메뉴 건너뛰기




Volumn 1822, Issue 9, 2012, Pages 1387-1396

Peroxisomal ABC transporters: Structure, function and role in disease

Author keywords

ABC transporter; Acyl CoA transport; Adrenoleukodystrophy; Fatty acid oxidation; Peroxisome targeting

Indexed keywords

ABC TRANSPORTER; ABCD1 PROTEIN; ABCD2 PROTEIN; ABCD3 PROTEIN; DOCOSAHEXAENOIC ACID; FATTY ACID; MYELIN; PEROXIN 19; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; POLYUNSATURATED FATTY ACID; RETINOID X RECEPTOR; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; THYROID HORMONE RECEPTOR; UNCLASSIFIED DRUG; VERY LONG CHAIN FATTY ACID;

EID: 84864052256     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2012.02.009     Document Type: Review
Times cited : (144)

References (113)
  • 1
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders R.J., Waterham H.R. Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 2006, 75:295-332.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 295-332
    • Wanders, R.J.1    Waterham, H.R.2
  • 2
    • 77956867734 scopus 로고    scopus 로고
    • Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism
    • Van Veldhoven P.P. Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism. J. Lipid Res. 2010, 51:2863-2895.
    • (2010) J. Lipid Res. , vol.51 , pp. 2863-2895
    • Van Veldhoven, P.P.1
  • 3
    • 77953715734 scopus 로고    scopus 로고
    • Be different-the diversity of peroxisomes in the animal kingdom
    • Islinger M., Cardoso M.J., Schrader M. Be different-the diversity of peroxisomes in the animal kingdom. Biochim. Biophys. Acta 2010, 1803:881-897.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 881-897
    • Islinger, M.1    Cardoso, M.J.2    Schrader, M.3
  • 5
    • 0026621245 scopus 로고
    • ABC transporters: from microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 1992, 8:67-113.
    • (1992) Annu. Rev. Cell Biol. , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 6
    • 0032951188 scopus 로고    scopus 로고
    • Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters
    • Saurin W., Hofnung M., Dassa E. Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters. J. Mol. Evol. 1999, 48:22-41.
    • (1999) J. Mol. Evol. , vol.48 , pp. 22-41
    • Saurin, W.1    Hofnung, M.2    Dassa, E.3
  • 7
    • 0035014565 scopus 로고    scopus 로고
    • The ABC of ABCS: a phylogenetic and functional classification of ABC systems in living organisms
    • Dassa E., Bouige P. The ABC of ABCS: a phylogenetic and functional classification of ABC systems in living organisms. Res. Microbiol. 2001, 152:211-229.
    • (2001) Res. Microbiol. , vol.152 , pp. 211-229
    • Dassa, E.1    Bouige, P.2
  • 8
    • 65549121495 scopus 로고    scopus 로고
    • Human ATP-binding cassette (ABC) transporter family
    • Vasiliou V., Vasiliou K., Nebert D.W. Human ATP-binding cassette (ABC) transporter family. Hum. Genomics 2009, 3:281-290.
    • (2009) Hum. Genomics , vol.3 , pp. 281-290
    • Vasiliou, V.1    Vasiliou, K.2    Nebert, D.W.3
  • 10
    • 0030034602 scopus 로고    scopus 로고
    • A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern
    • Lombard-Platet G., Savary S., Sarde C.O., Mandel J.L., Chimini G. A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:1265-1269.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1265-1269
    • Lombard-Platet, G.1    Savary, S.2    Sarde, C.O.3    Mandel, J.L.4    Chimini, G.5
  • 11
    • 0031561433 scopus 로고    scopus 로고
    • CDNA cloning and mRNA expression of the human adrenoleukodystrophy related protein (ALDRP), a peroxisomal ABC transporter
    • Holzinger A., Kammerer S., Berger J., Roscher A.A. cDNA cloning and mRNA expression of the human adrenoleukodystrophy related protein (ALDRP), a peroxisomal ABC transporter. Biochem. Biophys. Res. Commun. 1997, 239:261-264.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 261-264
    • Holzinger, A.1    Kammerer, S.2    Berger, J.3    Roscher, A.A.4
  • 12
    • 0026849933 scopus 로고
    • Mutations in the 70K peroxisomal membrane protein gene in Zellweger syndrome
    • Gartner J., Moser H., Valle D. Mutations in the 70K peroxisomal membrane protein gene in Zellweger syndrome. Nat. Genet. 1992, 1:16-23.
    • (1992) Nat. Genet. , vol.1 , pp. 16-23
    • Gartner, J.1    Moser, H.2    Valle, D.3
  • 13
    • 0026500670 scopus 로고
    • Nucleotide sequence of the human 70kDa peroxisomal membrane protein: a member of ATP-binding cassette transporters
    • Kamijo K., Kamijo T., Ueno I., Osumi T., Hashimoto T. Nucleotide sequence of the human 70kDa peroxisomal membrane protein: a member of ATP-binding cassette transporters. Biochim. Biophys. Acta 1992, 1129:323-327.
    • (1992) Biochim. Biophys. Acta , vol.1129 , pp. 323-327
    • Kamijo, K.1    Kamijo, T.2    Ueno, I.3    Osumi, T.4    Hashimoto, T.5
  • 14
    • 0025255475 scopus 로고
    • The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily
    • Kamijo K., Taketani S., Yokota S., Osumi T., Hashimoto T. The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-glycoprotein)-related ATP-binding protein superfamily. J. Biol. Chem. 1990, 265:4534-4540.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4534-4540
    • Kamijo, K.1    Taketani, S.2    Yokota, S.3    Osumi, T.4    Hashimoto, T.5
  • 15
    • 0032924991 scopus 로고    scopus 로고
    • Adrenoleukodystrophy-related protein can compensate functionally for adrenoleukodystrophy protein deficiency (X-ALD): implications for therapy
    • Netik A., Forss-Petter S., Holzinger A., Molzer B., Unterrainer G., Berger J. Adrenoleukodystrophy-related protein can compensate functionally for adrenoleukodystrophy protein deficiency (X-ALD): implications for therapy. Hum. Mol. Genet. 1999, 8:907-913.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 907-913
    • Netik, A.1    Forss-Petter, S.2    Holzinger, A.3    Molzer, B.4    Unterrainer, G.5    Berger, J.6
  • 17
    • 0031559581 scopus 로고    scopus 로고
    • Primary structure of human PMP69, a putative peroxisomal ABC-transporter
    • Holzinger A., Kammerer S., Roscher A.A. Primary structure of human PMP69, a putative peroxisomal ABC-transporter. Biochem. Biophys. Res. Commun. 1997, 237:152-157.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , pp. 152-157
    • Holzinger, A.1    Kammerer, S.2    Roscher, A.A.3
  • 18
    • 0030776037 scopus 로고    scopus 로고
    • Identification of a fourth half ABC transporter in the human peroxisomal membrane
    • Shani N., Jimenez-Sanchez G., Steel G., Dean M., Valle D. Identification of a fourth half ABC transporter in the human peroxisomal membrane. Hum. Mol. Genet. 1997, 6:1925-1931.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1925-1931
    • Shani, N.1    Jimenez-Sanchez, G.2    Steel, G.3    Dean, M.4    Valle, D.5
  • 20
    • 79957737791 scopus 로고    scopus 로고
    • Mammalian peroxisomal ABC transporters: from endogenous substrates to pathology and clinical significance
    • Kemp S., Theodoulou F.L., Wanders R.J. Mammalian peroxisomal ABC transporters: from endogenous substrates to pathology and clinical significance. Br. J. Pharmacol. 2011, 164:1753-1766.
    • (2011) Br. J. Pharmacol. , vol.164 , pp. 1753-1766
    • Kemp, S.1    Theodoulou, F.L.2    Wanders, R.J.3
  • 22
    • 0035831176 scopus 로고    scopus 로고
    • Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters
    • Roerig P., Mayerhofer P., Holzinger A., Gartner J. Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters. FEBS Lett. 2001, 492:66-72.
    • (2001) FEBS Lett. , vol.492 , pp. 66-72
    • Roerig, P.1    Mayerhofer, P.2    Holzinger, A.3    Gartner, J.4
  • 23
    • 0037131279 scopus 로고    scopus 로고
    • ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1)
    • Tanaka A.R., Tanabe K., Morita M., Kurisu M., Kasiwayama Y., Matsuo M., Kioka N., Amachi T., Imanaka T., Ueda K. ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1). J. Biol. Chem. 2002, 277:40142-40147.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40142-40147
    • Tanaka, A.R.1    Tanabe, K.2    Morita, M.3    Kurisu, M.4    Kasiwayama, Y.5    Matsuo, M.6    Kioka, N.7    Amachi, T.8    Imanaka, T.9    Ueda, K.10
  • 24
    • 0036291180 scopus 로고    scopus 로고
    • Nucleotide-induced conformational changes of PMP70, an ATP binding cassette transporter on rat liver peroxisomal membranes
    • Kashiwayama Y., Morita M., Kamijo K., Imanaka T. Nucleotide-induced conformational changes of PMP70, an ATP binding cassette transporter on rat liver peroxisomal membranes. Biochem. Biophys. Res. Commun. 2002, 291:1245-1251.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 1245-1251
    • Kashiwayama, Y.1    Morita, M.2    Kamijo, K.3    Imanaka, T.4
  • 25
    • 15944408418 scopus 로고    scopus 로고
    • Probing substrate-induced conformational alterations in adrenoleukodystrophy protein by proteolysis
    • Guimaraes C.P., Sa-Miranda C., Azevedo J.E. Probing substrate-induced conformational alterations in adrenoleukodystrophy protein by proteolysis. J. Hum. Genet. 2005, 50:99-105.
    • (2005) J. Hum. Genet. , vol.50 , pp. 99-105
    • Guimaraes, C.P.1    Sa-Miranda, C.2    Azevedo, J.E.3
  • 28
    • 34848912009 scopus 로고    scopus 로고
    • Live cell FRET microscopy: homo- and heterodimerization of two human peroxisomal ABC transporters, the adrenoleukodystrophy protein (ALDP, ABCD1) and PMP70 (ABCD3)
    • Hillebrand M., Verrier S.E., Ohlenbusch A., Schafer A., Soling H.D., Wouters F.S., Gartner J. Live cell FRET microscopy: homo- and heterodimerization of two human peroxisomal ABC transporters, the adrenoleukodystrophy protein (ALDP, ABCD1) and PMP70 (ABCD3). J. Biol. Chem. 2007, 282:26997-27005.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26997-27005
    • Hillebrand, M.1    Verrier, S.E.2    Ohlenbusch, A.3    Schafer, A.4    Soling, H.D.5    Wouters, F.S.6    Gartner, J.7
  • 30
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson R.J., Locher K.P. Structure of a bacterial multidrug ABC transporter. Nature 2006, 443:180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 31
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: alternating access with a twist
    • Ward A., Reyes C.L., Yu J., Roth C.B., Chang G. Flexibility in the ABC transporter MsbA: alternating access with a twist. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:19005-19010.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 32
    • 33646791462 scopus 로고    scopus 로고
    • The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER
    • Kim P.K., Mullen R.T., Schumann U., Lippincott-Schwartz J. The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER. J. Cell Biol. 2006, 173:521-532.
    • (2006) J. Cell Biol. , vol.173 , pp. 521-532
    • Kim, P.K.1    Mullen, R.T.2    Schumann, U.3    Lippincott-Schwartz, J.4
  • 33
    • 59449104113 scopus 로고    scopus 로고
    • The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway
    • Matsuzaki T., Fujiki Y. The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway. J. Cell Biol. 2008, 183:1275-1286.
    • (2008) J. Cell Biol. , vol.183 , pp. 1275-1286
    • Matsuzaki, T.1    Fujiki, Y.2
  • 35
    • 77953507085 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins insert into the endoplasmic reticulum
    • van der Zand A., Braakman I., Tabak H.F. Peroxisomal membrane proteins insert into the endoplasmic reticulum. Mol. Biol. Cell 2010, 21:2057-2065.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2057-2065
    • van der Zand, A.1    Braakman, I.2    Tabak, H.F.3
  • 36
    • 79955505833 scopus 로고    scopus 로고
    • Peroxisome assembly: matrix and membrane protein biogenesis
    • Ma C., Agrawal G., Subramani S. Peroxisome assembly: matrix and membrane protein biogenesis. J. Cell Biol. 2011, 193:7-16.
    • (2011) J. Cell Biol. , vol.193 , pp. 7-16
    • Ma, C.1    Agrawal, G.2    Subramani, S.3
  • 37
    • 33845318535 scopus 로고    scopus 로고
    • Import of peroxisomal membrane proteins: the interplay of Pex3p- and Pex19p-mediated interactions
    • Fujiki Y., Matsuzono Y., Matsuzaki T., Fransen M. Import of peroxisomal membrane proteins: the interplay of Pex3p- and Pex19p-mediated interactions. Biochim. Biophys. Acta 2006, 1763:1639-1646.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1639-1646
    • Fujiki, Y.1    Matsuzono, Y.2    Matsuzaki, T.3    Fransen, M.4
  • 38
    • 4644250692 scopus 로고    scopus 로고
    • Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins
    • Shibata H., Kashiwayama Y., Imanaka T., Kato H. Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins. J. Biol. Chem. 2004, 279:38486-38494.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38486-38494
    • Shibata, H.1    Kashiwayama, Y.2    Imanaka, T.3    Kato, H.4
  • 40
    • 78650269198 scopus 로고    scopus 로고
    • Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p
    • Sato Y., Shibata H., Nakatsu T., Nakano H., Kashiwayama Y., Imanaka T., Kato H. Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p. EMBO J. 2010, 29:4083-4093.
    • (2010) EMBO J. , vol.29 , pp. 4083-4093
    • Sato, Y.1    Shibata, H.2    Nakatsu, T.3    Nakano, H.4    Kashiwayama, Y.5    Imanaka, T.6    Kato, H.7
  • 42
    • 0034817401 scopus 로고    scopus 로고
    • Targeting elements in the amino-terminal part direct the human 70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomes
    • Biermanns M., Gartner J. Targeting elements in the amino-terminal part direct the human 70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomes. Biochem. Biophys. Res. Commun. 2001, 285:649-655.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 649-655
    • Biermanns, M.1    Gartner, J.2
  • 43
    • 36348963175 scopus 로고    scopus 로고
    • Hydrophobic regions adjacent to transmembrane domains 1 and 5 are important for the targeting of the 70-kDa peroxisomal membrane protein
    • Kashiwayama Y., Asahina K., Morita M., Imanaka T. Hydrophobic regions adjacent to transmembrane domains 1 and 5 are important for the targeting of the 70-kDa peroxisomal membrane protein. J. Biol. Chem. 2007, 282:33831-33844.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33831-33844
    • Kashiwayama, Y.1    Asahina, K.2    Morita, M.3    Imanaka, T.4
  • 44
    • 0034611003 scopus 로고    scopus 로고
    • PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis
    • Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J. PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis. J. Cell Biol. 2000, 148:931-944.
    • (2000) J. Cell Biol. , vol.148 , pp. 931-944
    • Sacksteder, K.A.1    Jones, J.M.2    South, S.T.3    Li, X.4    Liu, Y.5    Gould, S.J.6
  • 45
    • 3042724871 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals
    • Rottensteiner H., Kramer A., Lorenzen S., Stein K., Landgraf C., Volkmer-Engert R., Erdmann R. Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Mol. Biol. Cell 2004, 15:3406-3417.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3406-3417
    • Rottensteiner, H.1    Kramer, A.2    Lorenzen, S.3    Stein, K.4    Landgraf, C.5    Volkmer-Engert, R.6    Erdmann, R.7
  • 46
    • 20444400829 scopus 로고    scopus 로고
    • Function of the PEX19-binding site of human adrenoleukodystrophy protein as targeting motif in man and yeast. PMP targeting is evolutionarily conserved
    • Halbach A., Lorenzen S., Landgraf C., Volkmer-Engert R., Erdmann R., Rottensteiner H. Function of the PEX19-binding site of human adrenoleukodystrophy protein as targeting motif in man and yeast. PMP targeting is evolutionarily conserved. J. Biol. Chem. 2005, 280:21176-21182.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21176-21182
    • Halbach, A.1    Lorenzen, S.2    Landgraf, C.3    Volkmer-Engert, R.4    Erdmann, R.5    Rottensteiner, H.6
  • 50
    • 78651253382 scopus 로고    scopus 로고
    • Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid β-oxidation
    • van Roermund C.W., Visser W.F., Ijlst L., Waterham H.R., Wanders R.J. Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid β-oxidation. Biochim. Biophys. Acta 2011, 1811:148-152.
    • (2011) Biochim. Biophys. Acta , vol.1811 , pp. 148-152
    • van Roermund, C.W.1    Visser, W.F.2    Ijlst, L.3    Waterham, H.R.4    Wanders, R.J.5
  • 52
    • 0037109002 scopus 로고    scopus 로고
    • Cholesterol regulates ABCD2 expression: implications for the therapy of X-linked adrenoleukodystrophy
    • Weinhofer I., Forss-Petter S., Zigman M., Berger J. Cholesterol regulates ABCD2 expression: implications for the therapy of X-linked adrenoleukodystrophy. Hum. Mol. Genet. 2002, 11:2701-2708.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2701-2708
    • Weinhofer, I.1    Forss-Petter, S.2    Zigman, M.3    Berger, J.4
  • 53
    • 26844531338 scopus 로고    scopus 로고
    • X-linked adrenoleukodystrophy mice demonstrate abnormalities in cholesterol metabolism
    • Weinhofer I., Forss-Petter S., Kunze M., Zigman M., Berger J. X-linked adrenoleukodystrophy mice demonstrate abnormalities in cholesterol metabolism. FEBS Lett. 2005, 579:5512-5516.
    • (2005) FEBS Lett. , vol.579 , pp. 5512-5516
    • Weinhofer, I.1    Forss-Petter, S.2    Kunze, M.3    Zigman, M.4    Berger, J.5
  • 55
    • 79957728343 scopus 로고    scopus 로고
    • Conservation of targeting but divergence in function and quality control of peroxisomal ABC transporters: an analysis using cross-kingdom expression
    • Zhang X., De Marcos Lousa C., Schutte-Lensink N., Ofman R., Wanders R.J., Baldwin S.A., Baker A., Kemp S., Theodoulou F.L. Conservation of targeting but divergence in function and quality control of peroxisomal ABC transporters: an analysis using cross-kingdom expression. Biochem. J. 2011, 436:547-557.
    • (2011) Biochem. J. , vol.436 , pp. 547-557
    • Zhang, X.1    De Marcos Lousa, C.2    Schutte-Lensink, N.3    Ofman, R.4    Wanders, R.J.5    Baldwin, S.A.6    Baker, A.7    Kemp, S.8    Theodoulou, F.L.9
  • 57
    • 79953142344 scopus 로고    scopus 로고
    • Substrate specificity overlap and interaction between adrenoleukodystrophy protein (ALDP/ABCD1) and adrenoleukodystrophy-related protein (ALDRP/ABCD2)
    • Genin E.C., Geillon F., Gondcaille C., Athias A., Gambert P., Trompier D., Savary S. Substrate specificity overlap and interaction between adrenoleukodystrophy protein (ALDP/ABCD1) and adrenoleukodystrophy-related protein (ALDRP/ABCD2). J. Biol. Chem. 2011, 286:8075-8084.
    • (2011) J. Biol. Chem. , vol.286 , pp. 8075-8084
    • Genin, E.C.1    Geillon, F.2    Gondcaille, C.3    Athias, A.4    Gambert, P.5    Trompier, D.6    Savary, S.7
  • 61
    • 29244469095 scopus 로고    scopus 로고
    • Liver X receptor α interferes with SREBP1c-mediated Abcd2 expression. Novel cross-talk in gene regulation
    • Weinhofer I., Kunze M., Rampler H., Bookout A.L., Forss-Petter S., Berger J. Liver X receptor α interferes with SREBP1c-mediated Abcd2 expression. Novel cross-talk in gene regulation. J. Biol. Chem. 2005, 280:41243-41251.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41243-41251
    • Weinhofer, I.1    Kunze, M.2    Rampler, H.3    Bookout, A.L.4    Forss-Petter, S.5    Berger, J.6
  • 63
    • 0031946259 scopus 로고    scopus 로고
    • Mirror expression of adrenoleukodystrophy and adrenoleukodystrophy related genes in mouse tissues and human cell lines
    • Troffer-Charlier N., Doerflinger N., Metzger E., Fouquet F., Mandel J.L., Aubourg P. Mirror expression of adrenoleukodystrophy and adrenoleukodystrophy related genes in mouse tissues and human cell lines. Eur. J. Cell Biol. 1998, 75:254-264.
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 254-264
    • Troffer-Charlier, N.1    Doerflinger, N.2    Metzger, E.3    Fouquet, F.4    Mandel, J.L.5    Aubourg, P.6
  • 65
    • 33646123772 scopus 로고    scopus 로고
    • Therapy of X-linked adrenoleukodystrophy
    • Moser H.W. Therapy of X-linked adrenoleukodystrophy. NeuroRx 2006, 3:246-253.
    • (2006) NeuroRx , vol.3 , pp. 246-253
    • Moser, H.W.1
  • 66
    • 77953228906 scopus 로고    scopus 로고
    • Biochemical aspects of X-linked adrenoleukodystrophy
    • Kemp S., Wanders R. Biochemical aspects of X-linked adrenoleukodystrophy. Brain Pathol. 2010, 20:831-837.
    • (2010) Brain Pathol. , vol.20 , pp. 831-837
    • Kemp, S.1    Wanders, R.2
  • 67
    • 79953326378 scopus 로고    scopus 로고
    • ABC subfamily D proteins and very long chain fatty acid metabolism as novel targets in adrenoleukodystrophy
    • Morita M., Shimozawa N., Kashiwayama Y., Suzuki Y., Imanaka T. ABC subfamily D proteins and very long chain fatty acid metabolism as novel targets in adrenoleukodystrophy. Curr. Drug Targets 2011, 12:694-706.
    • (2011) Curr. Drug Targets , vol.12 , pp. 694-706
    • Morita, M.1    Shimozawa, N.2    Kashiwayama, Y.3    Suzuki, Y.4    Imanaka, T.5
  • 68
    • 19744370528 scopus 로고    scopus 로고
    • Decreased expression of ABCD4 and BG1 genes early in the pathogenesis of X-linked adrenoleukodystrophy
    • Asheuer M., Bieche I., Laurendeau I., Moser A., Hainque B., Vidaud M., Aubourg P. Decreased expression of ABCD4 and BG1 genes early in the pathogenesis of X-linked adrenoleukodystrophy. Hum. Mol. Genet. 2005, 14:1293-1303.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1293-1303
    • Asheuer, M.1    Bieche, I.2    Laurendeau, I.3    Moser, A.4    Hainque, B.5    Vidaud, M.6    Aubourg, P.7
  • 70
    • 0030860131 scopus 로고    scopus 로고
    • Adrenoleukodystrophy: phenotype, genetics, pathogenesis and therapy
    • Moser H.W. Adrenoleukodystrophy: phenotype, genetics, pathogenesis and therapy. Brain 1997, 120(Pt. 8):1485-1508.
    • (1997) Brain , vol.120 , Issue.PART. 8 , pp. 1485-1508
    • Moser, H.W.1
  • 71
    • 77953523933 scopus 로고    scopus 로고
    • Very long-chain fatty acid accumulation causes lipotoxic response via 5-lipoxygenase in cerebral adrenoleukodystrophy
    • Khan M., Singh J., Gilg A.G., Uto T., Singh I. Very long-chain fatty acid accumulation causes lipotoxic response via 5-lipoxygenase in cerebral adrenoleukodystrophy. J. Lipid Res. 2010, 51:1685-1695.
    • (2010) J. Lipid Res. , vol.51 , pp. 1685-1695
    • Khan, M.1    Singh, J.2    Gilg, A.G.3    Uto, T.4    Singh, I.5
  • 72
    • 44849118490 scopus 로고    scopus 로고
    • Toxic effects of X-linked adrenoleukodystrophy-associated, very long chain fatty acids on glial cells and neurons from rat hippocampus in culture
    • Hein S., Schonfeld P., Kahlert S., Reiser G. Toxic effects of X-linked adrenoleukodystrophy-associated, very long chain fatty acids on glial cells and neurons from rat hippocampus in culture. Hum. Mol. Genet. 2008, 17:1750-1761.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1750-1761
    • Hein, S.1    Schonfeld, P.2    Kahlert, S.3    Reiser, G.4
  • 73
    • 0031042221 scopus 로고    scopus 로고
    • Effects of exogenous hexacosanoic acid on biochemical myelin composition in weaning and post-weaning rats
    • Di Biase A., Avellino C., Pieroni F., Quaresima T., Grisolia A., Cappa M., Salvati S. Effects of exogenous hexacosanoic acid on biochemical myelin composition in weaning and post-weaning rats. Neurochem. Res. 1997, 22:327-331.
    • (1997) Neurochem. Res. , vol.22 , pp. 327-331
    • Di Biase, A.1    Avellino, C.2    Pieroni, F.3    Quaresima, T.4    Grisolia, A.5    Cappa, M.6    Salvati, S.7
  • 74
    • 0034810289 scopus 로고    scopus 로고
    • Potential environmental and host participants in the early white matter lesion of adreno-leukodystrophy: morphologic evidence for CD8 cytotoxic T cells, cytolysis of oligodendrocytes, and CD1-mediated lipid antigen presentation
    • Ito M., Blumberg B.M., Mock D.J., Goodman A.D., Moser A.B., Moser H.W., Smith K.D., Powers J.M. Potential environmental and host participants in the early white matter lesion of adreno-leukodystrophy: morphologic evidence for CD8 cytotoxic T cells, cytolysis of oligodendrocytes, and CD1-mediated lipid antigen presentation. J. Neuropathol. Exp. Neurol. 2001, 60:1004-1019.
    • (2001) J. Neuropathol. Exp. Neurol. , vol.60 , pp. 1004-1019
    • Ito, M.1    Blumberg, B.M.2    Mock, D.J.3    Goodman, A.D.4    Moser, A.B.5    Moser, H.W.6    Smith, K.D.7    Powers, J.M.8
  • 79
    • 60149094802 scopus 로고    scopus 로고
    • Plasmalogens participate in very-long-chain fatty acid-induced pathology
    • Brites P., Mooyer P.A., El Mrabet L., Waterham H.R., Wanders R.J. Plasmalogens participate in very-long-chain fatty acid-induced pathology. Brain 2009, 132:482-492.
    • (2009) Brain , vol.132 , pp. 482-492
    • Brites, P.1    Mooyer, P.A.2    El Mrabet, L.3    Waterham, H.R.4    Wanders, R.J.5
  • 80
    • 48749084577 scopus 로고    scopus 로고
    • Plasmalogen deficiency in cerebral adrenoleukodystrophy and its modulation by lovastatin
    • Khan M., Singh J., Singh I. Plasmalogen deficiency in cerebral adrenoleukodystrophy and its modulation by lovastatin. J. Neurochem. 2008, 106:1766-1779.
    • (2008) J. Neurochem. , vol.106 , pp. 1766-1779
    • Khan, M.1    Singh, J.2    Singh, I.3
  • 81
    • 79951558626 scopus 로고    scopus 로고
    • Identification of novel SNPs of ABCD1, ABCD2, ABCD3, and ABCD4 genes in patients with X-linked adrenoleukodystrophy (ALD) based on comprehensive resequencing and association studies with ALD phenotypes
    • Matsukawa T., Asheuer M., Takahashi Y., Goto J., Suzuki Y., Shimozawa N., Takano H., Onodera O., Nishizawa M., Aubourg P., Tsuji S. Identification of novel SNPs of ABCD1, ABCD2, ABCD3, and ABCD4 genes in patients with X-linked adrenoleukodystrophy (ALD) based on comprehensive resequencing and association studies with ALD phenotypes. Neurogenetics 2011, 12:41-50.
    • (2011) Neurogenetics , vol.12 , pp. 41-50
    • Matsukawa, T.1    Asheuer, M.2    Takahashi, Y.3    Goto, J.4    Suzuki, Y.5    Shimozawa, N.6    Takano, H.7    Onodera, O.8    Nishizawa, M.9    Aubourg, P.10    Tsuji, S.11
  • 86
    • 43249126038 scopus 로고    scopus 로고
    • Oligodendroglial impact on axonal function and survival - a hypothesis
    • Kassmann C.M., Nave K.A. Oligodendroglial impact on axonal function and survival - a hypothesis. Curr. Opin. Neurol. 2008, 21:235-241.
    • (2008) Curr. Opin. Neurol. , vol.21 , pp. 235-241
    • Kassmann, C.M.1    Nave, K.A.2
  • 87
    • 68949151976 scopus 로고    scopus 로고
    • Peroxisomes, myelination, and axonal integrity in the CNS
    • Baes M., Aubourg P. Peroxisomes, myelination, and axonal integrity in the CNS. Neuroscientist 2009, 15:367-379.
    • (2009) Neuroscientist , vol.15 , pp. 367-379
    • Baes, M.1    Aubourg, P.2
  • 88
    • 79958228923 scopus 로고    scopus 로고
    • Astrocyte phenotypes and their relationship to myelination
    • Nash B., Ioannidou K., Barnett S.C. Astrocyte phenotypes and their relationship to myelination. J. Anat. 2010, 219:44-52.
    • (2010) J. Anat. , vol.219 , pp. 44-52
    • Nash, B.1    Ioannidou, K.2    Barnett, S.C.3
  • 89
    • 79960459422 scopus 로고    scopus 로고
    • Cholesterol metabolism in neurons and astrocytes
    • Pfrieger F.W., Ungerer N. Cholesterol metabolism in neurons and astrocytes. Prog. Lipid Res. 2011, 50:357-371.
    • (2011) Prog. Lipid Res. , vol.50 , pp. 357-371
    • Pfrieger, F.W.1    Ungerer, N.2
  • 90
    • 1842790914 scopus 로고    scopus 로고
    • Glial lipoproteins stimulate axon growth of central nervous system neurons in compartmented cultures
    • Hayashi H., Campenot R.B., Vance D.E., Vance J.E. Glial lipoproteins stimulate axon growth of central nervous system neurons in compartmented cultures. J. Biol. Chem. 2004, 279:14009-14015.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14009-14015
    • Hayashi, H.1    Campenot, R.B.2    Vance, D.E.3    Vance, J.E.4
  • 92
    • 0842326606 scopus 로고    scopus 로고
    • Therapeutic effects of normal cells on ABCD1 deficient cells in vitro and hematopoietic cell transplantation in the X-ALD mouse model
    • Yamada T., Ohyagi Y., Shinnoh N., Kikuchi H., Osoegawa M., Ochi H., Kira J., Furuya H. Therapeutic effects of normal cells on ABCD1 deficient cells in vitro and hematopoietic cell transplantation in the X-ALD mouse model. J. Neurol. Sci. 2004, 218:91-97.
    • (2004) J. Neurol. Sci. , vol.218 , pp. 91-97
    • Yamada, T.1    Ohyagi, Y.2    Shinnoh, N.3    Kikuchi, H.4    Osoegawa, M.5    Ochi, H.6    Kira, J.7    Furuya, H.8
  • 96
    • 0035201037 scopus 로고    scopus 로고
    • The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette transporter-like protein required for peroxisomal fatty acid β-oxidation
    • Zolman B.K., Silva I.D., Bartel B. The Arabidopsis pxa1 mutant is defective in an ATP-binding cassette transporter-like protein required for peroxisomal fatty acid β-oxidation. Plant Physiol. 2001, 127:1266-1278.
    • (2001) Plant Physiol. , vol.127 , pp. 1266-1278
    • Zolman, B.K.1    Silva, I.D.2    Bartel, B.3
  • 97
    • 70849102767 scopus 로고    scopus 로고
    • The ABC transporter PXA1 and peroxisomal β-oxidation are vital for metabolism in mature leaves of Arabidopsis during extended darkness
    • Kunz H.H., Scharnewski M., Feussner K., Feussner I., Flugge U.I., Fulda M., Gierth M. The ABC transporter PXA1 and peroxisomal β-oxidation are vital for metabolism in mature leaves of Arabidopsis during extended darkness. Plant Cell 2009, 21:2733-2749.
    • (2009) Plant Cell , vol.21 , pp. 2733-2749
    • Kunz, H.H.1    Scharnewski, M.2    Feussner, K.3    Feussner, I.4    Flugge, U.I.5    Fulda, M.6    Gierth, M.7
  • 98
    • 77956922124 scopus 로고    scopus 로고
    • The Arabidopsis peroxisomal ABC transporter, comatose, complements the Saccharomyces cerevisiae pxa1pxa2Delta mutant for metabolism of long-chain fatty acids and exhibits fatty acyl-CoA-stimulated ATPase activity
    • Nyathi Y., De Marcos Lousa C., van Roermund C.W., Wanders R.J., Johnson B., Baldwin S.A., Theodoulou F.L., Baker A. The Arabidopsis peroxisomal ABC transporter, comatose, complements the Saccharomyces cerevisiae pxa1pxa2Delta mutant for metabolism of long-chain fatty acids and exhibits fatty acyl-CoA-stimulated ATPase activity. J. Biol. Chem. 2010, 285:29892-29902.
    • (2010) J. Biol. Chem. , vol.285 , pp. 29892-29902
    • Nyathi, Y.1    De Marcos Lousa, C.2    van Roermund, C.W.3    Wanders, R.J.4    Johnson, B.5    Baldwin, S.A.6    Theodoulou, F.L.7    Baker, A.8
  • 99
    • 20444476835 scopus 로고    scopus 로고
    • Jasmonic acid levels are reduced in COMATOSE ATP-binding cassette transporter mutants. Implications for transport of jasmonate precursors into peroxisomes
    • Theodoulou F.L., Job K., Slocombe S.P., Footitt S., Holdsworth M., Baker A., Larson T.R., Graham I.A. Jasmonic acid levels are reduced in COMATOSE ATP-binding cassette transporter mutants. Implications for transport of jasmonate precursors into peroxisomes. Plant Physiol. 2005, 137:835-840.
    • (2005) Plant Physiol. , vol.137 , pp. 835-840
    • Theodoulou, F.L.1    Job, K.2    Slocombe, S.P.3    Footitt, S.4    Holdsworth, M.5    Baker, A.6    Larson, T.R.7    Graham, I.A.8
  • 101
    • 0035839555 scopus 로고    scopus 로고
    • The Arabidopsis thaliana ABC protein superfamily, a complete inventory
    • Sanchez-Fernandez R., Davies T.G., Coleman J.O., Rea P.A. The Arabidopsis thaliana ABC protein superfamily, a complete inventory. J. Biol. Chem. 2001, 276:30231-30244.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30231-30244
    • Sanchez-Fernandez, R.1    Davies, T.G.2    Coleman, J.O.3    Rea, P.A.4
  • 102
    • 33646883726 scopus 로고    scopus 로고
    • Trypanosoma brucei glycosomal ABC transporters: identification and membrane targeting
    • Yernaux C., Fransen M., Brees C., Lorenzen S., Michels P.A. Trypanosoma brucei glycosomal ABC transporters: identification and membrane targeting. Mol. Membr. Biol. 2006, 23:157-172.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 157-172
    • Yernaux, C.1    Fransen, M.2    Brees, C.3    Lorenzen, S.4    Michels, P.A.5
  • 103
    • 79951809054 scopus 로고    scopus 로고
    • Glycosomal ABC transporters of Trypanosoma brucei: characterisation of their expression, topology and substrate specificity
    • Igoillo-Esteve M., Mazet M., Deumer G., Wallemacq P., Michels P.A. Glycosomal ABC transporters of Trypanosoma brucei: characterisation of their expression, topology and substrate specificity. Int. J. Parasitol. 2011, 41:429-438.
    • (2011) Int. J. Parasitol. , vol.41 , pp. 429-438
    • Igoillo-Esteve, M.1    Mazet, M.2    Deumer, G.3    Wallemacq, P.4    Michels, P.A.5
  • 104
    • 0037077426 scopus 로고    scopus 로고
    • RNA interference of peroxisome-related genes in C. elegans: a new model for human peroxisomal disorders
    • Petriv O.I., Pilgrim D.B., Rachubinski R.A., Titorenko V.I. RNA interference of peroxisome-related genes in C. elegans: a new model for human peroxisomal disorders. Physiol. Genomics 2002, 10:79-91.
    • (2002) Physiol. Genomics , vol.10 , pp. 79-91
    • Petriv, O.I.1    Pilgrim, D.B.2    Rachubinski, R.A.3    Titorenko, V.I.4
  • 105
    • 68749099747 scopus 로고    scopus 로고
    • Caenorhabditis elegans utilizes dauer pheromone biosynthesis to dispose of toxic peroxisomal fatty acids for cellular homoeostasis
    • Joo H.J., Yim Y.H., Jeong P.Y., Jin Y.X., Lee J.E., Kim H., Jeong S.K., Chitwood D.J., Paik Y.K. Caenorhabditis elegans utilizes dauer pheromone biosynthesis to dispose of toxic peroxisomal fatty acids for cellular homoeostasis. Biochem. J. 2009, 422:61-71.
    • (2009) Biochem. J. , vol.422 , pp. 61-71
    • Joo, H.J.1    Yim, Y.H.2    Jeong, P.Y.3    Jin, Y.X.4    Lee, J.E.5    Kim, H.6    Jeong, S.K.7    Chitwood, D.J.8    Paik, Y.K.9
  • 106
    • 0029783210 scopus 로고    scopus 로고
    • The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae
    • Hettema E.H., van Roermund C.W., Distel B., van den Berg M., Vilela C., Rodrigues-Pousada C., Wanders R.J., Tabak H.F. The ABC transporter proteins Pat1 and Pat2 are required for import of long-chain fatty acids into peroxisomes of Saccharomyces cerevisiae. EMBO J. 1996, 15:3813-3822.
    • (1996) EMBO J. , vol.15 , pp. 3813-3822
    • Hettema, E.H.1    van Roermund, C.W.2    Distel, B.3    van den Berg, M.4    Vilela, C.5    Rodrigues-Pousada, C.6    Wanders, R.J.7    Tabak, H.F.8
  • 107
    • 0030662714 scopus 로고    scopus 로고
    • Transport of activated fatty acids by the peroxisomal ATP-binding-cassette transporter Pxa2 in a semi-intact yeast cell system
    • Verleur N., Hettema E.H., van Roermund C.W., Tabak H.F., Wanders R.J. Transport of activated fatty acids by the peroxisomal ATP-binding-cassette transporter Pxa2 in a semi-intact yeast cell system. Eur. J. Biochem. 1997, 249:657-661.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 657-661
    • Verleur, N.1    Hettema, E.H.2    van Roermund, C.W.3    Tabak, H.F.4    Wanders, R.J.5
  • 108
    • 2442536808 scopus 로고    scopus 로고
    • Defect in peroxisomal multifunctional enzyme MFE1 affects cAMP relay in Dictyostelium
    • Matsuoka S., Kuwayama H., Ikeno D., Oyama M., Maeda M. Defect in peroxisomal multifunctional enzyme MFE1 affects cAMP relay in Dictyostelium. Dev. Growth Differ. 2004, 46:195-199.
    • (2004) Dev. Growth Differ. , vol.46 , pp. 195-199
    • Matsuoka, S.1    Kuwayama, H.2    Ikeno, D.3    Oyama, M.4    Maeda, M.5
  • 109
    • 0038143240 scopus 로고    scopus 로고
    • MFE1, a member of the peroxisomal hydroxyacyl coenzyme A dehydrogenase family, affects fatty acid metabolism necessary for morphogenesis in Dictyostelium spp
    • Matsuoka S., Saito T., Kuwayama H., Morita N., Ochiai H., Maeda M. MFE1, a member of the peroxisomal hydroxyacyl coenzyme A dehydrogenase family, affects fatty acid metabolism necessary for morphogenesis in Dictyostelium spp. Eukaryot. Cell 2003, 2:638-645.
    • (2003) Eukaryot. Cell , vol.2 , pp. 638-645
    • Matsuoka, S.1    Saito, T.2    Kuwayama, H.3    Morita, N.4    Ochiai, H.5    Maeda, M.6
  • 110
    • 0036688643 scopus 로고    scopus 로고
    • Evolutionary analyses of ABC transporters of Dictyostelium discoideum
    • Anjard C., Loomis W.F. Evolutionary analyses of ABC transporters of Dictyostelium discoideum. Eukaryot. Cell 2002, 1:643-652.
    • (2002) Eukaryot. Cell , vol.1 , pp. 643-652
    • Anjard, C.1    Loomis, W.F.2
  • 111
  • 112
    • 0029094333 scopus 로고
    • Interactions of a very long chain fatty acid with model membranes and serum albumin. Implications for the pathogenesis of adrenoleukodystrophy
    • Ho J.K., Moser H., Kishimoto Y., Hamilton J.A. Interactions of a very long chain fatty acid with model membranes and serum albumin. Implications for the pathogenesis of adrenoleukodystrophy. J. Clin. Invest. 1995, 96:1455-1463.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1455-1463
    • Ho, J.K.1    Moser, H.2    Kishimoto, Y.3    Hamilton, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.