Yamamoto S., and Bloch K. Studies on squalene epoxidase of rat liver. J. Biol. Chem. 245 (1970) 1670-1674
    • (1970) J. Biol. Chem. , vol.245 , pp. 1670-1674
    • Yamamoto, S.1    Bloch, K.2
  • 4
    • 0015523227 scopus 로고
    • Squalene epoxidase of rat liver
    • Tai H.H., and Bloch K. Squalene epoxidase of rat liver. J. Biol. Chem. 247 (1972) 3767-3773
    • (1972) J. Biol. Chem. , vol.247 , pp. 3767-3773
    • Tai, H.H.1    Bloch, K.2
  • 5
    • 0016641043 scopus 로고
    • Solubilization and partial characterization of rat liver squalene epoxidase
    • Ono T., and Bloch K. Solubilization and partial characterization of rat liver squalene epoxidase. J. Biol. Chem. 250 (1975) 1571-1579
    • (1975) J. Biol. Chem. , vol.250 , pp. 1571-1579
    • Ono, T.1    Bloch, K.2
  • 6
    • 0036502854 scopus 로고    scopus 로고
    • Cholesterol biosynthesis: Lanosterol to cholesterol
    • Risley J.M. Cholesterol biosynthesis: Lanosterol to cholesterol. J. Chem. Educ. 79 (2002) 377-384
    • (2002) J. Chem. Educ. , vol.79 , pp. 377-384
    • Risley, J.M.1
  • 7
    • 0034652106 scopus 로고    scopus 로고
    • Evidence for requirement of NADPH-cytochrome P450 oxidoreductase in the microsomal NADPH-sterol Delta7-reductase system
    • Nishino H., and Ishibashi T. Evidence for requirement of NADPH-cytochrome P450 oxidoreductase in the microsomal NADPH-sterol Delta7-reductase system. Arch. Biochem. Biophys. 374 (2000) 293-298
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 293-298
    • Nishino, H.1    Ishibashi, T.2
  • 8
    • 0032750635 scopus 로고    scopus 로고
    • Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction
    • Lamb D.C., Kelly D.E., Manning N.J., Kaderbhai M.A., and Kelly S.L. Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction. FEBS Lett. 462 (1999) 283-288
    • (1999) FEBS Lett. , vol.462 , pp. 283-288
    • Lamb, D.C.1    Kelly, D.E.2    Manning, N.J.3    Kaderbhai, M.A.4    Kelly, S.L.5
  • 9
    • 0037155271 scopus 로고    scopus 로고
    • Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase
    • Shen A.L., O'Leary K.A., and Kasper C.B. Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase. J. Biol. Chem. 277 (2002) 6536-6541
    • (2002) J. Biol. Chem. , vol.277 , pp. 6536-6541
    • Shen, A.L.1    O'Leary, K.A.2    Kasper, C.B.3
  • 10
    • 0041468898 scopus 로고    scopus 로고
    • Identification of novel roles of the cytochrome p450 system in early embryogenesis: effects on vasculogenesis and retinoic acid homeostasis
    • Otto D.M., Henderson C.J., Carrie D., Davey M., Gundersen T.E., Blomhoff R., Adams R.H., Tickle C., and Wolf C.R. Identification of novel roles of the cytochrome p450 system in early embryogenesis: effects on vasculogenesis and retinoic acid homeostasis. Mol. Cell Biol. 23 (2003) 6103-6116
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6103-6116
    • Otto, D.M.1    Henderson, C.J.2    Carrie, D.3    Davey, M.4    Gundersen, T.E.5    Blomhoff, R.6    Adams, R.H.7    Tickle, C.8    Wolf, C.R.9
  • 11
    • 0038507099 scopus 로고    scopus 로고
    • Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase
    • Gu J., Weng Y., Zhang Q.Y., Cui H., Behr M., Wu L., Yang W., Zhang L., and Ding X. Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase. J. Biol. Chem. 278 (2003) 25895-25901
    • (2003) J. Biol. Chem. , vol.278 , pp. 25895-25901
    • Gu, J.1    Weng, Y.2    Zhang, Q.Y.3    Cui, H.4    Behr, M.5    Wu, L.6    Yang, W.7    Zhang, L.8    Ding, X.9
  • 12
    • 0037790603 scopus 로고    scopus 로고
    • Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase
    • Henderson C.J., Otto D.M., Carrie D., Magnuson M.A., McLaren A.W., Rosewell I., and Wolf C.R. Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase. J. Biol. Chem. 278 (2003) 13480-13486
    • (2003) J. Biol. Chem. , vol.278 , pp. 13480-13486
    • Henderson, C.J.1    Otto, D.M.2    Carrie, D.3    Magnuson, M.A.4    McLaren, A.W.5    Rosewell, I.6    Wolf, C.R.7
  • 15
    • 0037458661 scopus 로고    scopus 로고
    • Phosphorylation of supernatant protein factor enhances its ability to stimulate microsomal squalene monooxygenase
    • Singh D.K., Mokashi V., Elmore C.L., and Porter T.D. Phosphorylation of supernatant protein factor enhances its ability to stimulate microsomal squalene monooxygenase. J. Biol. Chem. 278 (2003) 5646-5651
    • (2003) J. Biol. Chem. , vol.278 , pp. 5646-5651
    • Singh, D.K.1    Mokashi, V.2    Elmore, C.L.3    Porter, T.D.4
  • 16
    • 0024322441 scopus 로고
    • Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole
    • Sutter T.R., and Loper J.C. Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole. Biochem. Biophys. Res. Commun. 160 (1989) 1257-1266
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 1257-1266
    • Sutter, T.R.1    Loper, J.C.2
  • 17
    • 0017684545 scopus 로고
    • Purification and properties of a soluble protein activator of rat liver squalene epoxidase
    • Ferguson J.B., and Bloch K. Purification and properties of a soluble protein activator of rat liver squalene epoxidase. J. Biol. Chem. 252 (1977) 5381-5385
    • (1977) J. Biol. Chem. , vol.252 , pp. 5381-5385
    • Ferguson, J.B.1    Bloch, K.2
  • 18
    • 9944258589 scopus 로고    scopus 로고
    • Supernatant protein factor stimulates HMG-CoA reductase in cell culture and in vitro
    • Mokashi V., Singh D.K., and Porter T.D. Supernatant protein factor stimulates HMG-CoA reductase in cell culture and in vitro. Arch. Biochem. Biophys. 433 (2005) 474-480
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 474-480
    • Mokashi, V.1    Singh, D.K.2    Porter, T.D.3
  • 20
    • 0030858044 scopus 로고    scopus 로고
    • Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol delta 24-reductase
    • Bae S.H., and Paik Y.K. Cholesterol biosynthesis from lanosterol: development of a novel assay method and characterization of rat liver microsomal lanosterol delta 24-reductase. Biochem. J. 326 Pt 2 (1997) 609-616
    • (1997) Biochem. J. , vol.326 , Issue.PART 2 , pp. 609-616
    • Bae, S.H.1    Paik, Y.K.2
  • 21
    • 0032940786 scopus 로고    scopus 로고
    • Lanosterol analogs: dual-action inhibitors of cholesterol biosynthesis
    • Frye L.L., and Leonard D.A. Lanosterol analogs: dual-action inhibitors of cholesterol biosynthesis. Crit. Rev. Biochem. Mol. Biol. 34 (1999) 123-140
    • (1999) Crit. Rev. Biochem. Mol. Biol. , vol.34 , pp. 123-140
    • Frye, L.L.1    Leonard, D.A.2
  • 22
    • 21744456583 scopus 로고    scopus 로고
    • Relationship between hepatic phenotype and changes in gene expression in cytochrome P450 reductase (POR) null mice
    • Wang X.J., Chamberlain M., Vassieva O., Henderson C.J., and Wolf C.R. Relationship between hepatic phenotype and changes in gene expression in cytochrome P450 reductase (POR) null mice. Biochem. J. 388 (2005) 857-867
    • (2005) Biochem. J. , vol.388 , pp. 857-867
    • Wang, X.J.1    Chamberlain, M.2    Vassieva, O.3    Henderson, C.J.4    Wolf, C.R.5
  • 23
    • 24744466284 scopus 로고    scopus 로고
    • Hepatic gene expression changes in mouse models with liver-specific deletion or global suppression of the NADPH-cytochrome P450 reductase gene. Mechanistic implications for the regulation of microsomal cytochrome P450 and the fatty liver phenotype
    • Weng Y., DiRusso C.C., Reilly A.A., Black P.N., and Ding X. Hepatic gene expression changes in mouse models with liver-specific deletion or global suppression of the NADPH-cytochrome P450 reductase gene. Mechanistic implications for the regulation of microsomal cytochrome P450 and the fatty liver phenotype. J. Biol. Chem. 280 (2005) 31686-31698
    • (2005) J. Biol. Chem. , vol.280 , pp. 31686-31698
    • Weng, Y.1    DiRusso, C.C.2    Reilly, A.A.3    Black, P.N.4    Ding, X.5
  • 24
    • 0017339034 scopus 로고
    • Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system
    • Ono T., Ozasa S., Hasegawa F., and Imai Y. Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system. Biochim. Biophys. Acta 486 (1977) 401-407
    • (1977) Biochim. Biophys. Acta , vol.486 , pp. 401-407
    • Ono, T.1    Ozasa, S.2    Hasegawa, F.3    Imai, Y.4
  • 25
    • 0019321487 scopus 로고
    • Supernatant protein factor facilitates intermembrane transfer of squalene
    • Friedlander E.J., Caras I.W., Lin L.F., and Bloch K. Supernatant protein factor facilitates intermembrane transfer of squalene. J. Biol. Chem. 255 (1980) 8042-8045
    • (1980) J. Biol. Chem. , vol.255 , pp. 8042-8045
    • Friedlander, E.J.1    Caras, I.W.2    Lin, L.F.3    Bloch, K.4
  • 26
    • 0037253579 scopus 로고    scopus 로고
    • Supernatant protein factor and tocopherol-associated protein: An unexpected link between cholesterol synthesis and vitamin E
    • Porter T.D. Supernatant protein factor and tocopherol-associated protein: An unexpected link between cholesterol synthesis and vitamin E. J. Nutr. Biochem. 14 (2003) 3-6
    • (2003) J. Nutr. Biochem. , vol.14 , pp. 3-6
    • Porter, T.D.1
  • 31
    • 12844267002 scopus 로고    scopus 로고
    • Supernatant protein factor requires phosphorylation and interaction with Golgi to stimulate cholesterol synthesis in hepatoma cells
    • Mokashi V., and Porter T.D. Supernatant protein factor requires phosphorylation and interaction with Golgi to stimulate cholesterol synthesis in hepatoma cells. Arch. Biochem. Biophys. 435 (2005) 175-181
    • (2005) Arch. Biochem. Biophys. , vol.435 , pp. 175-181
    • Mokashi, V.1    Porter, T.D.2
  • 32
    • 18544378347 scopus 로고    scopus 로고
    • Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol
    • Song B.L., Javitt N.B., and DeBose-Boyd R.A. Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol. Cell Metab. 1 (2005) 179-189
    • (2005) Cell Metab. , vol.1 , pp. 179-189
    • Song, B.L.1    Javitt, N.B.2    DeBose-Boyd, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.