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Volumn 1453, Issue 1, 1999, Pages 161-174

Targeted disruption of the mouse ferrochelatase gene producing an exon 10 deletion

Author keywords

Embryonic stem cell; Exon 10 deletion; Ferrochelatase; Gene targeting; Protoporphyria

Indexed keywords

FERROCHELATASE; MESSENGER RNA;

EID: 0032926350     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0925-4439(98)00096-9     Document Type: Article
Times cited : (12)

References (55)
  • 2
    • 0026576256 scopus 로고
    • Structure of the human ferrochelatase gene. Exon/intron gene organization and localization of the gene to chromosome 18
    • S. Taketani, J. Nazawa, Y. Nakahashi, T. Abe, R. Tokunaga, Structure of the human ferrochelatase gene. Exon/intron gene organization and localization of the gene to chromosome 18, Eur. J. Biochem. 205 (1992) 217-222.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 217-222
    • Taketani, S.1    Nazawa, J.2    Nakahashi, Y.3    Abe, T.4    Tokunaga, R.5
  • 3
    • 0026331629 scopus 로고
    • Assignment of the human ferrochelatase gene (FECH) and a locus for protoporphyria to chromosome 18q22
    • D.M. Whitcomb, N.P. Carter, D.G. Albertson, S.J. Smith, Assignment of the human ferrochelatase gene (FECH) and a locus for protoporphyria to chromosome 18q22., Genomics 11 (1991) 1152-1154.
    • (1991) Genomics , vol.11 , pp. 1152-1154
    • Whitcomb, D.M.1    Carter, N.P.2    Albertson, D.G.3    Smith, S.J.4
  • 5
    • 0028034531 scopus 로고
    • A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene
    • A.T. Tugores, S.T. Magness, D.A. Brenner, A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene, J. Biol. Chem. 269 (1994) 30789-30797.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30789-30797
    • Tugores, A.T.1    Magness, S.T.2    Brenner, D.A.3
  • 6
    • 0032126635 scopus 로고    scopus 로고
    • Analysis of the ferrochelatase promoter in transgenic mice
    • S.T. Magness, A. Tugores, E.S. Diala, D.A. Brenner, Analysis of the ferrochelatase promoter in transgenic mice, Blood 91 (1998) 320-328.
    • (1998) Blood , vol.91 , pp. 320-328
    • Magness, S.T.1    Tugores, A.2    Diala, E.S.3    Brenner, D.A.4
  • 7
    • 0027377723 scopus 로고
    • Biphasic ordered induction of heme synthesis in differentiation murine erythroleukemia cells : Role of erythroid 5-aminolevulinate synthase
    • H. Lake-Bullock, H.A. Dailey, Biphasic ordered induction of heme synthesis in differentiation murine erythroleukemia cells : role of erythroid 5-aminolevulinate synthase, Mol. Cell Biol. 13 (1993) 7122-7132.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 7122-7132
    • Lake-Bullock, H.1    Dailey, H.A.2
  • 8
    • 0024363023 scopus 로고
    • The 'priming phenomenon' in the acute phototoxicity of erythropoietic protoporphyria
    • M.B. Poh-Fitzpatrick, The 'priming phenomenon' in the acute phototoxicity of erythropoietic protoporphyria, J. Am. Acad. Dermatol. 21 (1989) 311.
    • (1989) J. Am. Acad. Dermatol. , vol.21 , pp. 311
    • Poh-Fitzpatrick, M.B.1
  • 10
    • 0023902682 scopus 로고
    • The liver and protoporphyria
    • J.R. Bloomer, The liver and protoporphyria, Hepatology 8 (1988) 402-407.
    • (1988) Hepatology , vol.8 , pp. 402-407
    • Bloomer, J.R.1
  • 12
    • 0028045062 scopus 로고
    • Species-specific changes in regulatory elements of mouse haptoglobin genes
    • S. Pajovic, V.E. Jones, K.R. Prowse, F.G. Berger, H. Baumann, Species-specific changes in regulatory elements of mouse haptoglobin genes, J. Biol. Chem. 269 (1994) 2215-2224.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2215-2224
    • Pajovic, S.1    Jones, V.E.2    Prowse, K.R.3    Berger, F.G.4    Baumann, H.5
  • 16
    • 0030036639 scopus 로고    scopus 로고
    • A novel mutation in the ferrochelatase gene associated with erythropoietic protoporphyria
    • S. Imoto, Y. Tanizawa, Y. Sato, K. Kaku, Y. Oka, A novel mutation in the ferrochelatase gene associated with erythropoietic protoporphyria, Br. J. Haematol. 94 (1996) 191-197.
    • (1996) Br. J. Haematol. , vol.94 , pp. 191-197
    • Imoto, S.1    Tanizawa, Y.2    Sato, Y.3    Kaku, K.4    Oka, Y.5
  • 19
    • 0028230273 scopus 로고
    • Molecular characterization of a ferrochelatase gene defect causing anomalous RNa splicing in erythropoietic protoporphyria
    • R.P. Sarkany, D.M. Whitcombe, T.M. Cox, Molecular characterization of a ferrochelatase gene defect causing anomalous RNA splicing in erythropoietic protoporphyria, J. Invest. Dermatol. 102 (1994) 481-484.
    • (1994) J. Invest. Dermatol. , vol.102 , pp. 481-484
    • Sarkany, R.P.1    Whitcombe, D.M.2    Cox, T.M.3
  • 20
    • 0027301851 scopus 로고
    • Human erythropoietic protoporphyria: Identification of a mutation at the splice donor site of intron 7 causing exon 7 skipping of the ferrochelatase gene
    • Y. Nakahashi, H. Miyazaki, Y. Kadota, Y. Naitoh, K. Inoue, M. Yamamoto, N. Hayashi, S. Taketani, Human erythropoietic protoporphyria: identification of a mutation at the splice donor site of intron 7 causing exon 7 skipping of the ferrochelatase gene, Hum. Mol. Genet. 2 (1993) 1069-1070.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 1069-1070
    • Nakahashi, Y.1    Miyazaki, H.2    Kadota, Y.3    Naitoh, Y.4    Inoue, K.5    Yamamoto, M.6    Hayashi, N.7    Taketani, S.8
  • 22
    • 0027952902 scopus 로고
    • Screening for ferrochelatase mutations: Molecular heterogeneity of erythropoietic protoporphyria
    • X. Wang, M. Poh-Fitzpatrick, S. Tekaetani, T. Chen, S. Piomelli, Screening for ferrochelatase mutations: molecular heterogeneity of erythropoietic protoporphyria, Biochim. Biophys. Acta 1225 (1994) 187-190.
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 187-190
    • Wang, X.1    Poh-Fitzpatrick, M.2    Tekaetani, S.3    Chen, T.4    Piomelli, S.5
  • 23
    • 0021615176 scopus 로고
    • Genetic aspects of erythropoietic protoporphyria
    • L.N. Went, E.C. Klasen, Genetic aspects of erythropoietic protoporphyria, Ann. Hum. Genet. 48 (1984) 105-117.
    • (1984) Ann. Hum. Genet. , vol.48 , pp. 105-117
    • Went, L.N.1    Klasen, E.C.2
  • 25
    • 0028290552 scopus 로고
    • Recessive inheritance of erythropoietic protoporphyria with liver failure
    • R.P. Sarkany, G.J. Alexander, T.M. Cox, Recessive inheritance of erythropoietic protoporphyria with liver failure, Lancet 343 (1994) 1394-1396.
    • (1994) Lancet , vol.343 , pp. 1394-1396
    • Sarkany, R.P.1    Alexander, G.J.2    Cox, T.M.3
  • 26
    • 0028244645 scopus 로고
    • Recessive inheritance of erythropoietic protoporphyria with liver failure
    • X. Schneider-Yin, S. Taketani, B. Schafer, E.I. Minder, Recessive inheritance of erythropoietic protoporphyria with liver failure, Lancet 344 (1994) 337.
    • (1994) Lancet , vol.344 , pp. 337
    • Schneider-Yin, X.1    Taketani, S.2    Schafer, B.3    Minder, E.I.4
  • 27
    • 0026340594 scopus 로고
    • The functional size of ferrochelatase determined in situ by radiation inactivation
    • J.G. Straka, J.R. Bloomer, E.S. Kempner, The functional size of ferrochelatase determined in situ by radiation inactivation, J. Biol. Chem. 266 (1991) 24637-24641.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24637-24641
    • Straka, J.G.1    Bloomer, J.R.2    Kempner, E.S.3
  • 29
    • 0017707460 scopus 로고
    • Bovine protoporphyria : The first non-human model of this hereditary photosensitizing disease
    • G.R. Ruth, S. Schwartz, B. Stephenson, Bovine protoporphyria : The first non-human model of this hereditary photosensitizing disease, Science 198 (1977) 199-201.
    • (1977) Science , vol.198 , pp. 199-201
    • Ruth, G.R.1    Schwartz, S.2    Stephenson, B.3
  • 30
    • 0020044045 scopus 로고
    • Bovine protoporphyria: Documentation of autosomal recessive inheritance and comparison with the human disease through measurement of heme synthase activity
    • J.R. Bloomer, K.O. Morton, R.J. Reuter, G.R. Ruth, Bovine protoporphyria: Documentation of autosomal recessive inheritance and comparison with the human disease through measurement of heme synthase activity, Am. J. Hum. Genet. 34 (1982) 322-330.
    • (1982) Am. J. Hum. Genet. , vol.34 , pp. 322-330
    • Bloomer, J.R.1    Morton, K.O.2    Reuter, R.J.3    Ruth, G.R.4
  • 34
    • 0032525082 scopus 로고    scopus 로고
    • Examination of ferrochelatase mutations that cause erythropoietic protoporphyria
    • V.M. Sellers, T.A. Dailey, H.A. Dailey, Examination of ferrochelatase mutations that cause erythropoietic protoporphyria, Blood 91 (1998) 3980-3985.
    • (1998) Blood , vol.91 , pp. 3980-3985
    • Sellers, V.M.1    Dailey, T.A.2    Dailey, H.A.3
  • 35
    • 0029970569 scopus 로고    scopus 로고
    • Function of the [2Fe-2S] cluster in mammalian ferrochelatase: A possible role as a nitric oxide sensor
    • V.M. Sellers, M.K. Johnson, H.A. Dailey, Function of the [2Fe-2S] cluster in mammalian ferrochelatase: a possible role as a nitric oxide sensor, Biochemistry 35 (1996) 2699-2704.
    • (1996) Biochemistry , vol.35 , pp. 2699-2704
    • Sellers, V.M.1    Johnson, M.K.2    Dailey, H.A.3
  • 39
    • 0028838353 scopus 로고
    • Ferrochelatase cDNA delivered by adenoviral vector corrects biochemical deficiency in protoporphyric cells
    • S.T. Magness, D.A. Brenner, Ferrochelatase cDNA delivered by adenoviral vector corrects biochemical deficiency in protoporphyric cells, Hum. Gene Ther. 6 (1995) 1285-1290.
    • (1995) Hum. Gene Ther. , vol.6 , pp. 1285-1290
    • Magness, S.T.1    Brenner, D.A.2
  • 40
    • 0017753876 scopus 로고
    • Study of factors causing excess protoporphyrin accumulation in cultured skin fibroblasts from patients with protoporphyria
    • J.R. Bloomer, D.A. Brenner, M.J. Mahoney, Study of factors causing excess protoporphyrin accumulation in cultured skin fibroblasts from patients with protoporphyria, J. Clin. Invest. 60 (1977) 1354-1361.
    • (1977) J. Clin. Invest. , vol.60 , pp. 1354-1361
    • Bloomer, J.R.1    Brenner, D.A.2    Mahoney, M.J.3
  • 41
    • 0025847853 scopus 로고
    • High-performance liquid chromatographic assays for protoporphyrinogen oxidase and ferrochelatase in human leukocytes
    • R. Guo, C.K. Lim, T.J. Peters, High-performance liquid chromatographic assays for protoporphyrinogen oxidase and ferrochelatase in human leukocytes, J. Chromatogr. 566 (1991) 383-396.
    • (1991) J. Chromatogr. , vol.566 , pp. 383-396
    • Guo, R.1    Lim, C.K.2    Peters, T.J.3
  • 42
    • 0023614235 scopus 로고
    • An HPLC assay for rat liver ferrochelatase activity
    • F.M. Li, C.K. Lim, T.J. Peters, An HPLC assay for rat liver ferrochelatase activity, Biomed. Chromatogr. 2 (1987) 164-168.
    • (1987) Biomed. Chromatogr. , vol.2 , pp. 164-168
    • Li, F.M.1    Lim, C.K.2    Peters, T.J.3
  • 43
    • 0029972527 scopus 로고    scopus 로고
    • Ferrochelatase activities in patients with erythropoietic protoporphyria and their families
    • G. Goerz, S. Bunselmeyer, K. Bolsen, N.Y. Schurer, Ferrochelatase activities in patients with erythropoietic protoporphyria and their families, Br. J. Dermatol. 134 (1996) 880-885.
    • (1996) Br. J. Dermatol. , vol.134 , pp. 880-885
    • Goerz, G.1    Bunselmeyer, S.2    Bolsen, K.3    Schurer, N.Y.4
  • 45
    • 0028149374 scopus 로고
    • Erythropoietic protoporphyria
    • D.J. Todd, Erythropoietic protoporphyria, Br. J. Dermatol. 131 (1994) 751-766.
    • (1994) Br. J. Dermatol. , vol.131 , pp. 751-766
    • Todd, D.J.1
  • 47
    • 0028928182 scopus 로고
    • The molecular basis of HEXA mRNA deficiency caused by the most common Tay-Sachs disease mutation
    • D.J. Boles, R.L. Proia, The molecular basis of HEXA mRNA deficiency caused by the most common Tay-Sachs disease mutation, Am. J. Hum. Genet. 56 (1995) 716-724.
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 716-724
    • Boles, D.J.1    Proia, R.L.2
  • 48
    • 0032128422 scopus 로고    scopus 로고
    • Molecular defects in ferrochelatase in patients with protoporphyria requiring liver transplantation
    • J. Bloomer, C. Bruzzone, L. Zhu, Y. Scarlett, S. Magness, D. Brenner, Molecular defects in ferrochelatase in patients with protoporphyria requiring liver transplantation, J. Clin. Invest. 102 (1998) 107-114.
    • (1998) J. Clin. Invest. , vol.102 , pp. 107-114
    • Bloomer, J.1    Bruzzone, C.2    Zhu, L.3    Scarlett, Y.4    Magness, S.5    Brenner, D.6
  • 49
    • 0031459894 scopus 로고    scopus 로고
    • Methylation of the minimal promoter of an embryonic globin gene silences transcription in primary erythroid cells
    • R. Singal, R. Ferris, J.A. Little, S.Z. Wang, G.D. Ginder, Methylation of the minimal promoter of an embryonic globin gene silences transcription in primary erythroid cells, Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 13724-13729.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13724-13729
    • Singal, R.1    Ferris, R.2    Little, J.A.3    Wang, S.Z.4    Ginder, G.D.5
  • 50
    • 0032485196 scopus 로고    scopus 로고
    • CpG methylation within the 5′ regulatory region of the BRCA1 gene is tumor specific and includes a putative CREB binding site
    • D.N. Mancini, D.I. Rodenhiser, P.J. Ainsworth, F.P. O'Malley, S.M. Singh, W. Xing, T.K. Archer, CpG methylation within the 5′ regulatory region of the BRCA1 gene is tumor specific and includes a putative CREB binding site, Oncogene 16 (1998) 1161-1169.
    • (1998) Oncogene , vol.16 , pp. 1161-1169
    • Mancini, D.N.1    Rodenhiser, D.I.2    Ainsworth, P.J.3    O'Malley, F.P.4    Singh, S.M.5    Xing, W.6    Archer, T.K.7
  • 51
    • 0030879709 scopus 로고    scopus 로고
    • 6-methylguanine DNA methyltransferase gene is associated with the loss of nucleosome-like positioning
    • 6-methylguanine DNA methyltransferase gene is associated with the loss of nucleosome-like positioning, Mol. Cell. Biol. 17 (1997) 5813-5822.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5813-5822
    • Patel, S.A.1    Graunke, D.M.2    Pieper, R.O.3
  • 52
    • 0031577559 scopus 로고    scopus 로고
    • Targeted disruption of exon 52 in the mouse dystrophin gene induced muscle degeneration similar to that observed in Duchenne muscular dystrophy
    • E. Araki, K. Nakamura, K. Nakao, S. Kameya, O. Kobayashi, I. Nonaka, T. Kobayashi, M. Katsuki, Targeted disruption of exon 52 in the mouse dystrophin gene induced muscle degeneration similar to that observed in Duchenne muscular dystrophy, Biochem. Biophys. Res. Commun. 238 (1997) 492-497.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 492-497
    • Araki, E.1    Nakamura, K.2    Nakao, K.3    Kameya, S.4    Kobayashi, O.5    Nonaka, I.6    Kobayashi, T.7    Katsuki, M.8


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