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Volumn 78, Issue 2, 2010, Pages 182-190

Cytochrome-P450 2B1 gene silencing attenuates puromycin aminonucleoside-induced cytotoxicity in glomerular epithelial cells

Author keywords

cytochrome P450; cytotoxicity; gene expression oxidative stress

Indexed keywords

CASPASE 3; CYTOCHROME P450 2B1; ENZYME PRECURSOR; EPITHELIAL CELL ADHESION MOLECULE; HEME OXYGENASE 1; MESSENGER RNA; PROCASPASE 12; PUROMYCIN AMINONUCLEOSIDE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 77954242629     PISSN: 00852538     EISSN: 15231755     Source Type: Journal    
DOI: 10.1038/ki.2010.100     Document Type: Article
Times cited : (12)

References (64)
  • 1
    • 0030052563 scopus 로고    scopus 로고
    • Role of catalytic iron in an animal model of minimal change nephrotic syndrome
    • Ueda N, Baliga R, Shah SV. Role of catalytic iron in an animal model of minimal change nephrotic syndrome. Kidney Int 1996; 49: 370-373.
    • (1996) Kidney Int , vol.49 , pp. 370-373
    • Ueda, N.1    Baliga, R.2    Shah, S.V.3
  • 3
    • 9044254525 scopus 로고    scopus 로고
    • P450 superfamily: Update on new sequences, gene mapping, accession numbers and nomenclature
    • Nelson DR, Koymans L, Kamataki T et al. P450 superfamily: update on new sequences, gene mapping, accession numbers and nomenclature. Pharmacogenetics 1996; 6: 1-42.
    • (1996) Pharmacogenetics , vol.6 , pp. 1-42
    • Nelson, D.R.1    Koymans, L.2    Kamataki, T.3
  • 4
    • 0017817052 scopus 로고
    • Generation of superoxide anion as a source of hydrogen peroxide in a reconstituted monooxygenase system
    • Kuthan H, Tsuji H, Graf H et al. Generation of superoxide anion as a source of hydrogen peroxide in a reconstituted monooxygenase system. FEBS Lett 1978; 91: 343-345.
    • (1978) FEBS Lett , vol.91 , pp. 343-345
    • Kuthan, H.1    Tsuji, H.2    Graf, H.3
  • 5
    • 0024546914 scopus 로고
    • Rat liver microsomal NADPHsupported oxidase activity and lipid peroxidation dependent on ethanolinducible cytochrome P-450 (P-450IIE1)
    • Ekstrom G, Ingelman-Sundberg M. Rat liver microsomal NADPHsupported oxidase activity and lipid peroxidation dependent on ethanolinducible cytochrome P-450 (P-450IIE1). Biochem Pharmacol 1989; 38: 1313-1319.
    • (1989) Biochem Pharmacol , vol.38 , pp. 1313-1319
    • Ekstrom, G.1    Ingelman-Sundberg, M.2
  • 6
    • 0017409578 scopus 로고
    • Hydrogen peroxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome P-450
    • Nordblom GD, Coon MJ. Hydrogen peroxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome P-450. Arch Biochem Biophys 1977; 180: 343-347.
    • (1977) Arch Biochem Biophys , vol.180 , pp. 343-347
    • Nordblom, G.D.1    Coon, M.J.2
  • 7
    • 0025825789 scopus 로고
    • Functional effects of cytochrome P450 arachidonate metabolites in the kidney
    • Hirt DL, Jacobson HR. Functional effects of cytochrome P450 arachidonate metabolites in the kidney. Semin Nephrol 1991; 11: 148-155.
    • (1991) Semin Nephrol , vol.11 , pp. 148-155
    • Hirt, D.L.1    Jacobson, H.R.2
  • 8
    • 0030979319 scopus 로고    scopus 로고
    • Cytochrome P450-derived renal HETEs: Storage and release
    • Carroll MA, Balazy M, Huang DD et al. Cytochrome P450-derived renal HETEs: storage and release. Kidney Int 1997; 51: 1696-1702.
    • (1997) Kidney Int , vol.51 , pp. 1696-1702
    • Ma, C.1    Balazy, M.2    Huang, D.D.3
  • 9
    • 0031758531 scopus 로고    scopus 로고
    • Role of cytochrome P-450 as a source of catalytic iron in cisplatin-induced nephrotoxicity
    • Baliga R, Zhang Z, Baliga M et al. Role of cytochrome P-450 as a source of catalytic iron in cisplatin-induced nephrotoxicity. Kidney Int 1998; 54: 1562-1569.
    • (1998) Kidney Int , vol.54 , pp. 1562-1569
    • Baliga, R.1    Zhang, Z.2    Baliga, M.3
  • 10
    • 53049099406 scopus 로고    scopus 로고
    • Ex vivo carbon monoxide prevents cytochrome P450 degradation and ischemia/reperfusion injury of kidney grafts
    • Nakao A, Faleo G, Shimizu H et al. Ex vivo carbon monoxide prevents cytochrome P450 degradation and ischemia/reperfusion injury of kidney grafts. Kidney Int 2008; 74: 1009-1016.
    • (2008) Kidney Int , vol.74 , pp. 1009-1016
    • Nakao, A.1    Faleo, G.2    Shimizu, H.3
  • 11
    • 0034799622 scopus 로고    scopus 로고
    • Effect of cytochrome P450 1A induction on oxidative damage in rat brain
    • Liu L, Bridges RJ, Eyer CL. Effect of cytochrome P450 1A induction on oxidative damage in rat brain. Mol Cell Biochem 2001; 223: 89-94.
    • (2001) Mol Cell Biochem , vol.223 , pp. 89-94
    • Liu, L.1    Bridges, R.J.2    Eyer, C.L.3
  • 12
    • 0346366740 scopus 로고    scopus 로고
    • The CYP inhibitor 1-aminobenzotriazole does not prevent oxidative stress associated with alcohol-induced liver injury in rats and mice
    • Isayama F, Froh M, Bradford BU et al. The CYP inhibitor 1-aminobenzotriazole does not prevent oxidative stress associated with alcohol-induced liver injury in rats and mice. Free Radic Biol Med 2003; 35: 1568-1581.
    • (2003) Free Radic Biol Med , vol.35 , pp. 1568-1581
    • Isayama, F.1    Froh, M.2    Bradford, B.U.3
  • 14
    • 0037871865 scopus 로고    scopus 로고
    • Role of cytochrome P450 2B1 in puromycin aminonucleoside-induced cytotoxicity to glomerular epithelial cells
    • Liu H, Baliga M, Bigler SA et al. Role of cytochrome P450 2B1 in puromycin aminonucleoside-induced cytotoxicity to glomerular epithelial cells. Nephron Exp Nephrol 2003; 94: e17-e24.
    • (2003) Nephron Exp Nephrol , vol.94
    • Liu, H.1    Baliga, M.2    Bigler, S.A.3
  • 15
    • 0036419909 scopus 로고    scopus 로고
    • Cytochrome P450 2B1 mediates oxidant injury in puromycin-induced nephrotic syndrome
    • Liu H, Bigler SA, Henegar JR et al. Cytochrome P450 2B1 mediates oxidant injury in puromycin-induced nephrotic syndrome. Kidney Int 2002; 62: 868-876.
    • (2002) Kidney Int , vol.62 , pp. 868-876
    • Liu, H.1    Bigler, S.A.2    Henegar, J.R.3
  • 16
    • 33745058119 scopus 로고    scopus 로고
    • The podocytes response to injury: Role in proteinuria and glomerulosclerosis
    • Shankland SJ. The podocytes response to injury: role in proteinuria and glomerulosclerosis. Kidney Int 2006; 69: 2131-2147.
    • (2006) Kidney Int , vol.69 , pp. 2131-2147
    • Shankland, S.J.1
  • 17
    • 0036891810 scopus 로고    scopus 로고
    • Podocyte biology and response to injury
    • Mundel P, Shankland SJ. Podocyte biology and response to injury. J Am Soc Nephrol 2002; 13: 3005-3015.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 3005-3015
    • Mundel, P.1    Shankland, S.J.2
  • 18
    • 0017286132 scopus 로고
    • Alterations of the glomerular epithelium in acute aminonucleoside nephrosis. Evidence for formation of occluding junctions and epithelial cell detachment
    • Caulfield JP, Reid JJ, Farquhar MG. Alterations of the glomerular epithelium in acute aminonucleoside nephrosis. Evidence for formation of occluding junctions and epithelial cell detachment. Lab Invest 1976; 34: 43-59.
    • (1976) Lab Invest , vol.34 , pp. 43-59
    • Caulfield, J.P.1    Reid, J.J.2    Farquhar, M.G.3
  • 19
    • 0033644002 scopus 로고    scopus 로고
    • Regulation and role of heme oxygenase in oxidative injury
    • Dennery PA. Regulation and role of heme oxygenase in oxidative injury. Curr Top Cell Regul 2000; 36: 181-199.
    • (2000) Curr Top Cell Regul , vol.36 , pp. 181-199
    • Dennery, P.A.1
  • 20
    • 27744500069 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-associated caspase 12 mediates cisplatin-induced LLC-PK1 cell apoptosis
    • Liu H, Baliga R. Endoplasmic reticulum stress-associated caspase 12 mediates cisplatin-induced LLC-PK1 cell apoptosis. J Am Soc Nephrol 2005; 16: 1985-1992.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 1985-1992
    • Liu, H.1    Baliga, R.2
  • 21
    • 0025728788 scopus 로고
    • Contractile proteins in podocytes: Immunocytochemical localization of actin and alpha-actinin in normal and nephrotic rat kidneys
    • Lachapelle M, Bendayan M. Contractile proteins in podocytes: immunocytochemical localization of actin and alpha-actinin in normal and nephrotic rat kidneys. Virchows Arch B Cell Pathol Incl Mol Pathol 1991; 60: 105-111.
    • (1991) Virchows Arch B Cell Pathol Incl Mol Pathol , vol.60 , pp. 105-111
    • Lachapelle, M.1    Bendayan, M.2
  • 22
    • 0034990905 scopus 로고    scopus 로고
    • Repression of phenobarbitaldependent CYP2B1 mRNA induction by reactive oxygen species in primary rat hepatocyte cultures
    • Hirsch-Ernst KI, Schlaefer K, Bauer D et al. Repression of phenobarbitaldependent CYP2B1 mRNA induction by reactive oxygen species in primary rat hepatocyte cultures. Mol Pharmacol 2001; 59: 1402-1409.
    • (2001) Mol Pharmacol , vol.59 , pp. 1402-1409
    • Hirsch-Ernst, K.I.1    Schlaefer, K.2    Bauer, D.3
  • 23
    • 38149062111 scopus 로고    scopus 로고
    • Nitric oxide-dependent proteasomal degradation of cytochrome P450 2B proteins
    • Lee CM, Kim BY, Li L et al. Nitric oxide-dependent proteasomal degradation of cytochrome P450 2B proteins. J Biol Chem 2008; 283: 889-898.
    • (2008) J Biol Chem , vol.283 , pp. 889-898
    • Lee, C.M.1    Kim, B.Y.2    Li, L.3
  • 24
    • 0026512675 scopus 로고
    • Phenobarbital induction of cytochrome P-450 gene expression
    • Pt 3
    • Waxman DJ, Azaroff L. Phenobarbital induction of cytochrome P-450 gene expression. Biochem J 1992; 281(Pt 3): 577-592.
    • (1992) Biochem J , vol.281 , pp. 577-592
    • Waxman, D.J.1    Azaroff, L.2
  • 25
    • 0032032380 scopus 로고    scopus 로고
    • Protein serine/threonine phosphatase inhibitors suppress phenobarbital-induced Cyp2b10 gene transcription in mouse primary hepatocytes
    • Pt 2
    • Honkakoski P, Negishi M. Protein serine/threonine phosphatase inhibitors suppress phenobarbital-induced Cyp2b10 gene transcription in mouse primary hepatocytes. Biochem J 1998; 330(Pt 2): 889-895.
    • (1998) Biochem J , vol.330 , pp. 889-895
    • Honkakoski, P.1    Negishi, M.2
  • 26
    • 47749112410 scopus 로고    scopus 로고
    • Development of oxidative stress by cytochrome P450 induction in rodents is selective for barbiturates and related to loss of pyridine nucleotide-dependent protective systems
    • Dostalek M, Hardy KD, Milne GL et al. Development of oxidative stress by cytochrome P450 induction in rodents is selective for barbiturates and related to loss of pyridine nucleotide-dependent protective systems. J Biol Chem 2008; 283: 17147-17157.
    • (2008) J Biol Chem , vol.283 , pp. 17147-17157
    • Dostalek, M.1    Hardy, K.D.2    Milne, G.L.3
  • 27
    • 0026578971 scopus 로고
    • Roles of active oxygen species in glomerular epithelial cell injury in vitro caused by puromycin aminonucleoside
    • Kawaguchi M, Yamada M, Wada H et al. Roles of active oxygen species in glomerular epithelial cell injury in vitro caused by puromycin aminonucleoside. Toxicology 1992; 72: 329-340.
    • (1992) Toxicology , vol.72 , pp. 329-340
    • Kawaguchi, M.1    Yamada, M.2    Wada, H.3
  • 28
    • 0028145046 scopus 로고
    • Reactive oxygen species in puromycin aminonucleoside nephrosis: In vitro studies
    • Ricardo SD, Bertram JF, Ryan GB. Reactive oxygen species in puromycin aminonucleoside nephrosis: in vitro studies. Kidney Int 1994; 45: 1057-1069.
    • (1994) Kidney Int , vol.45 , pp. 1057-1069
    • Ricardo, S.D.1    Bertram, J.F.2    Ryan, G.B.3
  • 29
    • 0346724935 scopus 로고    scopus 로고
    • Role of phenobarbital-inducible cytochrome P450s as a source of active oxygen species in DNA-oxidation
    • Imaoka S, Osada M, Minamiyama Y et al. Role of phenobarbital-inducible cytochrome P450s as a source of active oxygen species in DNA-oxidation. Cancer Lett 2004; 203: 117-125.
    • (2004) Cancer Lett , vol.203 , pp. 117-125
    • Imaoka, S.1    Osada, M.2    Minamiyama, Y.3
  • 30
    • 0037692895 scopus 로고    scopus 로고
    • The effect of valproic acid on hepatic and plasma levels of 15-F2t-isoprostane in rats
    • Tong V, Chang TK, Chen J et al. The effect of valproic acid on hepatic and plasma levels of 15-F2t-isoprostane in rats. Free Radic Biol Med 2003; 34: 1435-1446.
    • (2003) Free Radic Biol Med , vol.34 , pp. 1435-1446
    • Tong, V.1    Chang, T.K.2    Chen, J.3
  • 31
    • 0030033983 scopus 로고    scopus 로고
    • Evidence for cytochrome P-450 as a source of catalytic iron in myoglobinuric acute renal failure
    • Baliga R, Zhang Z, Baliga M et al. Evidence for cytochrome P-450 as a source of catalytic iron in myoglobinuric acute renal failure. Kidney Int 1996; 49: 362-369.
    • (1996) Kidney Int , vol.49 , pp. 362-369
    • Baliga, R.1    Zhang, Z.2    Baliga, M.3
  • 32
    • 0025015428 scopus 로고
    • Role of cytochrome P-450 in reperfusion injury of the rabbit lung
    • Bysani GK, Kennedy TP, Ky N et al. Role of cytochrome P-450 in reperfusion injury of the rabbit lung. J Clin Invest 1990; 86: 1434-1441.
    • (1990) J Clin Invest , vol.86 , pp. 1434-1441
    • Bysani, G.K.1    Kennedy, T.P.2    Ky, N.3
  • 33
    • 0028321518 scopus 로고
    • Cytochrome P-450 mediates tissue-damaging hydroxyl radical formation during reoxygenation of the kidney
    • Paller MS, Jacob HS. Cytochrome P-450 mediates tissue-damaging hydroxyl radical formation during reoxygenation of the kidney. Proc Natl Acad Sci USA 1994; 91: 7002-7006.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7002-7006
    • Paller, M.S.1    Jacob, H.S.2
  • 34
    • 0035000022 scopus 로고    scopus 로고
    • Cytochrome P-450 as a source of catalytic iron in minimal change nephrotic syndrome in rats
    • Liu H, Shah SV, Baliga R. Cytochrome P-450 as a source of catalytic iron in minimal change nephrotic syndrome in rats. Am J Physiol Renal Physiol 2001; 280: F88-F94.
    • (2001) Am J Physiol Renal Physiol , vol.280
    • Liu, H.1    Shah, S.V.2    Baliga, R.3
  • 35
    • 0028099510 scopus 로고
    • Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions
    • Karuzina II, Archakov AI. Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions. Free Radic Biol Med 1994; 17: 557-567.
    • (1994) Free Radic Biol Med , vol.17 , pp. 557-567
    • Karuzina, I.I.1    Archakov, A.I.2
  • 36
    • 0017087792 scopus 로고
    • Cytochrome P-450 heme and the regulation of hepatic heme oxygenase activity
    • Bissell DM, Hammaker LE. Cytochrome P-450 heme and the regulation of hepatic heme oxygenase activity. Arch Biochem Biophys 1976; 176: 91-102.
    • (1976) Arch Biochem Biophys , vol.176 , pp. 91-102
    • Bissell, D.M.1    Hammaker, L.E.2
  • 37
    • 54149107681 scopus 로고    scopus 로고
    • Caspases as therapeutic targets
    • Howley B, Fearnhead HO. Caspases as therapeutic targets. J Cell Mol Med 2008; 12: 1502-1516.
    • (2008) J Cell Mol Med , vol.12 , pp. 1502-1516
    • Howley, B.1    Fearnhead, H.O.2
  • 39
    • 34250013383 scopus 로고    scopus 로고
    • PPAR-gamma agonist protects podocytes from injury
    • Kanjanabuch T, Ma LJ, Chen J et al. PPAR-gamma agonist protects podocytes from injury. Kidney Int 2007; 71: 1232-1239.
    • (2007) Kidney Int , vol.71 , pp. 1232-1239
    • Kanjanabuch, T.1    Ma, L.J.2    Chen, J.3
  • 40
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, anendoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T, Imaizumi K, Oono K et al. Activation of caspase-12, anendoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 2001; 276: 13935-13940.
    • (2001) J Biol Chem , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3
  • 41
    • 18344388462 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program: Role of the ER chaperone GRP78
    • Rao RV, Peel A, Logvinova A et al. Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78. FEBS Lett 2002; 514: 122-128.
    • (2002) FEBS Lett , vol.514 , pp. 122-128
    • Rao, R.V.1    Peel, A.2    Logvinova, A.3
  • 42
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12
    • Morishima N, Nakanishi K, Takenouchi H et al. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem 2002; 277: 34287-34294.
    • (2002) J Biol Chem , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3
  • 43
    • 34547815735 scopus 로고    scopus 로고
    • Podocyte protection by darbepoetin: Preservation of the cytoskeleton and nephrin expression
    • Eto N, Wada T, Inagi R et al. Podocyte protection by darbepoetin: preservation of the cytoskeleton and nephrin expression. Kidney Int 2007; 72: 455-463.
    • (2007) Kidney Int , vol.72 , pp. 455-463
    • Eto, N.1    Wada, T.2    Inagi, R.3
  • 44
    • 32844469380 scopus 로고    scopus 로고
    • Glucocorticoids protect and enhance recovery of cultured murine podocytes via actin filament stabilization
    • Ransom RF, Lam NG, Hallett MA et al. Glucocorticoids protect and enhance recovery of cultured murine podocytes via actin filament stabilization. Kidney Int 2005; 68: 2473-2483.
    • (2005) Kidney Int , vol.68 , pp. 2473-2483
    • Ransom, R.F.1    Lam, N.G.2    Ma, H.3
  • 45
    • 30344475768 scopus 로고    scopus 로고
    • Role of p38 mitogen-activated protein kinase activation in podocyte injury and proteinuria in experimental nephrotic syndrome
    • Koshikawa M, Mukoyama M, Mori K et al. Role of p38 mitogen-activated protein kinase activation in podocyte injury and proteinuria in experimental nephrotic syndrome. J Am Soc Nephrol 2005; 16: 2690-2701.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 2690-2701
    • Koshikawa, M.1    Mukoyama, M.2    Mori, K.3
  • 46
    • 33645455275 scopus 로고    scopus 로고
    • Fluvastatin ameliorates podocyte injury in proteinuric rats via modulation of excessive Rho signaling
    • Shibata S, Nagase M, Fujita T. Fluvastatin ameliorates podocyte injury in proteinuric rats via modulation of excessive Rho signaling. J Am Soc Nephrol 2006; 17: 754-764.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 754-764
    • Shibata, S.1    Nagase, M.2    Fujita, T.3
  • 48
    • 0037350930 scopus 로고    scopus 로고
    • Animal models of FSGS: Lessons for pathogenesis and treatment
    • Fogo AB. Animal models of FSGS: lessons for pathogenesis and treatment. Semin Nephrol 2003; 23: 161-171.
    • (2003) Semin Nephrol , vol.23 , pp. 161-171
    • Fogo, A.B.1
  • 50
    • 0037213069 scopus 로고    scopus 로고
    • Hypercholesterolemia is a prerequisite for puromycin inducible damage in mouse kidney
    • Cheng ZZ, Patari A, Aalto-Setala K et al. Hypercholesterolemia is a prerequisite for puromycin inducible damage in mouse kidney. Kidney Int 2003; 63: 107-112.
    • (2003) Kidney Int , vol.63 , pp. 107-112
    • Cheng, Z.Z.1    Patari, A.2    Aalto-Setala, K.3
  • 51
    • 33745871229 scopus 로고    scopus 로고
    • An ancestral haplotype defines susceptibility to doxorubicin nephropathy in the laboratory mouse
    • Zheng Z, Pavlidis P, Chua S et al. An ancestral haplotype defines susceptibility to doxorubicin nephropathy in the laboratory mouse. J Am Soc Nephrol 2006; 17: 1796-1800.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1796-1800
    • Zheng, Z.1    Pavlidis, P.2    Chua, S.3
  • 52
    • 0028941309 scopus 로고
    • Induction of proteinuria by adriamycin or bovine serum albumin in the mouse
    • Chen A, Wei CH, Sheu LF et al. Induction of proteinuria by adriamycin or bovine serum albumin in the mouse. Nephron 1995; 69: 293-300.
    • (1995) Nephron , vol.69 , pp. 293-300
    • Chen, A.1    Ch, W.2    Sheu, L.F.3
  • 53
    • 35948945659 scopus 로고    scopus 로고
    • Puromycin induces reversible proteinuric injury in transgenic mice expressing cyclooxygenase-2 in podocytes
    • Jo YI, Cheng H, Wang S et al. Puromycin induces reversible proteinuric injury in transgenic mice expressing cyclooxygenase-2 in podocytes. Nephron Exp Nephrol 2007; 107: e87-e94.
    • (2007) Nephron Exp Nephrol , vol.107
    • Jo, Y.I.1    Cheng, H.2    Wang, S.3
  • 54
    • 13244251341 scopus 로고    scopus 로고
    • Cytochrome P4502C9-derived epoxyeicosatrienoic acids induce the expression of cyclooxygenase-2 in endothelial cells
    • Michaelis UR, Falck JR, Schmidt R et al. Cytochrome P4502C9-derived epoxyeicosatrienoic acids induce the expression of cyclooxygenase-2 in endothelial cells. Arterioscler Thromb Vasc Biol 2005; 25: 321-326.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , pp. 321-326
    • Michaelis, U.R.1    Falck, J.R.2    Schmidt, R.3
  • 55
    • 33748611622 scopus 로고    scopus 로고
    • N-6 and n-3 polyunsaturated fatty acids downregulate cytochrome P-450 2B1 gene expression induced by Phenobarbital in primary rat hepatocytes
    • Li CC, Lii CK, Liu KL et al. n-6 and n-3 polyunsaturated fatty acids downregulate cytochrome P-450 2B1 gene expression induced by Phenobarbital in primary rat hepatocytes. J Nutr Biochem 2006; 17: 707-715.
    • (2006) J Nutr Biochem , vol.17 , pp. 707-715
    • Li, C.C.1    Lii, C.K.2    Liu, K.L.3
  • 56
    • 0034454016 scopus 로고    scopus 로고
    • Determining the best animal model for human cytochrome P450 activities: A comparison of mouse, rat, rabbit, dog, micropig, monkey and man
    • Bogaards JJ, Bertrand M, Jackson P et al. Determining the best animal model for human cytochrome P450 activities: a comparison of mouse, rat, rabbit, dog, micropig, monkey and man. Xenobiotica 2000; 30: 1131-1152.
    • (2000) Xenobiotica , vol.30 , pp. 1131-1152
    • Bogaards, J.J.1    Bertrand, M.2    Jackson, P.3
  • 58
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: A review of programmed cell death
    • Elmore S. Apoptosis: a review of programmed cell death. Toxicol Pathol 2007; 35: 495-516.
    • (2007) Toxicol Pathol , vol.35 , pp. 495-516
    • Elmore, S.1
  • 59
    • 0036203312 scopus 로고    scopus 로고
    • Long-term enhancement of cytochrome P450 2B1/2 expression in rat hepatocyte spheroids through adenovirus-mediated gene transfer
    • Tzanakakis ES, Waxman DJ, Hansen LK et al. Long-term enhancement of cytochrome P450 2B1/2 expression in rat hepatocyte spheroids through adenovirus-mediated gene transfer. Cell Biol Toxicol 2002; 18: 13-27.
    • (2002) Cell Biol Toxicol , vol.18 , pp. 13-27
    • Tzanakakis, E.S.1    Waxman, D.J.2    Hansen, L.K.3
  • 60
    • 0026526252 scopus 로고
    • A microplate assay for the detection of oxidative products using 20,70-ichlorofluoresceindiacetate
    • Rosenkranz AR, Schmaldienst S, Stuhlmeier KM et al. A microplate assay for the detection of oxidative products using 20,70-ichlorofluoresceindiacetate. J Immunol Methods 1992; 156: 39-45.
    • (1992) J Immunol Methods , vol.156 , pp. 39-45
    • Rosenkranz, A.R.1    Schmaldienst, S.2    Stuhlmeier, K.M.3
  • 61
    • 0029851650 scopus 로고    scopus 로고
    • Role of cytochrome P-450 in hydrogen peroxide-induced cytotoxicity to LLC-PK1 cells
    • Baliga R, Zhang Z, Shah SV. Role of cytochrome P-450 in hydrogen peroxide-induced cytotoxicity to LLC-PK1 cells. Kidney Int 1996; 50: 1118-1124.
    • (1996) Kidney Int , vol.50 , pp. 1118-1124
    • Baliga, R.1    Zhang, Z.2    Shah, S.V.3
  • 62
    • 0023713899 scopus 로고
    • Anti-Fx1A produces complementdependent cytotoxicity of glomerular epithelial cells
    • Quigg RJ, Cybulsky AV, Jacobs JB et al. Anti-Fx1A produces complementdependent cytotoxicity of glomerular epithelial cells. Kidney Int 1988; 34:43-52.
    • (1988) Kidney Int , vol.34 , pp. 43-52
    • Quigg, R.J.1    Cybulsky, A.V.2    Jacobs, J.B.3
  • 63
    • 0027347272 scopus 로고
    • Analysis of membrane proteins by western blotting and enhanced chemiluminescence
    • Bradd SJ, Dunn MJ. Analysis of membrane proteins by western blotting and enhanced chemiluminescence. Methods Mol Biol 1993; 19: 211-218.
    • (1993) Methods Mol Biol , vol.19 , pp. 211-218
    • Bradd, S.J.1    Dunn, M.J.2
  • 64
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001; 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.