메뉴 건너뛰기




Volumn 216, Issue 4-5, 1999, Pages 511-517

Two novel sites of expression of NADPH cytochrome P450 reductase during murine embryogenesis: Limb mesenchyme and developing olfactory neuroepithelia

Author keywords

Cytochrome P450 reductase; Limb development; Mesenchymal cell differentiation; Mouse embryogenesis

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

EID: 0032757423     PISSN: 10588388     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0177(199912)216:4/5<511::aid-dvdy19>3.0.co;2-h     Document Type: Article
Times cited : (12)

References (27)
  • 1
    • 0026110377 scopus 로고
    • Characterization of the cytochrome P450 monooxygenase system in nonciliated bronchiolar epithelial (Clara) cells isolated from mouse lung
    • Chichester CH, Philpot RM, Weir AJ, Buckpitt AR, Plopper CG. 1991. Characterization of the cytochrome P450 monooxygenase system in nonciliated bronchiolar epithelial (Clara) cells isolated from mouse lung. Am J Respir Cell Mol Biol 4:179-186.
    • (1991) Am J Respir Cell Mol Biol , vol.4 , pp. 179-186
    • Chichester, C.H.1    Philpot, R.M.2    Weir, A.J.3    Buckpitt, A.R.4    Plopper, C.G.5
  • 2
    • 0019321169 scopus 로고
    • 5 with stearyl coenzyme A desaturase and NADPH:Cytochrome P-450 reductase
    • 5 with stearyl coenzyme A desaturase and NADPH:cytochrome P-450 reductase. J Biol Chem 255:5184-5189.
    • (1980) J Biol Chem , vol.255 , pp. 5184-5189
    • Dailey, H.A.1    Strittmatter, P.2
  • 3
    • 0001594031 scopus 로고
    • Extrahepatic microsomal forms: Olfactory cytochrome P450
    • Schenkman JB, Greim H, editors. Berlin: Springer-Verlag
    • Ding X, Coon MJ. 1992. Extrahepatic microsomal forms: olfactory cytochrome P450. In: Schenkman JB, Greim H, editors. Handbook of experimental pharmacology, volume. 105. Berlin: Springer-Verlag. p 351-361.
    • (1992) Handbook of Experimental Pharmacology , vol.105 , pp. 351-361
    • Ding, X.1    Coon, M.J.2
  • 4
    • 0027756145 scopus 로고
    • Sonic hedgehog, a member of a family of putative signaling molecules, is implicated in the regulation of CNS polarity
    • Echelard Y, Epstein DJ, St-Jaques B, Shen L, Mohler J, McMahon JA, McMahon AP. 1993. Sonic hedgehog, a member of a family of putative signaling molecules, is implicated in the regulation of CNS polarity. Cell 75:1417-1430.
    • (1993) Cell , vol.75 , pp. 1417-1430
    • Echelard, Y.1    Epstein, D.J.2    St-Jaques, B.3    Shen, L.4    Mohler, J.5    McMahon, J.A.6    McMahon, A.P.7
  • 5
    • 0018801347 scopus 로고
    • Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase
    • Enoch HG, Strittmatter P. 1979. Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase. J Biol Chem 254:8976-8981.
    • (1979) J Biol Chem , vol.254 , pp. 8976-8981
    • Enoch, H.G.1    Strittmatter, P.2
  • 6
    • 0030872361 scopus 로고    scopus 로고
    • Metabolic inactivation of retinoic acid by a novel P450 differentially expressed in developing mouse embryos
    • Fujii H, Sato T, Kaneko S, Gotoh K, Kato S, Hamada H. 1997. Metabolic inactivation of retinoic acid by a novel P450 differentially expressed in developing mouse embryos. EMBO J 16:4163-4173.
    • (1997) EMBO J , vol.16 , pp. 4163-4173
    • Fujii, H.1    Sato, T.2    Kaneko, S.3    Gotoh, K.4    Kato, S.5    Hamada, H.6
  • 7
    • 0024519596 scopus 로고
    • Immunohistochemical localization of NADPH-cytochrome P450 reductase in human tissues
    • Hall PM, Stupans I, Burgess W, Birkett DJ, McManus ME. 1989. Immunohistochemical localization of NADPH-cytochrome P450 reductase in human tissues. Carcinogenesis 10:521-530.
    • (1989) Carcinogenesis , vol.10 , pp. 521-530
    • Hall, P.M.1    Stupans, I.2    Burgess, W.3    Birkett, D.J.4    McManus, M.E.5
  • 8
    • 0031000922 scopus 로고    scopus 로고
    • Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: Pronounced expression in antennae may be related to odorant clearance
    • Hovemann BT, Sehlmeyer F, Malz J. 1997. Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: pronounced expression in antennae may be related to odorant clearance. Gene 189:213-219.
    • (1997) Gene , vol.189 , pp. 213-219
    • Hovemann, B.T.1    Sehlmeyer, F.2    Malz, J.3
  • 9
    • 0019877474 scopus 로고
    • Evidence for a new physiological role of hepatic NADPH:Ferricytochrome (P-450) oxidoreductase
    • Ilan Z, Ilan R, Cinti DL. 1981. Evidence for a new physiological role of hepatic NADPH:ferricytochrome (P-450) oxidoreductase. J Biol Chem 256:10066-10072.
    • (1981) J Biol Chem , vol.256 , pp. 10066-10072
    • Ilan, Z.1    Ilan, R.2    Cinti, D.L.3
  • 10
    • 0345294883 scopus 로고
    • On the mechanism of action of hepatic cytochrome P-450 reductase
    • King SE, Mason HS, Morrison M., editors. Oxford: Pergamon Press
    • Iyanagi T, Mason HS. 1979. On the mechanism of action of hepatic cytochrome P-450 reductase. In: King SE, Mason HS, Morrison M., editors. Oxidases and related redox systems. Oxford: Pergamon Press, p 887-901.
    • (1979) Oxidases and Related Redox Systems , pp. 887-901
    • Iyanagi, T.1    Mason, H.S.2
  • 11
    • 0004630507 scopus 로고    scopus 로고
    • Radiolabeled cRNA and in situ hybridization
    • Sundberg JP, Bogess D, editors. Boca Raton: CRC Press
    • Keeney DS. 1999. Radiolabeled cRNA and in situ hybridization. In: Sundberg JP, Bogess D, editors. Systematic approach to evaluation of mouse mutations. Boca Raton: CRC Press, p 145-167.
    • (1999) Systematic Approach to Evaluation of Mouse Mutations , pp. 145-167
    • Keeney, D.S.1
  • 12
    • 0029064861 scopus 로고
    • Cholesterol side-chain cleavage cytochrome P450 gene expression in the primitive gut of the mouse embryo does not require steroidogenic factor 1
    • Keeney DS, Ikeda Y, Waterman MR, Parker KL. 1995. Cholesterol side-chain cleavage cytochrome P450 gene expression in the primitive gut of the mouse embryo does not require steroidogenic factor 1. Mol Cell Endocrinol 9:1091-1098.
    • (1995) Mol Cell Endocrinol , vol.9 , pp. 1091-1098
    • Keeney, D.S.1    Ikeda, Y.2    Waterman, M.R.3    Parker, K.L.4
  • 13
    • 0033610838 scopus 로고    scopus 로고
    • Differentiating keratinocytes express a novel cytochrome P450 enzyme, CYP2B19, having arachidonate monooxygenase activity
    • Keeney DS, Skinner C, Travers JB, Capdevila JH, Nanney LB, King Jr. LE, Waterman MR. 1998a. Differentiating keratinocytes express a novel cytochrome P450 enzyme, CYP2B19, having arachidonate monooxygenase activity. J Biol Chem 273:32071-32079.
    • (1998) J Biol Chem , vol.273 , pp. 32071-32079
    • Keeney, D.S.1    Skinner, C.2    Travers, J.B.3    Capdevila, J.H.4    Nanney, L.B.5    King L.E., Jr.6    Waterman, M.R.7
  • 14
    • 0032502795 scopus 로고    scopus 로고
    • A keratinocyte-specific epoxygenase, CYP2B12, metabolizes arachidonic acid with unusual selectivity, producing a single major epoxyeicosatrienoic acid
    • Keeney DS, Skinner C, Wei S, Friedberg T, Waterman MR. 1998b. A keratinocyte-specific epoxygenase, CYP2B12, metabolizes arachidonic acid with unusual selectivity, producing a single major epoxyeicosatrienoic acid. J Biol Chem 273:9279-9284.
    • (1998) J Biol Chem , vol.273 , pp. 9279-9284
    • Keeney, D.S.1    Skinner, C.2    Wei, S.3    Friedberg, T.4    Waterman, M.R.5
  • 15
    • 0029038234 scopus 로고
    • The subcellular distribution of NADPH-cytochrome P450 reductase and isoenzymes of cytochrome P450 in the lungs of rats and mice
    • Lee MJ, Dinsdale D. 1995. The subcellular distribution of NADPH-cytochrome P450 reductase and isoenzymes of cytochrome P450 in the lungs of rats and mice. Biochem Pharmacol 49:1387-1394.
    • (1995) Biochem Pharmacol , vol.49 , pp. 1387-1394
    • Lee, M.J.1    Dinsdale, D.2
  • 16
    • 0018962751 scopus 로고
    • The history, properties, and function of NADPH-cytochrome P-450 reductase
    • Masters BSS, Okita RT. 1980. The history, properties, and function of NADPH-cytochrome P-450 reductase. Pharmacol Ther 9:227-244.
    • (1980) Pharmacol Ther , vol.9 , pp. 227-244
    • Masters, B.S.S.1    Okita, R.T.2
  • 17
    • 0033199227 scopus 로고    scopus 로고
    • A second CYP26 P450 in humans and zebrafish: CYP26B1
    • Nelson DR. 1999. A second CYP26 P450 in humans and zebrafish: CYP26B1. Arch Biochem Biophys 369:1-10.
    • (1999) Arch Biochem Biophys , vol.369 , pp. 1-10
    • Nelson, D.R.1
  • 18
    • 0018790605 scopus 로고
    • Specific requirement of NADPH-cytochrome c reductase for the microsomal heme oxygenase reaction yielding biliverdin IX
    • Noguchi M, Yoshida T, Kikuchi G. 1979. Specific requirement of NADPH-cytochrome c reductase for the microsomal heme oxygenase reaction yielding biliverdin IX. FEBS Letters 98:281-284.
    • (1979) FEBS Letters , vol.98 , pp. 281-284
    • Noguchi, M.1    Yoshida, T.2    Kikuchi, G.3
  • 19
    • 0017339034 scopus 로고
    • Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system
    • Ono T, Ozasa S, Hasegawa F, Imai Y. 1977. Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system. Biochim Biophys Acta 486:401-407.
    • (1977) Biochim Biophys Acta , vol.486 , pp. 401-407
    • Ono, T.1    Ozasa, S.2    Hasegawa, F.3    Imai, Y.4
  • 20
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of hedgehog signaling proteins in animal development
    • Porter JA, Young KE, Beachy PA. 1996 Cholesterol modification of hedgehog signaling proteins in animal development. Science 274: 255-259.
    • (1996) Science , vol.274 , pp. 255-259
    • Porter, J.A.1    Young, K.E.2    Beachy, P.A.3
  • 21
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • Schacter BA, Nelson EB, Marver HS, Masters BSS. 1972. Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system. J Biol Chem 247:3601-3607.
    • (1972) J Biol Chem , vol.247 , pp. 3601-3607
    • Schacter, B.A.1    Nelson, E.B.2    Marver, H.S.3    Masters, B.S.S.4
  • 22
    • 0003168207 scopus 로고
    • Protein and gene structure and regulation of NADPH-cytochrome P450 oxidoreductase
    • Schenkman JB, Greim H, editors. Berlin:Springer-Verlag
    • Shen AL, Kasper CB. 1993. Protein and gene structure and regulation of NADPH-cytochrome P450 oxidoreductase. In: Schenkman JB, Greim H, editors. Cytochrome P450. Berlin:Springer-Verlag. p 35-59.
    • (1993) Cytochrome P450 , pp. 35-59
    • Shen, A.L.1    Kasper, C.B.2
  • 24
    • 0025439242 scopus 로고
    • The immunocytochemical detection of cytochrome P-450 monooxygenase in the lungs of fetal, neonatal, and adult hamsters
    • Strum JM, Ito T, Philpot RM, DeSanti AM, McDowell EM. 1990. The immunocytochemical detection of cytochrome P-450 monooxygenase in the lungs of fetal, neonatal, and adult hamsters. Am J Respir Cell Mol Biol 2:493-501.
    • (1990) Am J Respir Cell Mol Biol , vol.2 , pp. 493-501
    • Strum, J.M.1    Ito, T.2    Philpot, R.M.3    DeSanti, A.M.4    McDowell, E.M.5
  • 25
    • 0021814201 scopus 로고
    • Localization of a cytochrome P-450 isozyme (cytochrome P-450 PB-B) and NADPH-cytochrome P-450 reductase in rat nasal mucosa
    • Voigt JM, Guengerich FP, Baron J. 1985. Localization of a cytochrome P-450 isozyme (cytochrome P-450 PB-B) and NADPH-cytochrome P-450 reductase in rat nasal mucosa. Cancer Letters 27:241-247.
    • (1985) Cancer Letters , vol.27 , pp. 241-247
    • Voigt, J.M.1    Guengerich, F.P.2    Baron, J.3
  • 26
    • 0001244671 scopus 로고
    • Whole mount in situ hybridization of vertebrate embryos
    • Wilkinson DG, editor. Oxford: IRL Press
    • Wilkinson DG. 1992. Whole mount in situ hybridization of vertebrate embryos. In: Wilkinson DG, editor. In situ hybridization a practical approach. Oxford: IRL Press, p 75-83.
    • (1992) In Situ Hybridization a Practical Approach , pp. 75-83
    • Wilkinson, D.G.1
  • 27
    • 0016761268 scopus 로고
    • Participation of NADPH-cytochrome c reductase in thyroid hormone biosynthesis
    • Yamamoto J, DeGroot LJ. 1975. Participation of NADPH-cytochrome c reductase in thyroid hormone biosynthesis. Endocrinology 96:1022-1029.
    • (1975) Endocrinology , vol.96 , pp. 1022-1029
    • Yamamoto, J.1    DeGroot, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.