메뉴 건너뛰기




Volumn 78, Issue 4, 2003, Pages 250-258

Expression of short-chain acyl-CoA dehydrogenase (SCAD) proteins in the liver of SCAD deficient mice after hydrodynamic gene transfer

Author keywords

Butyrylcarnitine; EMA; In vivo characterization; Non viral gene transfer; SCAD deficiency; Tail vein injection; Oxidation

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; CARNITINE DERIVATIVE; COMPLEMENTARY DNA; NAKED DNA; UBIQUITIN;

EID: 0037389776     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1096-7192(03)00038-6     Document Type: Article
Times cited : (19)

References (30)
  • 1
    • 0000576457 scopus 로고
    • Mitochondrial fatty acid oxidation disorders
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, & D. Valle. New York: McGraw-Hill
    • Roe C.R., Coates P.M. Mitochondrial fatty acid oxidation disorders. Scriver C.R., Beaudet A.L., Sly W.S., Valle D. The Metabolic and Molecular Bases of Inherited Disease. 1995;1501-1533 McGraw-Hill, New York.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 1501-1533
    • Roe, C.R.1    Coates, P.M.2
  • 2
    • 0001464908 scopus 로고
    • Acyl-CoA dehydrogenases
    • Beinert H. Acyl-CoA dehydrogenases. Enzymes. 7:1963;447-476.
    • (1963) Enzymes , vol.7 , pp. 447-476
    • Beinert, H.1
  • 3
    • 0029416813 scopus 로고
    • β-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress
    • Kunau W.H., Dommes V., Schulz H. β-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress. Prog. Lipid Res. 34:1995;267-342.
    • (1995) Prog. Lipid Res. , vol.34 , pp. 267-342
    • Kunau, W.H.1    Dommes, V.2    Schulz, H.3
  • 4
  • 6
    • 0023875592 scopus 로고
    • Genetic deficiency of short-chain acyl-coenzyme A dehydrogenase in cultured fibroblasts from a patient with muscle carnitine deficiency and severe skeletal muscle weakness
    • Coates P.M., Hale D.E., Finocchiaro G., Tanaka K., Winter S.C. Genetic deficiency of short-chain acyl-coenzyme A dehydrogenase in cultured fibroblasts from a patient with muscle carnitine deficiency and severe skeletal muscle weakness. J. Clin. Invest. 81:1988;171-175.
    • (1988) J. Clin. Invest. , vol.81 , pp. 171-175
    • Coates, P.M.1    Hale, D.E.2    Finocchiaro, G.3    Tanaka, K.4    Winter, S.C.5
  • 7
    • 0025325156 scopus 로고
    • Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency
    • Naito E., Indo Y., Tanaka K. Identification of two variant short chain acyl-coenzyme A dehydrogenase alleles, each containing a different point mutation in a patient with short chain acyl-coenzyme A dehydrogenase deficiency. J. Clin. Invest. 85:1990;1575-1582.
    • (1990) J. Clin. Invest. , vol.85 , pp. 1575-1582
    • Naito, E.1    Indo, Y.2    Tanaka, K.3
  • 12
    • 0033166561 scopus 로고    scopus 로고
    • High levels of foreign gene expression in hepatocytes after tail vein injections of naked plasmid DNA
    • Zhang G., Budker V., Wolff J.A. High levels of foreign gene expression in hepatocytes after tail vein injections of naked plasmid DNA. Hum. Gene. Ther. 10:1999;1735-1737.
    • (1999) Hum. Gene. Ther. , vol.10 , pp. 1735-1737
    • Zhang, G.1    Budker, V.2    Wolff, J.A.3
  • 13
    • 0032805251 scopus 로고    scopus 로고
    • Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA
    • Liu F., Song Y., Liu D. Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA. Gene. Ther. 6:1999;1258-1266.
    • (1999) Gene. Ther. , vol.6 , pp. 1258-1266
    • Liu, F.1    Song, Y.2    Liu, D.3
  • 15
    • 0036460628 scopus 로고    scopus 로고
    • Physiological effects of human growth hormone produced after hydrodynamic gene transfer of a plasmid vector containing the human ubiquitin promotor
    • Dagnaes-Hansen F., Holst H.U., Sondergaard M., Vorup-Jensen T., Flyvbjerg A., Jensen U.B., Jensen T.G. Physiological effects of human growth hormone produced after hydrodynamic gene transfer of a plasmid vector containing the human ubiquitin promotor. J. Mol. Med. 80:2002;665-670.
    • (2002) J. Mol. Med. , vol.80 , pp. 665-670
    • Dagnaes-Hansen, F.1    Holst, H.U.2    Sondergaard, M.3    Vorup-Jensen, T.4    Flyvbjerg, A.5    Jensen, U.B.6    Jensen, T.G.7
  • 16
    • 0034950612 scopus 로고    scopus 로고
    • Long-term and therapeutic-level hepatic gene expression of human factor IX after naked plasmid transfer in vivo
    • Miao C.H., Thompson A.R., Loeb K., Ye X. Long-term and therapeutic-level hepatic gene expression of human factor IX after naked plasmid transfer in vivo. Mol. Ther. 3:2001;947-957.
    • (2001) Mol. Ther. , vol.3 , pp. 947-957
    • Miao, C.H.1    Thompson, A.R.2    Loeb, K.3    Ye, X.4
  • 19
    • 0027285713 scopus 로고
    • Null allele at Bcd-1 locus in BALB/cByJ mice is due to a deletion in the short-chain acyl-CoA dehydrogenase gene and results in missplicing of mRNA
    • Hinsdale M.E., Kelly C.L., Wood P.A. Null allele at Bcd-1 locus in BALB/cByJ mice is due to a deletion in the short-chain acyl-CoA dehydrogenase gene and results in missplicing of mRNA. Genomics. 16:1993;605-611.
    • (1993) Genomics , vol.16 , pp. 605-611
    • Hinsdale, M.E.1    Kelly, C.L.2    Wood, P.A.3
  • 20
    • 0032557512 scopus 로고    scopus 로고
    • Rapid degradation of short-chain acyl-CoA dehydrogenase (SCAD) with temperature-sensitive folding defects occurs after import into mitochondria
    • Corydon T.J., Bross P., Jensen T.G., Corydon M.J., Lund T.B., Jensen U.B., Kim J.P., Gregersen N., Bolund L. Rapid degradation of short-chain acyl-CoA dehydrogenase (SCAD) with temperature-sensitive folding defects occurs after import into mitochondria. J. Biol. Chem. 273:1998;13065-13071.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13065-13071
    • Corydon, T.J.1    Bross, P.2    Jensen, T.G.3    Corydon, M.J.4    Lund, T.B.5    Jensen, U.B.6    Kim, J.P.7    Gregersen, N.8    Bolund, L.9
  • 21
    • 0035227198 scopus 로고    scopus 로고
    • Isolation and subfractionation of mitochondria from animal cells and tissue culture lines
    • New York: Academic Press
    • Pallotti F., Lenaz G. Isolation and subfractionation of mitochondria from animal cells and tissue culture lines. Methods Cell Biology. 2001;1-31 Academic Press, New York.
    • (2001) Methods Cell Biology , pp. 1-31
    • Pallotti, F.1    Lenaz, G.2
  • 22
    • 0036667911 scopus 로고    scopus 로고
    • Sensitivity and accuracy of quantitative real-time polymerase chain reaction using SYBR green I depends on cDNA synthesis conditions
    • Lekanne Deprez R.H., Fijnvandraat A.C., Ruijter J.M., Moorman A.F. Sensitivity and accuracy of quantitative real-time polymerase chain reaction using SYBR green I depends on cDNA synthesis conditions. Anal. Biochem. 307:2002;63-69.
    • (2002) Anal. Biochem. , vol.307 , pp. 63-69
    • Lekanne Deprez, R.H.1    Fijnvandraat, A.C.2    Ruijter, J.M.3    Moorman, A.F.4
  • 23
    • 0033858353 scopus 로고    scopus 로고
    • The biochemical metabolite screen in the Munich ENU Mouse Mutagenesis Project: Determination of amino acids and acylcarnitines by tandem mass spectrometry
    • Rolinski B., Arnecke R., Dame T., Kreischer J., Olgemoller B., Wolf E., Balling R., Hrabe de Angelis M., Roscher A.A. The biochemical metabolite screen in the Munich ENU Mouse Mutagenesis Project: determination of amino acids and acylcarnitines by tandem mass spectrometry. Mamm. Genome. 11:2000;547-551.
    • (2000) Mamm. Genome , vol.11 , pp. 547-551
    • Rolinski, B.1    Arnecke, R.2    Dame, T.3    Kreischer, J.4    Olgemoller, B.5    Wolf, E.6    Balling, R.7    Hrabe de Angelis, M.8    Roscher, A.A.9
  • 24
    • 0032805251 scopus 로고    scopus 로고
    • Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA
    • Liu F., Song Y., Liu D. Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA. Gene Ther. 6:1999;1258-1266.
    • (1999) Gene Ther. , vol.6 , pp. 1258-1266
    • Liu, F.1    Song, Y.2    Liu, D.3
  • 25
    • 0029147089 scopus 로고
    • Green fluorescent protein as a reporter of gene expression and protein localization
    • Kain S.R., Adams M., Kondepudi A., Yang T.T., Ward W.W., Kitts P. Green fluorescent protein as a reporter of gene expression and protein localization. Biotechniques. 19:1995;650-655.
    • (1995) Biotechniques , vol.19 , pp. 650-655
    • Kain, S.R.1    Adams, M.2    Kondepudi, A.3    Yang, T.T.4    Ward, W.W.5    Kitts, P.6
  • 27
    • 0021970335 scopus 로고
    • Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme
    • Ikeda Y., Okamura-Ikeda K., Tanaka K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260:1985;1311-1325.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1311-1325
    • Ikeda, Y.1    Okamura-Ikeda, K.2    Tanaka, K.3
  • 28
    • 0028569536 scopus 로고
    • Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family
    • Rozen R., Vockley J., Zhou L., Milos R., Willard J., Fu K., Vicanek C., Low-Nang L., Torban E., Fournier B. Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family. Genomics. 24:1994;280-287.
    • (1994) Genomics , vol.24 , pp. 280-287
    • Rozen, R.1    Vockley, J.2    Zhou, L.3    Milos, R.4    Willard, J.5    Fu, K.6    Vicanek, C.7    Low-Nang, L.8    Torban, E.9    Fournier, B.10
  • 29
    • 0034866130 scopus 로고    scopus 로고
    • Mutation analysis in mitochondrial fatty acid oxidation defects: Exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship
    • Gregersen N., Andresen B.S., Corydon M.J., Corydon T.J., Olsen R.K., Bolund L., Bross P. Mutation analysis in mitochondrial fatty acid oxidation defects: exemplified by acyl-CoA dehydrogenase deficiencies, with special focus on genotype-phenotype relationship. Hum. Mutat. 18:2001;169-189.
    • (2001) Hum. Mutat. , vol.18 , pp. 169-189
    • Gregersen, N.1    Andresen, B.S.2    Corydon, M.J.3    Corydon, T.J.4    Olsen, R.K.5    Bolund, L.6    Bross, P.7
  • 30
    • 0012999844 scopus 로고    scopus 로고
    • Recombinant adeno-associated virus vectors for gene therapy of disorders of fatty acid oxidation
    • Conlon T.J., Matern D., Walter G., Vockley G., Terence F. Recombinant adeno-associated virus vectors for gene therapy of disorders of fatty acid oxidation. Mol. Ther. 5:2002;341.
    • (2002) Mol. Ther. , vol.5 , pp. 341
    • Conlon, T.J.1    Matern, D.2    Walter, G.3    Vockley, G.4    Terence, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.