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Volumn 83, Issue 1-2, 2004, Pages 16-27

Peroxisomes, lipid metabolism, and peroxisomal disorders

Author keywords

Etherphospholipid biosynthesis; Fatty acid oxidation; Fatty acid oxidation; Peroxisome biogenesis; Refsum disease; Zellweger syndrome

Indexed keywords

ACYL COENZYME A OXIDASE; PHOSPHOLIPID; RACEMASE;

EID: 4744371532     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ymgme.2004.08.016     Document Type: Review
Times cited : (176)

References (56)
  • 1
    • 0034255179 scopus 로고    scopus 로고
    • Peroxisome biogenesis disorders: Genetics and cell biology
    • S.J. Gould, and D. Valle Peroxisome biogenesis disorders: genetics and cell biology Trends Genet. 16 2000 340 345
    • (2000) Trends Genet. , vol.16 , pp. 340-345
    • Gould, S.J.1    Valle, D.2
  • 3
    • 0020345656 scopus 로고
    • Cerebro-hepato-renal (Zellweger) syndrome and neonatal adrenoleukodystrophy: Similarities in phenotype and accumulation of very long chain fatty acids
    • F.R. Brown, A.J. McAdams, J.W. Cummins, R. Konkol, I. Singh, A.B. Moser, and H.W. Moser Cerebro-hepato-renal (Zellweger) syndrome and neonatal adrenoleukodystrophy: similarities in phenotype and accumulation of very long chain fatty acids Johns Hopkins Med. J. 151 1982 344 351
    • (1982) Johns Hopkins Med. J. , vol.151 , pp. 344-351
    • Brown, F.R.1    McAdams, A.J.2    Cummins, J.W.3    Konkol, R.4    Singh, I.5    Moser, A.B.6    Moser, H.W.7
  • 4
    • 0020574070 scopus 로고
    • Severe plasmalogen deficiency in tissues of infants without peroxisomes (Zellweger syndrome)
    • H.S.A. Heymans, R.B.H. Schutgens, R. Tan, H. vanden Bosch, and P. Borst Severe plasmalogen deficiency in tissues of infants without peroxisomes (Zellweger syndrome) Nature 306 1983 69 70
    • (1983) Nature , vol.306 , pp. 69-70
    • Heymans, H.S.A.1    Schutgens, R.B.H.2    Tan, R.3    Vanden Bosch, H.4    Borst, P.5
  • 5
    • 0024501212 scopus 로고
    • Dihydroxyacetone phosphate acyltransferase and alkyldihydroxyacetone phosphate synthase activities in rat liver subcellular fractions and human skin fibroblasts
    • H. Singh, S. Usher, and A. Poulos Dihydroxyacetone phosphate acyltransferase and alkyldihydroxyacetone phosphate synthase activities in rat liver subcellular fractions and human skin fibroblasts Arch. Biochem. Biophys. 268 1989 676 686
    • (1989) Arch. Biochem. Biophys. , vol.268 , pp. 676-686
    • Singh, H.1    Usher, S.2    Poulos, A.3
  • 6
    • 0031590799 scopus 로고    scopus 로고
    • Ether lipid biosynthesis-isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase
    • T.P. Thai, H. Heid, H.R. Rackwitz, A. Hunziker, K. Gorgas, and W.W. Just Ether lipid biosynthesis-isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase FEBS Lett. 420 1997 205 211
    • (1997) FEBS Lett. , vol.420 , pp. 205-211
    • Thai, T.P.1    Heid, H.2    Rackwitz, H.R.3    Hunziker, A.4    Gorgas, K.5    Just, W.W.6
  • 7
    • 0031897918 scopus 로고    scopus 로고
    • Acyl-CoA-dihydroxyacetonephosphate acyltransferase - Cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2
    • R. Ofman, E.H. Hettema, E.M. Hogenhout, U. Caruso, A.O. Muijsers, and R.J.A. Wanders Acyl-CoA-dihydroxyacetonephosphate acyltransferase - cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2 Hum. Mol. Genet. 7 1998 847 853
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 847-853
    • Ofman, R.1    Hettema, E.H.2    Hogenhout, E.M.3    Caruso, U.4    Muijsers, A.O.5    Wanders, R.J.A.6
  • 8
    • 0031576030 scopus 로고    scopus 로고
    • Nucleotide sequence of human alkyl-dihydroxyacetonephosphate synthase cDNA reveals the presence of a peroxisomal targeting signal 2
    • E.C. de Vet, B.T. van den Broek, and H. van den Bosch Nucleotide sequence of human alkyl-dihydroxyacetonephosphate synthase cDNA reveals the presence of a peroxisomal targeting signal 2 Biochim. Biophys. Acta 1346 1997 25 29
    • (1997) Biochim. Biophys. Acta , vol.1346 , pp. 25-29
    • De Vet, E.C.1    Van Den Broek, B.T.2    Van Den Bosch, H.3
  • 9
    • 2942633430 scopus 로고    scopus 로고
    • Functions and biosynthesis of plasmalogens in health and disease
    • P. Brites, H.R. Waterham, and R.J.A. Wanders Functions and biosynthesis of plasmalogens in health and disease Biochim. Biophys. Acta 1636 2004 219 231
    • (2004) Biochim. Biophys. Acta , vol.1636 , pp. 219-231
    • Brites, P.1    Waterham, H.R.2    Wanders, R.J.A.3
  • 13
    • 0032562566 scopus 로고    scopus 로고
    • Alkyl-dihydroxyacetonephosphate synthase: Fate in peroxisome biogenesis disorders and identification of the point mutation underlying a single enzyme deficiency
    • E.C. de Vet, L. IJlst, W. Oostheim, R.J.A. Wanders, and H. van den Bosch Alkyl-dihydroxyacetonephosphate synthase: fate in peroxisome biogenesis disorders and identification of the point mutation underlying a single enzyme deficiency J. Biol. Chem. 273 1998 10296 10301
    • (1998) J. Biol. Chem. , vol.273 , pp. 10296-10301
    • De Vet, E.C.1    Ijlst, L.2    Oostheim, W.3    Wanders, R.J.A.4    Van Den Bosch, H.5
  • 19
    • 0005827475 scopus 로고    scopus 로고
    • Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes
    • J. Biermann, W.W. Just, R.J.A. Wanders, and H. van den Bosch Alkyl-dihydroxyacetone phosphate synthase and dihydroxyacetone phosphate acyltransferase form a protein complex in peroxisomes Eur. J. Biochem. 261 1999 492 499
    • (1999) Eur. J. Biochem. , vol.261 , pp. 492-499
    • Biermann, J.1    Just, W.W.2    Wanders, R.J.A.3    Van Den Bosch, H.4
  • 20
    • 0032693473 scopus 로고    scopus 로고
    • Ether lipid biosynthesis. Alkyl-dihydroxyacetonephosphate synthase protein deficiency leads to reduced dihydroxyacetonephosphate acyltransferase activities
    • E.C. de Vet, L. IJlst, W. Oostheim, C. Dekker, H.W. Moser, H. vanden Bosch, and R.J.A. Wanders Ether lipid biosynthesis. Alkyl- dihydroxyacetonephosphate synthase protein deficiency leads to reduced dihydroxyacetonephosphate acyltransferase activities J. Lipid Res. 40 1999 1998 2003
    • (1999) J. Lipid Res. , vol.40 , pp. 1998-2003
    • De Vet, E.C.1    Ijlst, L.2    Oostheim, W.3    Dekker, C.4    Moser, H.W.5    Vanden Bosch, H.6    Wanders, R.J.A.7
  • 21
    • 0029589279 scopus 로고
    • Reevaluation of the pathways for the biosynthesis of polyunsaturated fatty acids
    • H. Sprecher, D.L. Luthria, B.S. Mohammed, and S.P. Baykousheva Reevaluation of the pathways for the biosynthesis of polyunsaturated fatty acids J. Lipid Res. 36 1995 2471 2477
    • (1995) J. Lipid Res. , vol.36 , pp. 2471-2477
    • Sprecher, H.1    Luthria, D.L.2    Mohammed, B.S.3    Baykousheva, S.P.4
  • 22
  • 23
    • 0028982895 scopus 로고
    • Purification and characterization of an alpha-methylacyl-CoA racemase from human liver
    • W. Schmitz, C. Albers, R. Fingerhut, and E. Conzelmann Purification and characterization of an alpha-methylacyl-CoA racemase from human liver Eur. J. Biochem. 231 1995 815 822
    • (1995) Eur. J. Biochem. , vol.231 , pp. 815-822
    • Schmitz, W.1    Albers, C.2    Fingerhut, R.3    Conzelmann, E.4
  • 24
    • 0031053480 scopus 로고    scopus 로고
    • Stereochemistry of peroxisomal and mitochondrial beta-oxidation of alpha-methylacyl-CoAs
    • W. Schmitz, and E. Conzelmann Stereochemistry of peroxisomal and mitochondrial beta-oxidation of alpha-methylacyl-CoAs Eur. J. Biochem. 244 1997 434 440
    • (1997) Eur. J. Biochem. , vol.244 , pp. 434-440
    • Schmitz, W.1    Conzelmann, E.2
  • 25
    • 0030821703 scopus 로고    scopus 로고
    • Molecular cloning of cDNA species for rat and mouse liver alpha-methylacyl-CoA racemases
    • W. Schmitz, H.M. Helander, J.K. Hiltunen, and E. Conzelmann Molecular cloning of cDNA species for rat and mouse liver alpha-methylacyl-CoA racemases Biochem. J. 326 1997 883 889
    • (1997) Biochem. J. , vol.326 , pp. 883-889
    • Schmitz, W.1    Helander, H.M.2    Hiltunen, J.K.3    Conzelmann, E.4
  • 27
    • 0035130658 scopus 로고    scopus 로고
    • Plasma analysis of di- and trihydroxycholestanoic acid diastereoisomers in peroxisomal alpha-methylacyl-CoA racemase deficiency
    • S. Ferdinandusse, H. Overmars, S. Denis, H.R. Waterham, R.J.A. Wanders, and P. Vreken Plasma analysis of di- and trihydroxycholestanoic acid diastereoisomers in peroxisomal alpha-methylacyl-CoA racemase deficiency J. Lipid Res. 42 2001 137 141
    • (2001) J. Lipid Res. , vol.42 , pp. 137-141
    • Ferdinandusse, S.1    Overmars, H.2    Denis, S.3    Waterham, H.R.4    Wanders, R.J.A.5    Vreken, P.6
  • 29
    • 0036138306 scopus 로고    scopus 로고
    • The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism
    • M.C. Hunt, and S.E. Alexson The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism Prog. Lipid Res. 41 2002 99 130
    • (2002) Prog. Lipid Res. , vol.41 , pp. 99-130
    • Hunt, M.C.1    Alexson, S.E.2
  • 30
    • 0029064219 scopus 로고
    • The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions
    • C.W.T. van Roermund, Y. Elgersma, N. Singh, R.J.A. Wanders, and H.F. Tabak The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions EMBO J. 14 1995 3480 3486
    • (1995) EMBO J. , vol.14 , pp. 3480-3486
    • Van Roermund, C.W.T.1    Elgersma, Y.2    Singh, N.3    Wanders, R.J.A.4    Tabak, H.F.5
  • 31
    • 0029671098 scopus 로고    scopus 로고
    • L-Lactate dehydrogenase A4- and A3B isoforms are bona fide peroxisomal enzymes in rat liver. Evidence for involvement in intraperoxisomal NADH reoxidation
    • E. Baumgart, H.D. Fahimi, A. Stich, and A. Volkl l-Lactate dehydrogenase A4- and A3B isoforms are bona fide peroxisomal enzymes in rat liver. Evidence for involvement in intraperoxisomal NADH reoxidation J. Biol. Chem. 271 1996 3846 3855
    • (1996) J. Biol. Chem. , vol.271 , pp. 3846-3855
    • Baumgart, E.1    Fahimi, H.D.2    Stich, A.3    Volkl, A.4
  • 36
    • 0034488655 scopus 로고    scopus 로고
    • X-Linked adrenoleukodystrophy: Overview and prognosis as a function of age and brain magnetic resonance imaging abnormality. a study involving 372 patients
    • H.W. Moser, D.J. Loes, E.R. Melhem, G.V. Raymond, L. Bezman, C.S. Cox, and S.E. Lu X-Linked adrenoleukodystrophy: overview and prognosis as a function of age and brain magnetic resonance imaging abnormality. A study involving 372 patients Neuropediatrics 31 2000 227 239
    • (2000) Neuropediatrics , vol.31 , pp. 227-239
    • Moser, H.W.1    Loes, D.J.2    Melhem, E.R.3    Raymond, G.V.4    Bezman, L.5    Cox, C.S.6    Lu, S.E.7
  • 42
    • 0032816205 scopus 로고    scopus 로고
    • Enoyl-CoA hydratase deficiency: Identification of an new type of D-bifunctional protein deficiency
    • E.G. van Grunsven, P.A.W. Mooijer, P. Aubourg, and R.J.A. Wanders Enoyl-CoA hydratase deficiency: identification of an new type of D-bifunctional protein deficiency Hum. Mol. Genet. 8 1999 1509 1516
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1509-1516
    • Van Grunsven, E.G.1    Mooijer, P.A.W.2    Aubourg, P.3    Wanders, R.J.A.4
  • 46
    • 0001435689 scopus 로고
    • Ueber das Vorkommen der 3,7,11,15-Tetramethylhexadecansaure (phytansaure) in den Cholesterinestern und anderen Lipidfraktionen der Organe bei einem Krankheitsfall unbekanter Genese (Verdacht auf Heredopathia atactica polyneuritiformis, Refsum’s syndrome)
    • E. Klenk, and W. Kahlke Ueber das Vorkommen der 3,7,11,15- Tetramethylhexadecansaure (phytansaure) in den Cholesterinestern und anderen Lipidfraktionen der Organe bei einem Krankheitsfall unbekanter Genese (Verdacht auf Heredopathia atactica polyneuritiformis, Refsum’s syndrome) Hoppe Seylers Z. Physiol. Chem. 333 1963 133 139
    • (1963) Hoppe Seylers Z. Physiol. Chem. , vol.333 , pp. 133-139
    • Klenk, E.1    Kahlke, W.2
  • 47
    • 0037451008 scopus 로고    scopus 로고
    • Phytanic acid alpha-oxidation, new insights into an old problem: A review
    • R.J.A. Wanders, G.A. Jansen, and M.D. Lloyd Phytanic acid alpha-oxidation, new insights into an old problem: a review Biochim. Biophys. Acta 1631 2003 119 135
    • (2003) Biochim. Biophys. Acta , vol.1631 , pp. 119-135
    • Wanders, R.J.A.1    Jansen, G.A.2    Lloyd, M.D.3
  • 48
    • 0021713540 scopus 로고
    • Infantile Refsum’s disease (phytanic acid storage disease): A variant of Zellweger’s syndrome?
    • A. Poulos, P. Sharp, and M. Whiting Infantile Refsum’s disease (phytanic acid storage disease): a variant of Zellweger†™s syndrome? Clin. Genet. 26 1984 579 586
    • (1984) Clin. Genet. , vol.26 , pp. 579-586
    • Poulos, A.1    Sharp, P.2    Whiting, M.3
  • 49
    • 0028978668 scopus 로고
    • Phytanic acid alpha-oxidation in rat liver peroxisomes. Production of alpha-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors
    • S.J. Mihalik, A.M. Rainville, and P.A. Watkins Phytanic acid alpha-oxidation in rat liver peroxisomes. Production of alpha-hydroxyphytanoyl- CoA and formate is enhanced by dioxygenase cofactors Eur. J. Biochem. 232 1995 545 551
    • (1995) Eur. J. Biochem. , vol.232 , pp. 545-551
    • Mihalik, S.J.1    Rainville, A.M.2    Watkins, P.A.3
  • 50
    • 0030745425 scopus 로고    scopus 로고
    • Phytanoyl-Coenzyme a hydroxylase deficiencyâ€"the enzyme defect in Refsum’s disease
    • G.A. Jansen, R.J.A. Wanders, P.A. Watkins, and S.J. Mihalik Phytanoyl-Coenzyme A hydroxylase deficiencyâ€"the enzyme defect in Refsum’s disease N. Engl. J. Med. 337 1997 133 134
    • (1997) N. Engl. J. Med. , vol.337 , pp. 133-134
    • Jansen, G.A.1    Wanders, R.J.A.2    Watkins, P.A.3    Mihalik, S.J.4
  • 51
    • 0033621136 scopus 로고    scopus 로고
    • Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine pyrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids
    • V. Foulon, V.D. Antonenkov, K. Croes, E. Waelkens, G.P. Mannaerts, P.P. Van Veldhoven, and M. Casteels Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine pyrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids Proc. Natl. Acad. Sci. USA 96 1999 10039 10044
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10039-10044
    • Foulon, V.1    Antonenkov, V.D.2    Croes, K.3    Waelkens, E.4    Mannaerts, G.P.5    Van Veldhoven, P.P.6    Casteels, M.7
  • 52
    • 0034806097 scopus 로고    scopus 로고
    • Identification of pristanal dehydrogenase activity in peroxisomes: Conclusive evidence that the complete phytanic acid alpha-oxidation pathway is localized in peroxisomes
    • G.A. Jansen, D.M. vanden Brink, R. Ofman, O. Draghici, G. Dacremont, and R.J.A. Wanders Identification of pristanal dehydrogenase activity in peroxisomes: conclusive evidence that the complete phytanic acid alpha-oxidation pathway is localized in peroxisomes Biochem. Biophys. Res. Commun. 283 2001 674 679
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 674-679
    • Jansen, G.A.1    Vanden Brink, D.M.2    Ofman, R.3    Draghici, O.4    Dacremont, G.5    Wanders, R.J.A.6
  • 53
    • 0033551122 scopus 로고    scopus 로고
    • Human very-long-chain acyl-CoA synthetase: Cloning, topography, and relevance to branched-chain fatty acid metabolism
    • S.J. Steinberg, S.J. Wang, D.G. Kim, S.J. Mihalik, and P.A. Watkins Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism Biochem. Biophys. Res. Commun. 257 1999 615 621
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 615-621
    • Steinberg, S.J.1    Wang, S.J.2    Kim, D.G.3    Mihalik, S.J.4    Watkins, P.A.5
  • 54
    • 0031908208 scopus 로고    scopus 로고
    • Phytanic acid and pristanic acid are oxidized by sequential peroxisomal and mitochondrial reactions in cultured fibroblasts
    • N.M. Verhoeven, D.S. Roe, R.M. Kok, R.J.A. Wanders, C. Jakobs, and C. Roe Phytanic acid and pristanic acid are oxidized by sequential peroxisomal and mitochondrial reactions in cultured fibroblasts J. Lipid Res. 39 1998 66 74
    • (1998) J. Lipid Res. , vol.39 , pp. 66-74
    • Verhoeven, N.M.1    Roe, D.S.2    Kok, R.M.3    Wanders, R.J.A.4    Jakobs, C.5    Roe, C.6
  • 55
    • 0036316242 scopus 로고    scopus 로고
    • Refsum’s disease: A peroxisomal disorder affecting phytanic acid alpha-oxidation
    • A.S. Wierzbicki, M.D. Lloyd, C.J. Schofield, M.D. Feher, and F.B. Gibberd Refsum’s disease: a peroxisomal disorder affecting phytanic acid alpha-oxidation J. Neurochem. 80 2002 727 735
    • (2002) J. Neurochem. , vol.80 , pp. 727-735
    • Wierzbicki, A.S.1    Lloyd, M.D.2    Schofield, C.J.3    Feher, M.D.4    Gibberd, F.B.5
  • 56
    • 3042520951 scopus 로고    scopus 로고
    • Omicron-Hydroxylation of phytanic acid in rat liver microsomes: Implications for Refsum disease
    • J.C. Komen, M. Duran, and R.J. Wanders omicron-Hydroxylation of phytanic acid in rat liver microsomes: implications for Refsum disease J. Lipid Res. 45 2004 1341 1346
    • (2004) J. Lipid Res. , vol.45 , pp. 1341-1346
    • Komen, J.C.1    Duran, M.2    Wanders, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.