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Volumn 78, Issue 2, 2010, Pages 269-278

Erratum: Deletion of Microsomal Cytochrome b5 Profoundly Affects Hepatic and Extrahepatic Drug Metabolism (Molecular Pharmacology (2010) 78 (269-278) DOI: 10.1124/mol.110.064246);Deletion of microsomal cytochrome b5 profoundly affects hepatic and extrahepatic drug metabolism

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B5; CYTOCHROME P450; CYTOCHROME P450 17; DRUG METABOLIZING ENZYME; HYDROLASE; ISOPROTEIN; LYASE; MESSENGER RNA; METHEMOGLOBIN; MICROSOME ENZYME; TESTOSTERONE;

EID: 77954890052     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.114.85er01     Document Type: Erratum
Times cited : (62)

References (44)
  • 1
    • 28044470748 scopus 로고    scopus 로고
    • Cytochrome b(5) modulation of 17{alpha} hydroxylase and 17-20 lyase (CYP17) activities in steroidogenesis
    • Akhtar MK, Kelly SL, and Kaderbhai MA (2005) Cytochrome b(5) modulation of 17{alpha} hydroxylase and 17-20 lyase (CYP17) activities in steroidogenesis. J Endocrinol 187:267-274.
    • (2005) J Endocrinol , vol.187 , pp. 267-274
    • Akhtar, M.K.1    Kelly, S.L.2    Kaderbhai, M.A.3
  • 2
    • 0035893819 scopus 로고    scopus 로고
    • Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy
    • Anzenbacher P and Hudecek J (2001) Differences in flexibility of active sites of cytochromes P450 probed by resonance Raman and UV-Vis absorption spectroscopy. J Inorg Biochem 87:209-213.
    • (2001) J Inorg Biochem , vol.87 , pp. 209-213
    • Anzenbacher, P.1    Hudecek, J.2
  • 3
    • 0032488666 scopus 로고    scopus 로고
    • Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer
    • Auchus RJ, Lee TC, and Miller WL (1998) Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer. J Biol Chem 273:3158-3165.
    • (1998) J Biol Chem , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 4
    • 33847017210 scopus 로고    scopus 로고
    • Reduction of hexavalent chromium by human cytochrome b5: Generation of hydroxyl radical and superoxide
    • discussion 735-737.
    • Borthiry GR, Antholine WE, Kalyanaraman B, Myers JM, and Myers CR (2007) Reduction of hexavalent chromium by human cytochrome b5: generation of hydroxyl radical and superoxide. Free Radic Biol Med 42:738-755; discussion 735-737.
    • (2007) Free Radic Biol Med , vol.42 , pp. 738-755
    • Borthiry, G.R.1    Antholine, W.E.2    Kalyanaraman, B.3    Myers, J.M.4    Myers, C.R.5
  • 6
    • 0022647249 scopus 로고
    • Unique properties of NADPH- And NADH-dependent metabolism of p-nitroanisole catalyzed by cytochrome p-450 isozyme 2 in pulmonary and hepatic microsomal preparations from rabbits
    • DOI 10.1016/0009-2797(86)90034-7
    • Croft JE, Harrelson WG, Parandoosh Z, and Philpot RM (1986) Unique properties of NADPH- and NADH-dependent metabolism of p-nitroanisole catalyzed by cytochrome P-450 isozyme 2 in pulmonary and hepatic microsomal preparations from rabbits. Chem Biol Interact 57:143-160. (Pubitemid 16168267)
    • (1986) Chemico-Biological Interactions , vol.57 , Issue.2 , pp. 143-160
    • Croft, J.E.1    Harrelson, W.G.2    Parandoosh, Z.3    Philpot, R.M.4
  • 7
    • 58249089410 scopus 로고    scopus 로고
    • Unsaturated fatty acid regulation of cytochrome P450 expression via a CAR-dependent pathway
    • Finn RD, Henderson CJ, Scott CL, and Wolf CR (2009) Unsaturated fatty acid regulation of cytochrome P450 expression via a CAR-dependent pathway. Biochem J 417:43-54.
    • (2009) Biochem J , vol.417 , pp. 43-54
    • Finn, R.D.1    Henderson, C.J.2    Scott, C.L.3    Wolf, C.R.4
  • 9
    • 57649128309 scopus 로고    scopus 로고
    • Defining the in vivo role for cytochrome b5 in cytochrome P450 function through the conditional hepatic deletion of microsomal cytochrome b5
    • Finn RD, McLaughlin LA, Ronseaux S, Rosewell I, Houston JB, Henderson CJ, and Wolf CR (2008) Defining the in vivo role for cytochrome b5 in cytochrome P450 function through the conditional hepatic deletion of microsomal cytochrome b5. J Biol Chem 283:31385-31393.
    • (2008) J Biol Chem , vol.283 , pp. 31385-31393
    • Finn, R.D.1    McLaughlin, L.A.2    Ronseaux, S.3    Rosewell, I.4    Houston, J.B.5    Henderson, C.J.6    Wolf, C.R.7
  • 11
    • 0028860850 scopus 로고
    • The stoichiometry of the cytochrome P-450-catalyzed metabolism of methoxyflurane and benzphetamine in the presence and absence of cytochrome b5
    • Gruenke LD, Konopka K, Cadieu M, and Waskell L (1995) The stoichiometry of the cytochrome P-450-catalyzed metabolism of methoxyflurane and benzphetamine in the presence and absence of cytochrome b5. J Biol Chem 270:24707-24718.
    • (1995) J Biol Chem , vol.270 , pp. 24707-24718
    • Gruenke, L.D.1    Konopka, K.2    Cadieu, M.3    Waskell, L.4
  • 12
    • 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 QY, Cui H, Behr M, Wu L, Yang W, Zhang L, and Ding X (2003) 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 278:25895-25901.
    • (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
  • 13
    • 0035942308 scopus 로고    scopus 로고
    • Interaction of apocytochrome b5 with cytochromes P4503A4 and P45017A: Relevance of heme transfer reactions
    • Guryev OL, Gilep AA, Usanov SA, and Estabrook RW (2001) Interaction of apocytochrome b5 with cytochromes P4503A4 and P45017A: relevance of heme transfer reactions. Biochemistry 40:5018-5031.
    • (2001) Biochemistry , vol.40 , pp. 5018-5031
    • Guryev, O.L.1    Gilep, A.A.2    Usanov, S.A.3    Estabrook, R.W.4
  • 14
    • 0037790603 scopus 로고    scopus 로고
    • Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase
    • Henderson CJ, Otto DM, Carrie D, Magnuson MA, McLaren AW, Rosewell I, and Wolf CR (2003) Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase. J Biol Chem 278:13480-13486.
    • (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
    • 0015032258 scopus 로고
    • Evidence for the participation of cytochrome b 5 in hepatic microsomal mixed-function oxidation reactions
    • Hildebrandt A and Estabrook RW (1971) Evidence for the participation of cytochrome b 5 in hepatic microsomal mixed-function oxidation reactions. Arch Biochem Biophys 143:66-79.
    • (1971) Arch Biochem Biophys , vol.143 , pp. 66-79
    • Hildebrandt, A.1    Estabrook, R.W.2
  • 16
    • 0034800477 scopus 로고    scopus 로고
    • Allosteric phenomena in cytochrome P450-catalyzed monooxygenations
    • Hlavica P and Lewis DF (2001) Allosteric phenomena in cytochrome P450-catalyzed monooxygenations. Eur J Biochem 268:4817-4832.
    • (2001) Eur J Biochem , vol.268 , pp. 4817-4832
    • Hlavica, P.1    Lewis, D.F.2
  • 17
    • 0017616332 scopus 로고
    • Properties of rat liver microsomal stearoyl coenzyme a desaturase
    • Jeffcoat R, Brawn PR, Safford R, and James AT (1977) Properties of rat liver microsomal stearoyl-coenzyme A desaturase. Biochem J 161:431-437. (Pubitemid 8025747)
    • (1977) Biochemical Journal , vol.161 , Issue.2 , pp. 431-437
    • Jeffcoat, R.1    Brawn, P.R.2    Safford, R.3    James, A.T.4
  • 18
    • 34447298906 scopus 로고    scopus 로고
    • Discovery and characterization of a cytochrome b5 variant in humans with impaired hydroxylamine reduction capacity
    • Kurian JR, Longlais BJ, and Trepanier LA (2007) Discovery and characterization of a cytochrome b5 variant in humans with impaired hydroxylamine reduction capacity. Pharmacogenet Genomics 17:597-603.
    • (2007) Pharmacogenet Genomics , vol.17 , pp. 597-603
    • Kurian, J.R.1    Longlais, B.J.2    Trepanier, L.A.3
  • 19
    • 0032030846 scopus 로고    scopus 로고
    • Maternally expressed PGK-Cre transgene as a tool for early and uniform activation of the Cre sitespecific recombinase
    • Lallemand Y, Luria V, Haffner-Krausz R, and Lonai P (1998) Maternally expressed PGK-Cre transgene as a tool for early and uniform activation of the Cre sitespecific recombinase. Transgenic Res 7:105-112.
    • (1998) Transgenic Res , vol.7 , pp. 105-112
    • Lallemand, Y.1    Luria, V.2    Haffner-Krausz, R.3    Lonai, P.4
  • 21
    • 0025891307 scopus 로고
    • Biosynthesis of choline plasmalogens in neonatal rat myocytes
    • Lee TC, Qian CG, and Snyder F (1991) Biosynthesis of choline plasmalogens in neonatal rat myocytes. Arch Biochem Biophys 286:498-503.
    • (1991) Arch Biochem Biophys , vol.286 , pp. 498-503
    • Lee, T.C.1    Qian, C.G.2    Snyder, F.3
  • 22
    • 0023788714 scopus 로고
    • Regulation of phenobarbital-inducible cytochrome P-450s in rat and mouse liver following dexamethasone administration and hypophysectomy
    • Meehan RR, Forrester LM, Stevenson K, Hastie ND, Buchmann A, Kunz HW, and Wolf CR (1988) Regulation of phenobarbital-inducible cytochrome P-450s in rat and mouse liver following dexamethasone administration and hypophysectomy. Biochem J 254:789-797.
    • (1988) Biochem J , vol.254 , pp. 789-797
    • Meehan, R.R.1    Forrester, L.M.2    Stevenson, K.3    Hastie, N.D.4    Buchmann, A.5    Kunz, H.W.6    Wolf, C.R.7
  • 23
    • 31044440024 scopus 로고    scopus 로고
    • Human cytochrome b5 requires residues E48 and E49 to stimulate the 17,20-lyase activity of cytochrome P450c17
    • Naffin-Olivos JL and Auchus RJ (2006) Human cytochrome b5 requires residues E48 and E49 to stimulate the 17,20-lyase activity of cytochrome P450c17. Biochemistry 45:755-762.
    • (2006) Biochemistry , vol.45 , pp. 755-762
    • Naffin-Olivos, J.L.1    Auchus, R.J.2
  • 24
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T and Sato R (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239:2370-2378.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 25
    • 0037423276 scopus 로고    scopus 로고
    • Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6
    • Paine MJ, McLaughlin LA, Flanagan JU, Kemp CA, Sutcliffe MJ, Roberts GC, and Wolf CR (2003) Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6. J Biol Chem 278:4021-4027.
    • (2003) J Biol Chem , vol.278 , pp. 4021-4027
    • Paine, M.J.1    McLaughlin, L.A.2    Flanagan, J.U.3    Kemp, C.A.4    Sutcliffe, M.J.5    Roberts, G.C.6    Wolf, C.R.7
  • 26
    • 0016230515 scopus 로고
    • Evidence for the participation of cytochrome b5 in plasmalogen biosynthesis
    • Paltuaf F, Prough RA, Masters BS, and Johnston JM (1974) Evidence for the participation of cytochrome b5 in plasmalogen biosynthesis. J Biol Chem 249:2661-2662.
    • (1974) J Biol Chem , vol.249 , pp. 2661-2662
    • Paltuaf, F.1    Prough, R.A.2    Masters, B.S.3    Johnston, J.M.4
  • 27
    • 0028948688 scopus 로고
    • Baculovirus expression of human P450 2E1 and cytochrome b5: Spectral and catalytic properties and effect of b5 on the stoichiometry of P450 2E1-catalyzed reactions
    • Patten CJ and Koch P (1995) Baculovirus expression of human P450 2E1 and cytochrome b5: spectral and catalytic properties and effect of b5 on the stoichiometry of P450 2E1-catalyzed reactions. Arch Biochem Biophys 317:504-513.
    • (1995) Arch Biochem Biophys , vol.317 , pp. 504-513
    • Patten, C.J.1    Koch, P.2
  • 28
    • 0036947946 scopus 로고    scopus 로고
    • The roles of cytochrome b5 in cytochrome P450 reactions
    • Porter TD (2002) The roles of cytochrome b5 in cytochrome P450 reactions. J Biochem Mol Toxicol 16:311-316.
    • (2002) J Biochem Mol Toxicol , vol.16 , pp. 311-316
    • Porter, T.D.1
  • 30
    • 0037306331 scopus 로고    scopus 로고
    • The many roles of cytochrome b5
    • Schenkman JB and Jansson I (2003) The many roles of cytochrome b5. Pharmacol Ther 97:139-152.
    • (2003) Pharmacol Ther , vol.97 , pp. 139-152
    • Schenkman, J.B.1    Jansson, I.2
  • 31
    • 12844261851 scopus 로고    scopus 로고
    • Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b(5) enzymes
    • Shimada T, Mernaugh RL, and Guengerich FP (2005) Interactions of mammalian cytochrome P450, NADPH-cytochrome P450 reductase, and cytochrome b(5) enzymes. Arch Biochem Biophys 435:207-216.
    • (2005) Arch Biochem Biophys , vol.435 , pp. 207-216
    • Shimada, T.1    Mernaugh, R.L.2    Guengerich, F.P.3
  • 32
    • 0017795019 scopus 로고
    • Purification and properties of NADPHcytochrome P-450 reductase
    • Strobel HW and Dignam JD (1978) Purification and properties of NADPHcytochrome P-450 reductase. Methods Enzymol 52:89-96.
    • (1978) Methods Enzymol , vol.52 , pp. 89-96
    • Strobel, H.W.1    Dignam, J.D.2
  • 33
    • 33846476692 scopus 로고    scopus 로고
    • Methemoglobin-it's not just blue: A concise review
    • Umbreit J (2007) Methemoglobin-it's not just blue: a concise review. Am J Hematol 82:134-144.
    • (2007) Am J Hematol , vol.82 , pp. 134-144
    • Umbreit, J.1
  • 35
    • 0023007898 scopus 로고
    • Identification of the enzymes catalyzing metabolism of methoxyflurane
    • Waskell L, Canova-Davis E, Philpot R, Parandoush Z, and Chiang JY (1986) Identification of the enzymes catalyzing metabolism of methoxyflurane. Drug Metab Dispos 14:643-648. (Pubitemid 17202400)
    • (1986) Drug Metabolism and Disposition , vol.14 , Issue.6 , pp. 643-648
    • Waskell, L.1    Canova-Davis, E.2    Philpot, R.3
  • 36
    • 0017794805 scopus 로고
    • Enzymic studies on glial and neuronal cells during myelination
    • Woelk H and Jahrreiss R (1978) Enzymic studies on glial and neuronal cells during myelination. Adv Exp Med Biol 100:43-53.
    • (1978) Adv Exp Med Biol , vol.100 , pp. 43-53
    • Woelk, H.1    Jahrreiss, R.2
  • 37
    • 0345016882 scopus 로고    scopus 로고
    • Effects of cytochrome b(5) on drug oxidation activities of human cytochrome P450 (CYP) 3As: Similarity of CYP3A5 with CYP3A4 but not CYP3A7
    • Yamaori S, Yamazaki H, Suzuki A, Yamada A, Tani H, Kamidate T, Fujita K, and Kamataki T (2003) Effects of cytochrome b(5) on drug oxidation activities of human cytochrome P450 (CYP) 3As: similarity of CYP3A5 with CYP3A4 but not CYP3A7. Biochem Pharmacol 66:2333-2340.
    • (2003) Biochem Pharmacol , vol.66 , pp. 2333-2340
    • Yamaori, S.1    Yamazaki, H.2    Suzuki, A.3    Yamada, A.4    Tani, H.5    Kamidate, T.6    Fujita, K.7    Kamataki, T.8
  • 38
    • 0029926494 scopus 로고    scopus 로고
    • Lack of electron transfer from cytochrome b5 in stimulation of catalytic activities of cytochrome P450 3A4. Characterization of a reconstituted cytochrome P450 3A4/ NADPH-cytochrome P450 reductase system and studies with apo-cytochrome b5
    • Yamazaki H, Johnson WW, Ueng YF, Shimada T, and Guengerich FP (1996) Lack of electron transfer from cytochrome b5 in stimulation of catalytic activities of cytochrome P450 3A4. Characterization of a reconstituted cytochrome P450 3A4/ NADPH-cytochrome P450 reductase system and studies with apo-cytochrome b5. J Biol Chem 271:27438-27444.
    • (1996) J Biol Chem , vol.271 , pp. 27438-27444
    • Yamazaki, H.1    Johnson, W.W.2    Ueng, Y.F.3    Shimada, T.4    Guengerich, F.P.5
  • 39
    • 0036447583 scopus 로고    scopus 로고
    • Roles of NADPH-P450 reductase and apo- And holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli
    • Yamazaki H, Nakamura M, Komatsu T, Ohyama K, Hatanaka N, Asahi S, Shimada N, Guengerich FP, Shimada T, Nakajima M, et al. (2002) Roles of NADPH-P450 reductase and apo- and holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli. Protein Expr Purif 24:329-337.
    • (2002) Protein Expr Purif , vol.24 , pp. 329-337
    • Yamazaki, H.1    Nakamura, M.2    Komatsu, T.3    Ohyama, K.4    Hatanaka, N.5    Asahi, S.6    Shimada, N.7    Guengerich, F.P.8    Shimada, T.9    Nakajima, M.10
  • 40
    • 33745122525 scopus 로고    scopus 로고
    • Cytochrome P450 reconstitution systems
    • Yamazaki H and Shimada T (2006) Cytochrome P450 reconstitution systems. Methods Mol Biol 320:61-71.
    • (2006) Methods Mol Biol , vol.320 , pp. 61-71
    • Yamazaki, H.1    Shimada, T.2
  • 41
    • 0344823859 scopus 로고    scopus 로고
    • The low gonadotropin-independent constitutive production of testicular testosterone is sufficient to maintain spermatogenesis
    • Zhang FP, Pakarainen T, Poutanen M, Toppari J, and Huhtaniemi I (2003) The low gonadotropin-independent constitutive production of testicular testosterone is sufficient to maintain spermatogenesis. Proc Natl Acad Sci USA 100:13692-13697.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13692-13697
    • Zhang, F.P.1    Pakarainen, T.2    Poutanen, M.3    Toppari, J.4    Huhtaniemi, I.5
  • 42
    • 41949131364 scopus 로고    scopus 로고
    • Cytochrome b5 inhibits electron transfer from NADPH-cytochrome P450 reductase to ferric cytochrome P450 2B4
    • Zhang H, Hamdane D, Im SC, and Waskell L (2008) Cytochrome b5 inhibits electron transfer from NADPH-cytochrome P450 reductase to ferric cytochrome P450 2B4. J Biol Chem 283:5217-5225.
    • (2008) J Biol Chem , vol.283 , pp. 5217-5225
    • Zhang, H.1    Hamdane, D.2    Im, S.C.3    Waskell, L.4
  • 43
    • 35648963202 scopus 로고    scopus 로고
    • Cytochrome b5 increases the rate of product formation by cytochrome P450 2B4 and competes with cytochrome P450 reductase for a binding site on cytochrome P450 2B4
    • Zhang H, Im SC, and Waskell L (2007) Cytochrome b5 increases the rate of product formation by cytochrome P450 2B4 and competes with cytochrome P450 reductase for a binding site on cytochrome P450 2B4. J Biol Chem 282:29766-29776.
    • (2007) J Biol Chem , vol.282 , pp. 29766-29776
    • Zhang, H.1    Im, S.C.2    Waskell, L.3
  • 44
    • 27544474271 scopus 로고    scopus 로고
    • Role of cytochrome b5 in catalysis by cytochrome P450 2B4
    • Zhang H, Myshkin E, and Waskell L (2005) Role of cytochrome b5 in catalysis by cytochrome P450 2B4. Biochem Biophys Res Commun 338:499-506.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 499-506
    • Zhang, H.1    Myshkin, E.2    Waskell, L.3


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