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Volumn 21, Issue 2, 2010, Pages 203-207

Delivery of NADPH-cytochrome P450 reductase antisense oligos using avidin-biotin approach

Author keywords

[No Author keywords available]

Indexed keywords

COENZYMES; ELECTROPHORESIS; ENZYME ACTIVITY; GENES; OLIGONUCLEOTIDES;

EID: 77049123764     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc900449b     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0004563140 scopus 로고
    • Triphosphopyridine nucleotide-cytochrome c reductase in liver
    • Horecker, B. L. (1950) Triphosphopyridine nucleotide-cytochrome c reductase in liver. J. Biol. Chem. 183, 593-605.
    • (1950) J. Biol. Chem. , vol.183 , pp. 593-605
    • Horecker, B.L.1
  • 2
    • 0021454859 scopus 로고
    • The role of iron chelates in hydroxyl radical production by rat liver microsomes, NADPH-cytochrome P-450 reductase and xanthine oxidase
    • Winston, G. W., Feierman, D. E., and Cederbaum, A. I. (1984) The role of iron chelates in hydroxyl radical production by rat liver microsomes, NADPH-cytochrome P-450 reductase and xanthine oxidase. Arch. Biochem. Biophys. 232, 378-390
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 378-390
    • Winston, G.W.1    Feierman, D.E.2    Cederbaum, A.I.3
  • 3
    • 0021456537 scopus 로고
    • Superoxide generation by NADPH-cytochrome P-450 reductase: The effect of iron chelators and the role of superoxide in microsomal lipid peroxidation
    • Morehouse, L. A., Thomas, C. E., and Aust, S. D. (1984) Superoxide generation by NADPH-cytochrome P-450 reductase: the effect of iron chelators and the role of superoxide in microsomal lipid peroxidation. Arch. Biochem. Biophys. 232, 366-377
    • (1984) Arch. Biochem. Biophys. , vol.232 , pp. 366-377
    • Morehouse, L.A.1    Thomas, C.E.2    Aust, S.D.3
  • 4
    • 0019890891 scopus 로고
    • Spin trap evidence for production of superoxide radical anions by purified NADPHcytochrome P-450 reductase
    • Bosterling, B., and Trudell, J. R. (1981) Spin trap evidence for production of superoxide radical anions by purified NADPHcytochrome P-450 reductase. Biochem. Biophys. Res. Commun. 98, 569-575
    • (1981) Biochem. Biophys. Res. Commun. , vol.98 , pp. 569-575
    • Bosterling, B.1    Trudell, J.R.2
  • 5
    • 0018741206 scopus 로고
    • NADPH cytochrome P-450 reductase activation of quinine anticancer agents to free radicals
    • Bachur, N. R., Gordon, S. L., Gee, M. V., and Kon, H. (1979) NADPH cytochrome P-450 reductase activation of quinine anticancer agents to free radicals. Proc. Natl. Acad. Sci. U.S.A. 76, 954-957
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 954-957
    • Bachur, N.R.1    Gordon, S.L.2    Gee, M.V.3    Kon, H.4
  • 6
    • 4444268690 scopus 로고    scopus 로고
    • Mechanisms that regulate production of reactive oxygen species by cytochrome P450
    • Zangar, R. C., Davydov, D. R., and Verma, S. (2004) Mechanisms that regulate production of reactive oxygen species by cytochrome P450. Toxicol. Appl. Pharmacol. 199, 316-331
    • (2004) Toxicol. Appl. Pharmacol. , vol.199 , pp. 316-331
    • Zangar, R.C.1    Davydov, D.R.2    Verma, S.3
  • 7
    • 0035281995 scopus 로고    scopus 로고
    • Microsomal monooxygenase in apoptosis: Another target for cytochrome c signaling?
    • Davydov, D. R. (2001) Microsomal monooxygenase in apoptosis: another target for cytochrome c signaling? Trends Biochem. Sci. 26, 155-160
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 155-160
    • Davydov, D.R.1
  • 8
    • 33644638130 scopus 로고    scopus 로고
    • Human cytochrome P450 reductase can act as a source of endogenous oxidative DNA damage and genetic instability
    • Heine, T., Glatt, H., and Epe, B. (2006) Human cytochrome P450 reductase can act as a source of endogenous oxidative DNA damage and genetic instability. Free Radic. Biol. Med. 40, 801-807
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 801-807
    • Heine, T.1    Glatt, H.2    Epe, B.3
  • 9
    • 0026726737 scopus 로고
    • Thyroid hormone stimulation of NADPH P450 reductase expression in liver and extrahepatic tissues. Regulation by multiple mechanisms
    • Ram, P. A., and Waxman, D. J. (1992) Thyroid hormone stimulation of NADPH P450 reductase expression in liver and extrahepatic tissues. Regulation by multiple mechanisms. J. Biol. Chem. 267, 3294-3301
    • (1992) J. Biol. Chem. , vol.267 , pp. 3294-3301
    • Ram, P.A.1    Waxman, D.J.2
  • 10
    • 0036233011 scopus 로고    scopus 로고
    • Post-transcriptional regulation of hepatic NADPH-cytochrome P450 reductase by thyroid hormone: Independent effects on poly(A) tail length and mRNA stability
    • Liu, D., and Waxman, D. J. (2002) Post-transcriptional regulation of hepatic NADPH-cytochrome P450 reductase by thyroid hormone: independent effects on poly(A) tail length and mRNA stability. Mol. Pharmacol. 61, 1089-1096
    • (2002) Mol. Pharmacol. , vol.61 , pp. 1089-1096
    • Liu, D.1    Waxman, D.J.2
  • 11
    • 0028934858 scopus 로고
    • Effect of propylthiouracil treatment on NADPHcytochrome P450 reductase levels, oxygen consumption and hydroxyl radical formation in liver microsomes from rats fed ethanol or acetone chronically
    • Ross, A. D., Varghese, G., Oporto, B., Carmichael, F. J., and Israel, Y. (1995) Effect of propylthiouracil treatment on NADPHcytochrome P450 reductase levels, oxygen consumption and hydroxyl radical formation in liver microsomes from rats fed ethanol or acetone chronically. Biochem. Pharmacol. 49, 979-989
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 979-989
    • Ross, A.D.1    Varghese, G.2    Oporto, B.3    Carmichael, F.J.4    Israel, Y.5
  • 12
    • 0347318117 scopus 로고    scopus 로고
    • Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes
    • Herrera, B., Murillo, M. M., Alvarez-Barrientos, A., Beltran, J., Fernandez, M., and Fabregat, I. (2004) Source of early reactive oxygen species in the apoptosis induced by transforming growth factor-beta in fetal rat hepatocytes. Free Radic. Biol. Med. 36, 16-26.
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 16-26
    • Herrera, B.1    Murillo, M.M.2    Alvarez-Barrientos, A.3    Beltran, J.4    Fernandez, M.5    Fabregat, I.6
  • 13
    • 58149472378 scopus 로고    scopus 로고
    • Role of NADPH cytochrome P450 reductase and cytochrome b5/NADH b5 reductase in variability of CYP3A activity in human liver microsomes
    • Gan, L., Vonmoltke, L. L., Trepanier, L. A., Harmatz, J. S.,Greenblatt, D. J., and Court, M. H. (2009) Role of NADPH cytochrome P450 reductase and cytochrome b5/NADH b5 reductase in variability of CYP3A activity in human liver microsomes. Drug Metab. Dispos. 37, 90-96.
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 90-96
    • Gan, L.1    Vonmoltke, L.L.2    Trepanier, L.A.3    Harmatz, S.4    Greenblatt, J.D.J.5    Court, M.H.6
  • 14
    • 68549104191 scopus 로고    scopus 로고
    • Nanotechnologies and controlled release systems for the delivery of antisense oligonucleotides and small interfering RNA
    • Fattal, E., and Barratt, G. (2009) Nanotechnologies and controlled release systems for the delivery of antisense oligonucleotides and small interfering RNA. Br. J. Pharmacol. .
    • (2009) Br. J. Pharmacol.
    • Fattal, E.1    Barratt, G.2
  • 15
    • 0030862707 scopus 로고    scopus 로고
    • Morpholino antisense oligomers: Design, preparation, and properties
    • Summerton, J., and Weller, D. (1997) Morpholino antisense oligomers: design, preparation, and properties. Antisense Nucleic Acid Drug Dev. 7, 187-195
    • (1997) Antisense Nucleic Acid Drug Dev. , vol.7 , pp. 187-195
    • Summerton, J.1    Weller, D.2
  • 16
    • 34247566116 scopus 로고    scopus 로고
    • Morpholino, siRNA, and S-DNA compared: Impact of structure and mechanism of action on offtarget effects and sequence specificity
    • Summerton, J. E. (2007) Morpholino, siRNA, and S-DNA compared: impact of structure and mechanism of action on offtarget effects and sequence specificity. Curr. Top. Med. Chem. 7, 651-660
    • (2007) Curr. Top. Med. Chem. , vol.7 , pp. 651-660
    • Summerton, J.E.1
  • 17
    • 55649089421 scopus 로고    scopus 로고
    • State of the art and perspectives for the delivery of antisense oligonucleotides and siRNA by polymeric nanocarriers
    • Fattal, E., and Bochot, A. (2008) State of the art and perspectives for the delivery of antisense oligonucleotides and siRNA by polymeric nanocarriers. Int. J. Pharm. 364, 237-248
    • (2008) Int. J. Pharm. , vol.364 , pp. 237-248
    • Fattal, E.1    Bochot, A.2
  • 19
    • 0030032042 scopus 로고    scopus 로고
    • Antisense oligonucleotide therapeutics: Drug delivery and targeting
    • Rojanasakul, Y. Y. (1996) Antisense oligonucleotide therapeutics: Drug delivery and targeting. Adv. Drug Delivery Rev. 18, 115-131.
    • (1996) Adv. Drug Delivery Rev. , vol.18 , pp. 115-131
    • Rojanasakul, Y.Y.1
  • 20
    • 65349091267 scopus 로고    scopus 로고
    • Overcoming biological barriers to in vivo efficacy of antisense oligonucleotides
    • White, P. J., Anastasopoulos, F., Pouton, C. W., and Boyd, B. J. (2009) Overcoming biological barriers to in vivo efficacy of antisense oligonucleotides. Expert Rev. Mol. Med. 11, e10.
    • (2009) Expert Rev. Mol. Med. , vol.11
    • White, P.J.1    Anastasopoulos, F.2    Pouton, C.W.3    Boyd, B.J.4
  • 21
    • 0025814795 scopus 로고
    • Enhanced cellular uptake of biotinylated antisense oligonucleotide or peptide mediated by avidin, a cationic protein
    • Pardridge, W. M., and Boado, R. J. (1991) Enhanced cellular uptake of biotinylated antisense oligonucleotide or peptide mediated by avidin, a cationic protein. FEBS Lett. 288, 30-32
    • (1991) FEBS Lett. , vol.288 , pp. 30-32
    • Pardridge, W.M.1    Boado, R.J.2
  • 22
    • 0028500927 scopus 로고
    • Complete inactivation of target mRNA by biotinylated antisense oligodeoxynucleotide-avidin conjugates
    • Boado, R. J., and Pardridge, W. M. (1994) Complete inactivation of target mRNA by biotinylated antisense oligodeoxynucleotide- avidin conjugates. Bioconjugate Chem. 5, 406-410
    • (1994) Bioconjugate Chem. , vol.5 , pp. 406-410
    • Boado, R.J.1    Pardridge, W.M.2
  • 23
    • 0009563977 scopus 로고
    • Drug delivery of antisense oligonucleotides or peptides to tissues in vivo using an avidin-biotin system
    • Pardridge, W. M., Boado, R. J., and J. L., B. (1993) Drug delivery of antisense oligonucleotides or peptides to tissues in vivo using an avidin-biotin system. Drug Delivery 1, 43-50.
    • (1993) Drug Delivery , vol.1 , pp. 43-50
    • Pardridge, W.M.1    Boado, R.J.2    B, J.L.3
  • 25
    • 0025288944 scopus 로고
    • Avidin and streptavidin
    • Green, N. M. (1990) Avidin and streptavidin. Methods Enzymol. 184, 51-67.
    • (1990) Methods Enzymol. , vol.184 , pp. 51-67
    • Green, N.M.1
  • 26
    • 0021149409 scopus 로고
    • A diploid epithelial cell line from normal adult rat liver with phenotypic properties of 'oval' cells
    • Tsao, M. S., Smith, J. D., Nelson, K. G., and Grisham, J. W. (1984) A diploid epithelial cell line from normal adult rat liver with phenotypic properties of 'oval' cells. Exp. Cell. Res. 154, 38-52.
    • (1984) Exp. Cell. Res. , vol.154 , pp. 38-52
    • Tsao, M.S.1    Smith, J.D.2    Nelson, K.G.3    Grisham, J.W.4
  • 28
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterisation, and kinetic studies
    • Phillips, A. H., and Langdon, R. G. (1962) Hepatic triphosphopyridine nucleotide-cytochrome c reductase: isolation, characterisation, and kinetic studies. J. Biol. Chem. 237, 2652-2660.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 29
    • 0021703594 scopus 로고
    • Turnover of membrane proteins: Kinetics of induction and degradation of seven forms of rat liver microsomal cytochrome P-450, NADPHcytochrome P-450 reductase, and epoxide hydrolase
    • Shiraki, H., and Guengerich, F. P. (1984) Turnover of membrane proteins: kinetics of induction and degradation of seven forms of rat liver microsomal cytochrome P-450, NADPHcytochrome P-450 reductase, and epoxide hydrolase. Arch. Biochem. Biophys. 235, 86-96.
    • (1984) Arch. Biochem. Biophys. , vol.235 , pp. 86-96
    • Shiraki, H.1    Guengerich, F.P.2
  • 30
    • 33645818541 scopus 로고    scopus 로고
    • Effect of genetic variation on human cytochrome p450 reductase-mediated paraquat cytotoxicity
    • Han, J. F., Wang, S. L., He, X. Y., Liu, C. Y., and Hong, J. Y. (2006) Effect of genetic variation on human cytochrome p450 reductase-mediated paraquat cytotoxicity. Toxicol. Sci. 91, 42-48
    • (2006) Toxicol. Sci. , vol.91 , pp. 42-48
    • Han, J.F.1    Wang, S.L.2    He, X.Y.3    Liu, C.Y.4    Hong, J.Y.5


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