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Volumn 1841, Issue 8, 2014, Pages 1189-1199

From sheep to mice to cells: Tools for the study of the sphingolipidoses

Author keywords

Cell culture; Large animal model; Lysosomal storage disorder; Mouse model; Sphingolipid

Indexed keywords

GALACTOSYLCERAMIDASE; LIPID; PHOSPHOLIPASE A2; SPHINGOMYELIN PHOSPHODIESTERASE;

EID: 84903276555     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2014.02.008     Document Type: Review
Times cited : (14)

References (198)
  • 1
    • 34548329395 scopus 로고    scopus 로고
    • The metabolism and function of sphingolipids and glycosphingolipids
    • DOI 10.1007/s00018-007-7076-0
    • S. Lahiri, and A.H. Futerman The metabolism and function of sphingolipids and glycosphingolipids Cell. Mol. Life Sci. 64 2007 2270 2284 (Pubitemid 47347954)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.17 , pp. 2270-2284
    • Lahiri, S.1    Futerman, A.H.2
  • 2
    • 2942687937 scopus 로고    scopus 로고
    • The cell biology of lysosomal storage disorders
    • DOI 10.1038/nrm1423
    • A.H. Futerman, and G. van Meer The cell biology of lysosomal storage disorders Nat. Rev. Mol. Cell Biol. 5 2004 554 565 (Pubitemid 38868584)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.7 , pp. 554-565
    • Futerman, A.H.1    Van Meer, G.2
  • 3
    • 78649796983 scopus 로고    scopus 로고
    • Pathology and current treatment of neurodegenerative sphingolipidoses
    • M. Eckhardt Pathology and current treatment of neurodegenerative sphingolipidoses Neruomol. Med. 12 2010 362 382
    • (2010) Neruomol. Med. , vol.12 , pp. 362-382
    • Eckhardt, M.1
  • 4
    • 2942652829 scopus 로고    scopus 로고
    • The pathogenesis of glycosphingolipid storage disorders
    • DOI 10.1016/j.semcdb.2004.03.003, PII S1084952104000333
    • L. Ginzburg, Y. Kacher, and A.H. Futerman The pathogenesis of glycosphingolipid storage disorders Semin. Cell Dev. Biol. 15 2004 417 431 (Pubitemid 38781904)
    • (2004) Seminars in Cell and Developmental Biology , vol.15 , Issue.4 , pp. 417-431
    • Ginzburg, L.1    Kacher, Y.2    Futerman, A.H.3
  • 5
    • 0025826050 scopus 로고
    • Lysosomal storage diseases
    • E.F. Neufeld Lysosomal storage diseases Annu. Rev. Biochem. 60 1991 257 280
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 257-280
    • Neufeld, E.F.1
  • 6
    • 77954225471 scopus 로고    scopus 로고
    • Common and uncommon pathogenic cascades in lysosomal storage diseases
    • E.B. Vitner, F.M. Platt, and A.H. Futerman Common and uncommon pathogenic cascades in lysosomal storage diseases J. Biol. Chem. 285 2010 20423 20427
    • (2010) J. Biol. Chem. , vol.285 , pp. 20423-20427
    • Vitner, E.B.1    Platt, F.M.2    Futerman, A.H.3
  • 8
    • 0024997005 scopus 로고
    • Anderson-Fabry disease (angiokeratoma corporis diffusum universale)
    • K.W. Radcliffe, and B.A. Evans Anderson-Fabry disease (angiokeratoma corporis diffusum universale) Genitourin. Med. 66 1990 399 400 (Pubitemid 20355687)
    • (1990) Genitourinary Medicine , vol.66 , Issue.5 , pp. 399-400
    • Radcliffe, K.W.1    Evans, B.A.2
  • 10
    • 3242722272 scopus 로고    scopus 로고
    • Sphingolipidoses in Turkey
    • DOI 10.1016/j.braindev.2003.09.006, PII S0387760403001955
    • H.A. Ozkara, and M. Topcu Sphingolipidoses in Turkey Brain Dev. 26 2004 363 366 (Pubitemid 38953321)
    • (2004) Brain and Development , vol.26 , Issue.6 , pp. 363-366
    • Asuman Ozkara, H.1    Topcu, M.2
  • 12
    • 34248517981 scopus 로고    scopus 로고
    • CRC Press, Taylor and Francis Group Boca Raton, FL.
    • A.H. Futerman, and A. Zimran Gaucher Disease 2006 CRC Press, Taylor and Francis Group Boca Raton, FL.
    • (2006) Gaucher Disease
    • Futerman, A.H.1    Zimran, A.2
  • 13
    • 84874761253 scopus 로고    scopus 로고
    • Substrate compositional variation with tissue/region and Gba1 mutations in mouse models - Implications for Gaucher disease
    • Y. Sun, W. Zhang, Y.H. Xu, B. Quinn, N. Dasgupta, B. Liou, K.D. Setchell, and G.A. Grabowski Substrate compositional variation with tissue/region and Gba1 mutations in mouse models - implications for Gaucher disease PLoS One 8 2013 e57560
    • (2013) PLoS One , vol.8 , pp. 57560
    • Sun, Y.1    Zhang, W.2    Xu, Y.H.3    Quinn, B.4    Dasgupta, N.5    Liou, B.6    Setchell, K.D.7    Grabowski, G.A.8
  • 16
    • 0025897376 scopus 로고
    • Saposin proteins: Structure, function, and role in human lysosomal storage disorders
    • J.S. O'Brien, and Y. Kishimoto Saposin proteins: structure, function, and role in human lysosomal storage disorders FASEB J. 5 1991 301 308 (Pubitemid 21892890)
    • (1991) FASEB Journal , vol.5 , Issue.3 , pp. 301-308
    • O'Brien, J.S.1    Kishimoto, Y.2
  • 17
    • 0031292176 scopus 로고    scopus 로고
    • Gaucher disease: Gene frequencies and genotype/phenotype correlations
    • G.A. Grabowski Gaucher disease: gene frequencies and genotype/phenotype correlations Genet. Test. 1 1997 5 12 (Pubitemid 127526931)
    • (1997) Genetic Testing , vol.1 , Issue.1 , pp. 5-12
    • Grabowski, G.A.1
  • 23
    • 0026981191 scopus 로고
    • Inhibition of glucocerebrosidase and induction of neural abnormality by cyclophellitol in mice
    • DOI 10.1016/0003-9861(92)90685-P
    • S. Atsumi, C. Nosaka, H. Iinuma, and K. Umezawa Inhibition of glucocerebrosidase and induction of neural abnormality by cyclophellitol in mice Arch. Biochem. Biophys. 297 1992 362 367 (Pubitemid 23282893)
    • (1992) Archives of Biochemistry and Biophysics , vol.297 , Issue.2 , pp. 362-367
    • Atsumi, S.1    Nosaka, C.2    Iinuma, H.3    Umezawa, K.4
  • 24
    • 0027325612 scopus 로고
    • Accumulation of tissue glucosylsphingosine in Gaucher-like mouse induced by the glucosylceramidase inhibitor cyclophellitol
    • DOI 10.1006/abbi.1993.1353
    • S. Atsumi, C. Nosaka, H. Iinuma, and K. Umezawa Accumulation of tissue glucosylsphingosine in Gaucher-like mouse induced by the glucosylceramidase inhibitor cyclophellitol Arch. Biochem. Biophys. 304 1993 302 304 (Pubitemid 23214185)
    • (1993) Archives of Biochemistry and Biophysics , vol.304 , Issue.1 , pp. 302-304
    • Atsumi, S.1    Nosaka, C.2    Iinuma, H.3    Umezawa, K.4
  • 25
    • 43249127471 scopus 로고    scopus 로고
    • Dependence of reversibility and progression of mouse neuronopathic Gaucher disease on acid beta-glucosidase residual activity levels
    • Y.H. Xu, R. Reboulet, B. Quinn, J. Huelsken, D. Witte, and G.A. Grabowski Dependence of reversibility and progression of mouse neuronopathic Gaucher disease on acid beta-glucosidase residual activity levels Mol. Genet. Metab. 94 2008 190 203
    • (2008) Mol. Genet. Metab. , vol.94 , pp. 190-203
    • Xu, Y.H.1    Reboulet, R.2    Quinn, B.3    Huelsken, J.4    Witte, D.5    Grabowski, G.A.6
  • 29
    • 79952607967 scopus 로고    scopus 로고
    • Spatial and temporal correlation between neuron loss and neuroinflammation in a mouse model of neuronopathic Gaucher disease
    • T. Farfel-Becker, E.B. Vitner, S.N. Pressey, R. Eilam, J.D. Cooper, and A.H. Futerman Spatial and temporal correlation between neuron loss and neuroinflammation in a mouse model of neuronopathic Gaucher disease Hum. Mol. Genet. 20 2011 1375 1386
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1375-1386
    • Farfel-Becker, T.1    Vitner, E.B.2    Pressey, S.N.3    Eilam, R.4    Cooper, J.D.5    Futerman, A.H.6
  • 30
  • 31
    • 84861552789 scopus 로고    scopus 로고
    • Contribution of brain inflammation to neuronal cell death in neuronopathic forms of Gaucher's disease
    • E.B. Vitner, T. Farfel-Becker, R. Eilam, I. Biton, and A.H. Futerman Contribution of brain inflammation to neuronal cell death in neuronopathic forms of Gaucher's disease Brain 135 2012 1724 1735
    • (2012) Brain , vol.135 , pp. 1724-1735
    • Vitner, E.B.1    Farfel-Becker, T.2    Eilam, R.3    Biton, I.4    Futerman, A.H.5
  • 33
    • 0142244182 scopus 로고    scopus 로고
    • Viable Mouse Models of Acid β-Glucosidase Deficiency: The Defect in Gaucher Disease
    • Y.H. Xu, B. Quinn, D. Witte, and G.A. Grabowski Viable mouse models of acid beta-glucosidase deficiency: the defect in Gaucher disease Am. J. Pathol. 163 2003 2093 2101 (Pubitemid 37310038)
    • (2003) American Journal of Pathology , vol.163 , Issue.5 , pp. 2093-2101
    • Xu, Y.-H.1    Quinn, B.2    Witte, D.3    Grabowski, G.A.4
  • 38
    • 33846223535 scopus 로고    scopus 로고
    • Generation of a conditional knockout of murine glucocerebrosidase: Utility for the study of Gaucher disease
    • DOI 10.1016/j.ymgme.2006.09.008, PII S1096719206003015
    • G.B. Sinclair, G. Jevon, K.E. Colobong, D.R. Randall, F.Y. Choy, and L.A. Clarke Generation of a conditional knockout of murine glucocerebrosidase: utility for the study of Gaucher disease Mol. Genet. Metab. 90 2007 148 156 (Pubitemid 46108614)
    • (2007) Molecular Genetics and Metabolism , vol.90 , Issue.2 , pp. 148-156
    • Sinclair, G.B.1    Jevon, G.2    Colobong, K.E.3    Randall, D.R.4    Choy, F.Y.M.5    Clarke, L.A.6
  • 41
    • 0036392385 scopus 로고    scopus 로고
    • Prosaposin: Threshold rescue and analysis of the "neuritogenic" region in transgenic mice
    • Y. Sun, X. Qi, D.P. Witte, E. Ponce, K. Kondoh, B. Quinn, and G.A. Grabowski Prosaposin: threshold rescue and analysis of the " neuritogenic" region in transgenic mice Mol. Genet. Metab. 76 2002 271 286
    • (2002) Mol. Genet. Metab. , vol.76 , pp. 271-286
    • Sun, Y.1    Qi, X.2    Witte, D.P.3    Ponce, E.4    Kondoh, K.5    Quinn, B.6    Grabowski, G.A.7
  • 42
    • 25444512703 scopus 로고    scopus 로고
    • Gaucher disease mouse models: Point mutations at the acid β-glucosidase locus combined with low-level prosaposin expression lead to disease variants
    • DOI 10.1194/jlr.M500202-JLR200
    • Y. Sun, B. Quinn, D.P. Witte, and G.A. Grabowski Gaucher disease mouse models: point mutations at the acid beta-glucosidase locus combined with low-level prosaposin expression lead to disease variants J. Lipid Res. 46 2005 2102 2113 (Pubitemid 41377462)
    • (2005) Journal of Lipid Research , vol.46 , Issue.10 , pp. 2102-2113
    • Sun, Y.1    Quinn, B.2    Witte, D.P.3    Grabowski, G.A.4
  • 44
    • 33845577582 scopus 로고    scopus 로고
    • Conditional expression of human acid β-glucosidase improves the visceral phenotype in a Gaucher disease mouse model
    • DOI 10.1194/jlr.M600239-JLR200
    • Y. Sun, B. Quinn, Y.H. Xu, T. Leonova, D.P. Witte, and G.A. Grabowski Conditional expression of human acid beta-glucosidase improves the visceral phenotype in a Gaucher disease mouse model J. Lipid Res. 47 2006 2161 2170 (Pubitemid 44936126)
    • (2006) Journal of Lipid Research , vol.47 , Issue.10 , pp. 2161-2170
    • Sun, Y.1    Quinn, B.2    Xu, Y.-H.3    Leonova, T.4    Witte, D.P.5    Grabowski, G.A.6
  • 45
    • 84878398412 scopus 로고    scopus 로고
    • Transgenic mice expressing human glucocerebrosidase variants: Utility for the study of Gaucher disease
    • A. Sanders, H. Hemmelgarn, H.L. Melrose, L. Hein, M. Fuller, and L.A. Clarke Transgenic mice expressing human glucocerebrosidase variants: utility for the study of Gaucher disease Blood Cells Mol. Dis. 51 2013 109 115
    • (2013) Blood Cells Mol. Dis. , vol.51 , pp. 109-115
    • Sanders, A.1    Hemmelgarn, H.2    Melrose, H.L.3    Hein, L.4    Fuller, M.5    Clarke, L.A.6
  • 46
    • 0015740608 scopus 로고
    • Neurovisceral glucocerebroside storage (Gaucher's disease) in a dog
    • W.J. Hartley, and W.F. Blakemore Neurovisceral glucocerebroside storage (Gaucher's disease) in a dog Vet. Pathol. 10 1973 191 201
    • (1973) Vet. Pathol. , vol.10 , pp. 191-201
    • Hartley, W.J.1    Blakemore, W.F.2
  • 47
    • 0014759698 scopus 로고
    • Histiocytosis in two pigs and a cow: Conditions resembling lipid storage disorders in man
    • A.T. Sandison, and L.J. Anderson Histiocytosis in two pigs and a cow: conditions resembling lipid storage disorders in man J. Pathol. 100 1970 207 210
    • (1970) J. Pathol. , vol.100 , pp. 207-210
    • Sandison, A.T.1    Anderson, L.J.2
  • 48
    • 0014328651 scopus 로고
    • Lipidosis of the hepatic reticulo-endothelial cells in a sheep
    • L. Laws, and J.R. Saal Lipidosis of the hepatic reticulo-endothelial cells in a sheep Aust. Vet. J. 44 1968 416 417
    • (1968) Aust. Vet. J. , vol.44 , pp. 416-417
    • Laws, L.1    Saal, J.R.2
  • 50
    • 36148974001 scopus 로고    scopus 로고
    • Secondary sphingolipid accumulation in a macrophage model of Gaucher disease
    • DOI 10.1016/j.ymgme.2007.08.001, PII S1096719207002521
    • L.K. Hein, P.J. Meikle, J.J. Hopwood, and M. Fuller Secondary sphingolipid accumulation in a macrophage model of Gaucher disease Mol. Genet. Metab. 92 2007 336 345 (Pubitemid 350117716)
    • (2007) Molecular Genetics and Metabolism , vol.92 , Issue.4 , pp. 336-345
    • Hein, L.K.1    Meikle, P.J.2    Hopwood, J.J.3    Fuller, M.4
  • 51
    • 27744461413 scopus 로고    scopus 로고
    • Recombinant glucocerebrosidase uptake by Gaucher disease human osteoblast culture model
    • DOI 10.1016/j.bcmd.2005.07.009, PII S1079979605001117
    • M. Lamghari, C.C. Barrias, C. Sa Miranda, and M.A. Barbosa Recombinant glucocerebrosidase uptake by Gaucher disease human osteoblast culture model Blood Cells Mol. Dis. 35 2005 348 354 (Pubitemid 41630720)
    • (2005) Blood Cells, Molecules, and Diseases , vol.35 , Issue.3 , pp. 348-354
    • Lamghari, M.1    Barrias, C.C.2    Sa Miranda, C.3    Barbosa, M.A.4
  • 52
    • 0034088326 scopus 로고    scopus 로고
    • The increased sensitivity of neurons with elevated glucocerebroside to neurotoxic agents can be reversed by imiglucerase
    • DOI 10.1023/A:1005622001239
    • D. Pelled, H. Shogomori, and A.H. Futerman The increased sensitivity of neurons with elevated glucocerebroside to neurotoxic agents can be reversed by imiglucerase J. Inherit. Metab. Dis. 23 2000 175 184 (Pubitemid 30198120)
    • (2000) Journal of Inherited Metabolic Disease , vol.23 , Issue.2 , pp. 175-184
    • Pelled, D.1    Shogomori, H.2    Futerman, A.H.3
  • 53
    • 0030020497 scopus 로고    scopus 로고
    • In vitro accumulation of glucocerebroside in neuroblastoma cells: A model for study of Gaucher disease pathobiology
    • DOI 10.1002/(SICI)1097-4547(19960201)43:3<365::AID-JNR11>3.0.CO;2-4
    • E.M. Prence, P. Chaturvedi, and D.S. Newburg In vitro accumulation of glucocerebroside in neuroblastoma cells: a model for study of Gaucher disease pathobiology J. Neurosci. Res. 43 1996 365 371 (Pubitemid 26054023)
    • (1996) Journal of Neuroscience Research , vol.43 , Issue.3 , pp. 365-371
    • Prence, E.M.1    Chaturvedi, P.2    Newburg, D.S.3
  • 54
    • 34248536519 scopus 로고    scopus 로고
    • Changes in macrophage morphology in a Gaucher disease model are dependent on CTP:phosphocholine cytidylyltransferase α
    • DOI 10.1016/j.bcmd.2007.03.005, PII S1079979607000721
    • Y. Kacher, A. Golan, Y. Pewzner-Jung, and A.H. Futerman Changes in macrophage morphology in a Gaucher disease model are dependent on CTP: phosphocholine cytidylyltransferase alpha Blood Cells Mol. Dis. 39 2007 124 129 (Pubitemid 46754932)
    • (2007) Blood Cells, Molecules, and Diseases , vol.39 , Issue.1 , pp. 124-129
    • Kacher, Y.1    Golan, A.2    Pewzner-Jung, Y.3    Futerman, A.H.4
  • 55
    • 2942675199 scopus 로고    scopus 로고
    • Phosphatidylcholine metabolism is altered in a monocyte-derived macrophage model of Gaucher disease but not in lymphocytes
    • DOI 10.1016/j.bcmd.2004.03.001, PII S1079979604000440
    • S. Trajkovic-Bodennec, J. Bodennec, and A.H. Futerman Phosphatidylcholine metabolism is altered in a monocyte-derived macrophage model of Gaucher disease but not in lymphocytes Blood Cells Mol. Dis. 33 2004 77 82 (Pubitemid 38829602)
    • (2004) Blood Cells, Molecules, and Diseases , vol.33 , Issue.1 , pp. 77-82
    • Trajkovic-Bodennec, S.1    Bodennec, J.2    Futerman, A.H.3
  • 57
    • 0346218248 scopus 로고    scopus 로고
    • Toxicity of glucosylsphingosine (glucopsychosine) to cultured neuronal cells: A model system for assessing neuronal damage in Gaucher disease type 2 and 3
    • DOI 10.1016/j.nbd.2003.08.016
    • U.H. Schueler, T. Kolter, C.R. Kaneski, J.K. Blusztajn, M. Herkenham, K. Sandhoff, and R.O. Brady Toxicity of glucosylsphingosine (glucopsychosine) to cultured neuronal cells: a model system for assessing neuronal damage in Gaucher disease type 2 and 3 Neurobiol. Dis. 14 2003 595 601 (Pubitemid 37543536)
    • (2003) Neurobiology of Disease , vol.14 , Issue.3 , pp. 595-601
    • Schueler, U.H.1    Kolter, T.2    Kaneski, C.R.3    Blusztajn, J.K.4    Herkenham, M.5    Sandhoff, K.6    Brady, R.O.7
  • 58
    • 0242637088 scopus 로고    scopus 로고
    • Lyso-glycosphingolipids mobilize calcium from brain microsomes via multiple mechanisms
    • DOI 10.1042/BJ20030613
    • E. Lloyd-Evans, D. Pelled, C. Riebeling, and A.H. Futerman Lyso-glycosphingolipids mobilize calcium from brain microsomes via multiple mechanisms Biochem. J. 375 2003 561 565 (Pubitemid 37433504)
    • (2003) Biochemical Journal , vol.375 , Issue.3 , pp. 561-565
    • Lloyd-Evans, E.1    Pelled, D.2    Riebeling, C.3    Futerman, A.H.4
  • 60
    • 0037089589 scopus 로고    scopus 로고
    • Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cells
    • DOI 10.1101/gad.981002
    • P.J. Paddison, A.A. Caudy, E. Bernstein, G.J. Hannon, and D.S. Conklin Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cells Genes Dev 16 2002 948 958 (Pubitemid 34408544)
    • (2002) Genes and Development , vol.16 , Issue.8 , pp. 948-958
    • Paddison, P.J.1    Caudy, A.A.2    Bernstein, E.3    Hannon, G.J.4    Conklin, D.S.5
  • 61
    • 0035035316 scopus 로고    scopus 로고
    • Fabry disease: Twenty novel α-galactosidase a mutations causing the classical phenotype
    • DOI 10.1007/s100380170088
    • G.A. Ashley, J. Shabbeer, M. Yasuda, C.M. Eng, and R.J. Desnick Fabry disease: twenty novel alpha-galactosidase A mutations causing the classical phenotype J. Hum. Genet. 46 2001 192 196 (Pubitemid 32435602)
    • (2001) Journal of Human Genetics , vol.46 , Issue.4 , pp. 192-196
    • Ashley, G.A.1    Shabbeer, J.2    Yasuda, M.3    Eng, C.M.4    Desnick, R.J.5
  • 62
    • 0028269904 scopus 로고
    • Molecular basis of Fabry disease: Mutations and polymorphisms in the human α-galactosidase A gene
    • C.M. Eng, and R.J. Desnick Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene Hum. Mutat. 3 1994 103 111 (Pubitemid 24077226)
    • (1994) Human Mutation , vol.3 , Issue.2 , pp. 103-111
    • Eng, C.M.1    Desnick, R.J.2
  • 63
    • 5044228518 scopus 로고    scopus 로고
    • Fabry disease: A review
    • DOI 10.1016/j.jbspin.2003.10.015, PII S1297319X03002355
    • C. Masson, I. Cisse, V. Simon, P. Insalaco, and M. Audran Fabry disease: a review Joint Bone Spine 71 2004 381 383 (Pubitemid 39335671)
    • (2004) Joint Bone Spine , vol.71 , Issue.5 , pp. 381-383
    • Masson, C.1    Cisse, I.2    Simon, V.3    Insalaco, P.4    Audran, M.5
  • 68
    • 0030704337 scopus 로고    scopus 로고
    • Generation and characterization of transgenic mice expressing a human mutant α-galactosidase with an R301Q substitution causing a variant form of Fabry disease
    • DOI 10.1016/S0014-5793(97)01263-5, PII S0014579397012635
    • M. Shimmoto, R. Kase, K. Itoh, K. Utsumi, S. Ishii, C. Taya, H. Yonekawa, and H. Sakuraba Generation and characterization of transgenic mice expressing a human mutant alpha-galactosidase with an R301Q substitution causing a variant form of Fabry disease FEBS Lett. 417 1997 89 91 (Pubitemid 27490479)
    • (1997) FEBS Letters , vol.417 , Issue.1 , pp. 89-91
    • Shimmoto, M.1    Kase, R.2    Itoh, K.3    Utsumi, K.4    Ishii, S.5    Taya, C.6    Yonekawa, H.7    Sakuraba, H.8
  • 69
    • 7044284796 scopus 로고    scopus 로고
    • Transgenic mouse expressing human mutant α-galactosidase A in an endogenous enzyme deficient background: A biochemical animal model for studying active-site specific chaperone therapy for Fabry disease
    • DOI 10.1016/j.bbadis.2004.07.001, PII S0925443904001322
    • S. Ishii, H. Yoshioka, K. Mannen, A.B. Kulkarni, and J.Q. Fan Transgenic mouse expressing human mutant alpha-galactosidase A in an endogenous enzyme deficient background: a biochemical animal model for studying active-site specific chaperone therapy for Fabry disease Biochim. Biophys. Acta 1690 2004 250 257 (Pubitemid 39423620)
    • (2004) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1690 , Issue.3 , pp. 250-257
    • Ishii, S.1    Yoshioka, H.2    Mannen, K.3    Kulkarni, A.B.4    Fan, J.-Q.5
  • 70
  • 72
    • 34548505835 scopus 로고    scopus 로고
    • Establishment and characterization of Fabry disease endothelial cells with an extended lifespan
    • DOI 10.1016/j.ymgme.2007.06.003, PII S1096719207001941
    • J.S. Shen, X.L. Meng, R. Schiffmann, R.O. Brady, and C.R. Kaneski Establishment and characterization of Fabry disease endothelial cells with an extended lifespan Mol. Genet. Metab. 92 2007 137 144 (Pubitemid 47371101)
    • (2007) Molecular Genetics and Metabolism , vol.92 , Issue.1-2 , pp. 137-144
    • Shen, J.-S.1    Meng, X.-L.2    Schiffmann, R.3    Brady, R.O.4    Kaneski, C.R.5
  • 74
    • 0141997305 scopus 로고    scopus 로고
    • Metachromatic leukodystrophy: Recent research developments
    • V. Gieselmann Metachromatic leukodystrophy: recent research developments J. Child Neurol. 18 2003 591 594 (Pubitemid 37258463)
    • (2003) Journal of Child Neurology , vol.18 , Issue.9 , pp. 591-594
    • Gieselmann, V.1
  • 76
    • 55549101637 scopus 로고    scopus 로고
    • Molecular analysis of ARSA and PSAP genes in twenty-one Italian patients with metachromatic leukodystrophy: Identification and functional characterization of 11 novel ARSA alleles
    • S. Grossi, S. Regis, C. Rosano, F. Corsolini, G. Uziel, M. Sessa, M. Di Rocco, G. Parenti, F. Deodato, V. Leuzzi, R. Biancheri, and M. Filocamo Molecular analysis of ARSA and PSAP genes in twenty-one Italian patients with metachromatic leukodystrophy: identification and functional characterization of 11 novel ARSA alleles Hum. Mutat. 29 2008 E220 E230
    • (2008) Hum. Mutat. , vol.29
    • Grossi, S.1    Regis, S.2    Rosano, C.3    Corsolini, F.4    Uziel, G.5    Sessa, M.6    Di Rocco, M.7    Parenti, G.8    Deodato, F.9    Leuzzi, V.10    Biancheri, R.11    Filocamo, M.12
  • 79
    • 34548426172 scopus 로고    scopus 로고
    • Increasing sulfatide synthesis in myelin-forming cells of arylsulfatase A-deficient mice causes demyelination and neurological symptoms reminiscent of human metachromatic leukodystrophy
    • DOI 10.1523/JNEUROSCI.2287-07.2007
    • H. Ramakrishnan, K.K. Hedayati, R. Lullmann-Rauch, C. Wessig, S.N. Fewou, H. Maier, H.H. Goebel, V. Gieselmann, and M. Eckhardt Increasing sulfatide synthesis in myelin-forming cells of arylsulfatase A-deficient mice causes demyelination and neurological symptoms reminiscent of human metachromatic leukodystrophy J. Neurosci. 27 2007 9482 9490 (Pubitemid 47358222)
    • (2007) Journal of Neuroscience , vol.27 , Issue.35 , pp. 9482-9490
    • Ramakrishnan, H.1    Hedayati, K.K.2    Lullmann-Rauch, R.3    Wessig, C.4    Fewou, S.N.5    Maier, H.6    Goebel, H.-H.7    Gieselmann, V.8    Eckhardt, M.9
  • 80
    • 34548167106 scopus 로고    scopus 로고
    • Sulfatide storage in neurons causes hyperexcitability and axonal degeneration in a mouse model of metachromatic leukodystrophy
    • DOI 10.1523/JNEUROSCI.2329-07.2007
    • M. Eckhardt, K.K. Hedayati, J. Pitsch, R. Lullmann-Rauch, H. Beck, S.N. Fewou, and V. Gieselmann Sulfatide storage in neurons causes hyperexcitability and axonal degeneration in a mouse model of metachromatic leukodystrophy J. Neurosci. 27 2007 9009 9021 (Pubitemid 47312065)
    • (2007) Journal of Neuroscience , vol.27 , Issue.34 , pp. 9009-9021
    • Eckhardt, M.1    Hedayati, K.K.2    Pitsch, J.3    Lullmann-Rauch, R.4    Beck, H.5    Fewou, S.N.6    Gieselmann, V.7
  • 84
    • 79959813959 scopus 로고    scopus 로고
    • Intracerebroventricular enzyme infusion corrects central nervous system pathology and dysfunction in a mouse model of metachromatic leukodystrophy
    • S. Stroobants, D. Gerlach, F. Matthes, D. Hartmann, J. Fogh, V. Gieselmann, R. D'Hooge, and U. Matzner Intracerebroventricular enzyme infusion corrects central nervous system pathology and dysfunction in a mouse model of metachromatic leukodystrophy Hum. Mol. Genet. 20 2011 2760 2769
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2760-2769
    • Stroobants, S.1    Gerlach, D.2    Matthes, F.3    Hartmann, D.4    Fogh, J.5    Gieselmann, V.6    D'Hooge, R.7    Matzner, U.8
  • 86
    • 33947509648 scopus 로고    scopus 로고
    • A spontaneously immortalized Schwann cell line to study the molecular aspects of metachromatic leukodystrophy
    • DOI 10.1016/j.jneumeth.2006.11.009, PII S016502700600570X
    • K. Saravanan, H. Bussow, N. Weiler, V. Gieselmann, and S. Franken A spontaneously immortalized Schwann cell line to study the molecular aspects of metachromatic leukodystrophy J. Neurosci. Methods 161 2007 223 233 (Pubitemid 46466949)
    • (2007) Journal of Neuroscience Methods , vol.161 , Issue.2 , pp. 223-233
    • Saravanan, K.1    Bussow, H.2    Weiler, N.3    Gieselmann, V.4    Franken, S.5
  • 87
    • 0035873272 scopus 로고    scopus 로고
    • A mutation in the saposin A domain of the sphingolipid activator protein (prosaposin) gene results in a late-onset, chronic form of globoid cell leukodystrophy in the mouse
    • J. Matsuda, M.T. Vanier, Y. Saito, J. Tohyama, and K. Suzuki A mutation in the saposin A domain of the sphingolipid activator protein (prosaposin) gene results in a late-onset, chronic form of globoid cell leukodystrophy in the mouse Hum. Mol. Genet. 10 2001 1191 1199 (Pubitemid 32487542)
    • (2001) Human Molecular Genetics , vol.10 , Issue.11 , pp. 1191-1199
    • Matsuda, J.1    Vanier, M.T.2    Saito, Y.3    Tohyama, J.4    Suzuki, K.5    Suzuki, K.6
  • 88
    • 84876840657 scopus 로고    scopus 로고
    • Lysosomal leukodystrophies: Krabbe disease and metachromatic leukodystrophy
    • A. Kohlschutter Lysosomal leukodystrophies: Krabbe disease and metachromatic leukodystrophy Handb. Clin. Neurol. 113 2013 1611 1618
    • (2013) Handb. Clin. Neurol. , vol.113 , pp. 1611-1618
    • Kohlschutter, A.1
  • 89
    • 80955131264 scopus 로고    scopus 로고
    • The myelin mutants as models to study myelin repair in the leukodystrophies
    • I.D. Duncan, Y. Kondo, and S.-C. Zhang The myelin mutants as models to study myelin repair in the leukodystrophies Neurotherapeutics 8 2011 607 624
    • (2011) Neurotherapeutics , vol.8 , pp. 607-624
    • Duncan, I.D.1    Kondo, Y.2    Zhang, S.-C.3
  • 90
    • 67649432567 scopus 로고    scopus 로고
    • Pathogenesis of leukodystrophy for Krabbe disease: Molecular mechanism and clinical treatment
    • N. Sakai Pathogenesis of leukodystrophy for Krabbe disease: molecular mechanism and clinical treatment Brain Dev. 31 2009 485 487
    • (2009) Brain Dev. , vol.31 , pp. 485-487
    • Sakai, N.1
  • 91
    • 0018966157 scopus 로고
    • Hereditary leucodystrophy in the mouse: The new mutant twitcher
    • L.W. Duchen, E.M. Eicher, J.M. Jacobs, F. Scaravilli, and F. Teixeira Hereditary leucodystrophy in the mouse: the new mutant twitcher Brain 103 1980 695 710 (Pubitemid 10001187)
    • (1980) Brain , vol.103 , Issue.3 , pp. 695-710
    • Duchen, L.W.1    Eicher, E.M.2    Jacobs, J.M.3
  • 92
    • 0019274883 scopus 로고
    • The Twitcher mouse: An enzymatically authentic model of human globoid cell leukodystrophy (Krabbe disease)
    • DOI 10.1016/0006-8993(80)90159-6
    • T. Kobayashi, T. Yamanaka, J.M. Jacobs, F. Teixeira, and K. Suzuki The twitcher mouse: an enzymatically authentic model of human globoid cell leukodystrophy (Krabbe disease) Brain Res. 202 1980 479 483 (Pubitemid 11130332)
    • (1980) Brain Research , vol.202 , Issue.2 , pp. 479-483
    • Kobayashi, T.1    Yamanaka, T.2    Jacobs, J.M.3
  • 93
    • 0020424790 scopus 로고
    • An accumulation of galactocerebroside in kidney from mouse globoid cell leukodystrophy (Twitcher)
    • H. Ida, F. Umezawa, E. Kasai, Y. Eto, and K. Maekawa An accumulation of galactocerebroside in kidney from mouse globoid cell leukodystrophy (twitcher) Biochem. Biophys. Res. Commun. 109 1982 634 638 (Pubitemid 13143732)
    • (1982) Biochemical and Biophysical Research Communications , vol.109 , Issue.3 , pp. 634-638
    • Ida, H.1    Umezawa, F.2    Kasai, E.3
  • 96
    • 0034900717 scopus 로고    scopus 로고
    • Generation of a mouse with low galactocerebrosidase activity by gene targeting: A new model of globoid cell leukodystrophy (Krabbe disease)
    • DOI 10.1006/mgme.2001.3194
    • P. Luzi, M.A. Rafi, M. Zaka, M. Curtis, M.T. Vanier, and D.A. Wenger Generation of a mouse with low galactocerebrosidase activity by gene targeting: a new model of globoid cell leukodystrophy (Krabbe disease) Mol. Genet. Metab. 73 2001 211 223 (Pubitemid 32709611)
    • (2001) Molecular Genetics and Metabolism , vol.73 , Issue.3 , pp. 211-223
    • Luzi, P.1    Rafi, M.A.2    Zaka, M.3    Curtis, M.4    Vanier, M.T.5    Wenger, D.A.6
  • 97
    • 0015292037 scopus 로고
    • Animal model: Globoid cell leukodystrophy in the dog
    • T.F. Fletcher, and H.J. Kurtz Animal model: globoid cell leukodystrophy in the dog Am. J. Pathol. 1972 375 378
    • (1972) Am. J. Pathol. , pp. 375-378
    • Fletcher, T.F.1    Kurtz, H.J.2
  • 98
    • 0016261640 scopus 로고
    • Globoid cell leukodystrophy in the bluetick hound dog. 1. Clinical manifestations
    • B.G. Boysen Globoid cell leukodystrophy in the bluetick hound dog. 1. Clinical manifestations Can. Vet. J. 15 1974 303 308
    • (1974) Can. Vet. J. , vol.15 , pp. 303-308
    • Boysen, B.G.1
  • 99
    • 0029943028 scopus 로고    scopus 로고
    • Cloning of the canine GALC cDNA and identification of the mutation causing globoid cell leukodystrophy in West Highland White and Cairn terriers
    • DOI 10.1006/geno.1996.0220
    • T. Victoria, M.A. Rafi, and D.A. Wenger Cloning of the canine GALC cDNA and identification of the mutation causing globoid cell leukodystrophy in West Highland White and Cairn terriers Genomics 33 1996 457 462 (Pubitemid 26159861)
    • (1996) Genomics , vol.33 , Issue.3 , pp. 457-462
    • Victoria, T.1    Rafi, M.A.2    Wenger, D.A.3
  • 101
    • 0031172376 scopus 로고    scopus 로고
    • Characterization of the rhesus monkey galactocerebrosidase (GALC) cDNA and gene and identification of the mutation causing globoid cell leukodystrophy (Krabbe disease) in this primate
    • DOI 10.1006/geno.1997.4744
    • P. Luzi, M.A. Rafi, T. Victoria, G.B. Baskin, and D.A. Wenger Characterization of the rhesus monkey galactocerebrosidase (GALC) cDNA and gene and identification of the mutation causing globoid cell leukodystrophy (Krabbe disease) in this primate Genomics 42 1997 319 324 (Pubitemid 27263763)
    • (1997) Genomics , vol.42 , Issue.2 , pp. 319-324
    • Luzi, P.1    Rafi, M.A.2    Victoria, T.3    Baskin, G.B.4    Wenger, D.A.5
  • 104
  • 107
    • 66149133657 scopus 로고    scopus 로고
    • Gene therapy for lysosomal storage diseases (LSDs) in large animal models
    • M. Haskins Gene therapy for lysosomal storage diseases (LSDs) in large animal models ILAR J. 50 2009 112 121
    • (2009) ILAR J. , vol.50 , pp. 112-121
    • Haskins, M.1
  • 108
    • 0031932297 scopus 로고    scopus 로고
    • Twenty five years of the "psychosine hypothesis": A personal perspective of its history and present status
    • K. Suzuki Twenty five years of the "psychosine hypothesis": a personal perspective of its history and present status Neurochem. Res. 23 1998 251 259
    • (1998) Neurochem. Res. , vol.23 , pp. 251-259
    • Suzuki, K.1
  • 109
  • 110
    • 33746050965 scopus 로고    scopus 로고
    • Krabbe disease: Psychosine-mediated activation of phospholipase A2 in oligodendrocyte cell death
    • DOI 10.1194/jlr.M600084-JLR200
    • S. Giri, M. Khan, R. Rattan, I. Singh, and a.K. Singh Krabbe disease: psychosine-mediated activation of phospholipase A2 in oligodendrocyte cell death J. Lipid Res. 47 2006 1478 1492 (Pubitemid 44079902)
    • (2006) Journal of Lipid Research , vol.47 , Issue.7 , pp. 1478-1492
    • Giri, S.1    Khan, M.2    Rattan, R.3    Singh, I.4    Singh, A.K.5
  • 111
    • 0020419627 scopus 로고
    • Fast axonal transport in extruded axoplasm from squid giant axon
    • S.T. Brady, R.J. Lasek, and R.D. Allen Fast axonal transport in extruded axoplasm from squid giant axon Science 218 1982 1129 1131 (Pubitemid 13223316)
    • (1982) Science , vol.218 , Issue.4577 , pp. 1129-1131
    • Brady, S.T.1    Lasek, R.J.2    Allen, R.D.3
  • 114
    • 77951893147 scopus 로고    scopus 로고
    • Acid sphingomyelinase, cell membranes and human disease: Lessons from Niemann-Pick disease
    • E.H. Schuchman Acid sphingomyelinase, cell membranes and human disease: lessons from Niemann-Pick disease FEBS Lett. 584 2010 1895 1900
    • (2010) FEBS Lett. , vol.584 , pp. 1895-1900
    • Schuchman, E.H.1
  • 115
    • 0021085107 scopus 로고
    • Partial enzyme deficiencies: Residual activities and the development of neurological disorders
    • E. Conzelmann, and K. Sandhoff Partial enzyme deficiencies: residual activities and the development of neurological disorders Dev. Neurosci. 6 1983 58 71 (Pubitemid 14237247)
    • (1983) Developmental Neuroscience , vol.6 , Issue.1 , pp. 58-71
    • Conzelmann, E.1    Sandhoff, K.2
  • 116
    • 35248814255 scopus 로고    scopus 로고
    • The pathogenesis and treatment of acid sphingomyelinase-deficient Niemann-Pick disease
    • DOI 10.1007/s10545-007-0632-9
    • E.H. Schuchman The pathogenesis and treatment of acid sphingomyelinase-deficient Niemann-Pick disease J. Inherit. Metab. Dis. 30 2007 654 663 (Pubitemid 47559876)
    • (2007) Journal of Inherited Metabolic Disease , vol.30 , Issue.5 , pp. 654-663
    • Schuchman, E.H.1
  • 119
    • 0029014350 scopus 로고
    • Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease)
    • B. Otterbach, and W. Stoffel Acid sphingomyelinase-deficient mice mimic the neurovisceral form of human lysosomal storage disease (Niemann-Pick disease) Cell 81 1995 1053 1061
    • (1995) Cell , vol.81 , pp. 1053-1061
    • Otterbach, B.1    Stoffel, W.2
  • 120
    • 0031406064 scopus 로고    scopus 로고
    • Pathology of visceral organs and bone marrow in an acid sphingomyelinase deficient knock-out mouse line, mimicking human Niemann-Pick disease type A
    • T.A. Kuemmel, J. Thiele, R. Schroeder, and W. Stoffel Pathology of visceral organs and bone marrow in an acid sphingomyelinase deficient knock-out mouse line, mimicking human Niemann-Pick disease type A A light and electron microscopic study Pathol. Res. Pract. 193 1997 663 671 (Pubitemid 28064112)
    • (1997) Pathology Research and Practice , vol.193 , Issue.10 , pp. 663-671
    • Kuemmel, T.A.1    Thiele, J.2    Schroeder, R.3    Stoffel, W.4
  • 121
    • 0029012443 scopus 로고
    • Acid sphingomyelinase deficient mice: A model of types A and B Niemann Pick disease
    • K. Horinouchi, S. Erlich, D.P. Perl, and K. Ferlinz Acid sphingomyelinase deficient mice: a model of types A and B Niemann Pick disease Nat. Genet. 10 1995 288 293
    • (1995) Nat. Genet. , vol.10 , pp. 288-293
    • Horinouchi, K.1    Erlich, S.2    Perl, D.P.3    Ferlinz, K.4
  • 122
    • 56349145208 scopus 로고    scopus 로고
    • Neuropathology of the acid sphingomyelinase knockout mouse model of Niemann-Pick A disease including structure-function studies associated with cerebellar Purkinje cell degeneration
    • S.L. Macauley, R.L. Sidman, E.H. Schuchman, T. Taksir, and G.R. Stewart Neuropathology of the acid sphingomyelinase knockout mouse model of Niemann-Pick A disease including structure-function studies associated with cerebellar Purkinje cell degeneration Exp. Neurol. 214 2008 181 192
    • (2008) Exp. Neurol. , vol.214 , pp. 181-192
    • Macauley, S.L.1    Sidman, R.L.2    Schuchman, E.H.3    Taksir, T.4    Stewart, G.R.5
  • 123
    • 29144444023 scopus 로고    scopus 로고
    • Defective calcium homeostasis in the cerebellum in a mouse model of Niemann-Pick a disease
    • DOI 10.1111/j.1471-4159.2005.03534.x
    • L. Ginzburg, and A.H. Futerman Defective calcium homeostasis in the cerebellum in a mouse model of Niemann-Pick A disease J. Neurochem. 95 2005 1619 1628 (Pubitemid 41804059)
    • (2005) Journal of Neurochemistry , vol.95 , Issue.6 , pp. 1619-1628
    • Ginzburg, L.1    Futerman, A.H.2
  • 126
    • 0035976969 scopus 로고    scopus 로고
    • Acid sphingomyelinase-deficient macrophages have defective cholesterol trafficking and efflux
    • A.R. Leventhal, W. Chen, A.R. Tall, and I. Tabas Acid sphingomyelinase-deficient macrophages have defective cholesterol trafficking and efflux J. Biol. Chem. 276 2001 44976 44983
    • (2001) J. Biol. Chem. , vol.276 , pp. 44976-44983
    • Leventhal, A.R.1    Chen, W.2    Tall, A.R.3    Tabas, I.4
  • 127
    • 1542358155 scopus 로고    scopus 로고
    • Ceramide synthesis and metabolism as a target for cancer therapy
    • DOI 10.1016/j.canlet.2003.08.034, PII S0304383503006360
    • C.P. Reynolds, B.J. Maurer, and R.N. Kolesnick Ceramide synthesis and metabolism as a target for cancer therapy Cancer Lett. 206 2004 169 180 (Pubitemid 38317287)
    • (2004) Cancer Letters , vol.206 , Issue.2 , pp. 169-180
    • Reynolds, C.P.1    Maurer, B.J.2    Kolesnick, R.N.3
  • 128
    • 0034641594 scopus 로고    scopus 로고
    • Creation of a mouse model for non-neurological (type B) Niemann-Pick disease by stable, low level expression of lysosomal sphingomyelinase in the absence of secretory sphingomyelinase: Relationship between brain intra-lysosomal enzyme activity and central nervous system function
    • S. Marathe, S.R. Miranda, C. Devlin, a. Johns, G. Kuriakose, K.J. Williams, E.H. Schuchman, and I. Tabas Creation of a mouse model for non-neurological (type B) Niemann-Pick disease by stable, low level expression of lysosomal sphingomyelinase in the absence of secretory sphingomyelinase: relationship between brain intra-lysosomal enzyme activity and central nervous system function Hum. Mol. Genet. 9 2000 1967 1976 (Pubitemid 30642661)
    • (2000) Human Molecular Genetics , vol.9 , Issue.13 , pp. 1967-1976
    • Marathe, S.1    Miranda, S.R.P.2    Devlin, C.3    Johns, A.4    Kuriakose, G.5    Williams, K.J.6    Schuchman, E.H.7    Tabas, I.8
  • 130
    • 84881106622 scopus 로고    scopus 로고
    • Sphingomyelin lipidosis (Niemann-Pick disease) in a juvenile raccoon (Procyon lotor)
    • N. Vapniarsky, D.A. Wenger, D. Scheenstra, and A. Mete Sphingomyelin lipidosis (Niemann-Pick disease) in a juvenile raccoon (Procyon lotor) J. Comp. Pathol. 149 2013 385 389
    • (2013) J. Comp. Pathol. , vol.149 , pp. 385-389
    • Vapniarsky, N.1    Wenger, D.A.2    Scheenstra, D.3    Mete, A.4
  • 131
    • 42449159755 scopus 로고    scopus 로고
    • Sphingomyelinase deficiency (Niemann-Pick disease) in a Hereford calf
    • DOI 10.1354/vp.45-2-201
    • G.K. Saunders, and D.A. Wenger Sphingomyelinase deficiency (Niemann-Pick disease) in a Hereford calf Vet. Pathol. 45 2008 201 202 (Pubitemid 351571655)
    • (2008) Veterinary Pathology , vol.45 , Issue.2 , pp. 201-202
    • Saunders, G.K.1    Wenger, D.A.2
  • 132
    • 0023404512 scopus 로고
    • Sphingomyelin lipidosis in a cat
    • H.J. Baker, and P.A. Wood Sphingomyelin lipidosis in a cat Vet. Pathol. 24 1987 386 391
    • (1987) Vet. Pathol. , vol.24 , pp. 386-391
    • Baker, H.J.1    Wood, P.A.2
  • 133
    • 0021710368 scopus 로고
    • Sphingomyelin lipidosis in a cat: Golgi studies
    • DOI 10.1007/BF00690467
    • S.U. Walkley, and H.J. Baker Sphingomyelin lipidosis in a cat: Golgi studies Acta Neuropathol. 65 1984 138 144 (Pubitemid 15221065)
    • (1984) Acta Neuropathologica , vol.65 , Issue.2 , pp. 138-144
    • Walkley, S.U.1    Baker, H.J.2
  • 134
    • 0019305589 scopus 로고
    • Niemann-Pick disease: A genetic model in Siamese cats
    • D.A. Wenger, M. Sattler, and T. Kudoh Niemann-Pick disease: a genetic model in Siamese cats Science 200 1980 1471 1473 (Pubitemid 10022197)
    • (1980) Science , vol.208 , Issue.4451 , pp. 1471-1473
    • Wenger, D.A.1    Sattler, M.2    Kudoh, T.3
  • 136
    • 77951893147 scopus 로고    scopus 로고
    • Acid sphingomyelinase, cell membranes and human disease: Lessons from Niemann-Pick disease
    • E.H. Schuchman Acid sphingomyelinase, cell membranes and human disease: lessons from Niemann-Pick disease FEBS Lett. 584 2010 1895 1900
    • (2010) FEBS Lett. , vol.584 , pp. 1895-1900
    • Schuchman, E.H.1
  • 137
    • 77952943373 scopus 로고    scopus 로고
    • Small molecule inhibitors of acid sphingomyelinase
    • C. Arenz Small molecule inhibitors of acid sphingomyelinase Cell. Physiol. Biochem. 26 2010 1 8
    • (2010) Cell. Physiol. Biochem. , vol.26 , pp. 1-8
    • Arenz, C.1
  • 138
    • 79958052481 scopus 로고    scopus 로고
    • Drug targeting of sphingolipid metabolism: Sphingomyelinases and ceramidases
    • D. Canals, D.M. Perry, R.W. Jenkins, and Y.A. Hannun Drug targeting of sphingolipid metabolism: sphingomyelinases and ceramidases Br. J. Pharmacol. 163 2010 694 712
    • (2010) Br. J. Pharmacol. , vol.163 , pp. 694-712
    • Canals, D.1    Perry, D.M.2    Jenkins, R.W.3    Hannun, Y.A.4
  • 139
    • 84878740987 scopus 로고    scopus 로고
    • Farber disease: Understanding a fatal childhood disorder and dissecting ceramide biology
    • M.S. Sands Farber disease: understanding a fatal childhood disorder and dissecting ceramide biology EMBO Mol. Med. 5 2013 799 801
    • (2013) EMBO Mol. Med. , vol.5 , pp. 799-801
    • Sands, M.S.1
  • 145
    • 84864399150 scopus 로고    scopus 로고
    • Construction of conditional acid ceramidase knockout mice and in vivo effects on oocyte development and fertility
    • E. Eliyahu, N. Shtraizent, R. Shalgi, and E.H. Schuchman Construction of conditional acid ceramidase knockout mice and in vivo effects on oocyte development and fertility Cell. Physiol. Biochem. 30 2012 735 748
    • (2012) Cell. Physiol. Biochem. , vol.30 , pp. 735-748
    • Eliyahu, E.1    Shtraizent, N.2    Shalgi, R.3    Schuchman, E.H.4
  • 146
    • 0035114217 scopus 로고    scopus 로고
    • Induction of apoptotic cell death and prevention of tumor growth by ceramide analogues in metastatic human colon cancer
    • M. Selzner, A. Bielawska, M.A. Morse, H.A. Rudiger, D. Sindram, Y.A. Hannun, and P.A. Clavien Induction of apoptotic cell death and prevention of tumor growth by ceramide analogues in metastatic human colon cancer Cancer Res. 61 2001 1233 1240 (Pubitemid 32174448)
    • (2001) Cancer Research , vol.61 , Issue.3 , pp. 1233-1240
    • Selzner, M.1    Bielawska, A.2    Morse, M.A.3    Rudiger, H.A.4    Sindram, D.5    Hannun, Y.A.6    Clavien, P.-A.7
  • 147
    • 46749113388 scopus 로고    scopus 로고
    • GM1 gangliosidosis: Review of clinical, molecular, and therapeutic aspects
    • N. Brunetti-Pierri, and F. Scaglia GM1 gangliosidosis: review of clinical, molecular, and therapeutic aspects Mol. Genet. Metab. 94 2008 391 396
    • (2008) Mol. Genet. Metab. , vol.94 , pp. 391-396
    • Brunetti-Pierri, N.1    Scaglia, F.2
  • 148
    • 84879143450 scopus 로고    scopus 로고
    • Gangliosides and gangliosidoses: Principles of molecular and metabolic pathogenesis
    • K. Sandhoff, and K. Harzer Gangliosides and gangliosidoses: principles of molecular and metabolic pathogenesis J. Neurosci. 33 2013 10195 10208
    • (2013) J. Neurosci. , vol.33 , pp. 10195-10208
    • Sandhoff, K.1    Harzer, K.2
  • 150
    • 0031046840 scopus 로고    scopus 로고
    • Generalized CNS disease and massive G(M1)-ganglioside accumulation in mice defective in lysosomal acid β-galactosidase
    • DOI 10.1093/hmg/6.2.205
    • C.N. Hahn, M. del Pilar Martin, M. Schroder, M.T. Vanier, Y. Hara, K. Suzuki, and A. d'Azzo Generalized CNS disease and massive GM1-ganglioside accumulation in mice defective in lysosomal acid beta-galactosidase Hum. Mol. Genet. 6 1997 205 211 (Pubitemid 27078076)
    • (1997) Human Molecular Genetics , vol.6 , Issue.2 , pp. 205-211
    • Hahn, C.N.1    Del Pilar Martin, M.2    Schroder, M.3    Vanier, M.T.4    Hara, Y.5    Suzuki, K.6    Suzuki, K.7    D'Azzo, A.8
  • 157
  • 161
    • 0031710552 scopus 로고    scopus 로고
    • β-galactosidase deficiency in a Korat cat: A new form of feline G(M1)-gangliosidosis
    • DOI 10.1007/s004010050899
    • R. De Maria, S. Divari, S. Bo, S. Sonnio, D. Lotti, M.T. Capucchio, and M. Castagnaro Beta-galactosidase deficiency in a Korat cat: a new form of feline GM1-gangliosidosis Acta Neuropathol. 96 1998 307 314 (Pubitemid 28419850)
    • (1998) Acta Neuropathologica , vol.96 , Issue.3 , pp. 307-314
    • De Maria, R.1    Divari, S.2    Bo, S.3    Sonnino, S.4    Lotti, D.5    Capucchio, M.T.6    Castagnaro, M.7
  • 162
    • 0035109239 scopus 로고    scopus 로고
    • M1 gangliosidosis
    • S.J. Ryder, and M.M. Simmons A lysosomal storage disease of Romney sheep that resembles human type 3 GM1 gangliosidosis Acta Neuropathol. 101 2001 225 228 (Pubitemid 32219755)
    • (2001) Acta Neuropathologica , vol.101 , Issue.3 , pp. 225-228
    • Ryder, S.J.1    Simmons, M.M.2
  • 163
    • 0026195082 scopus 로고
    • Similarity of lectin histochemistry of a lysosomal storage disease in a New Zealand lamb to that of ovine GM1 gangliosidosis
    • R.D. Murnane, W.J. Hartley, and D.J. Prieur Similarity of lectin histochemistry of a lysosomal storage disease in a New Zealand lamb to that of ovine GM1 gangliosidosis Vet. Pathol. 28 1991 332 335
    • (1991) Vet. Pathol. , vol.28 , pp. 332-335
    • Murnane, R.D.1    Hartley, W.J.2    Prieur, D.J.3
  • 164
  • 165
    • 0017770365 scopus 로고
    • Leukocyte beta-galactosidase activity in the diagnosis of bovine GM1 gangliosidosis
    • W.J. Donnelly, and M. Kelly Leukocyte beta-galactosidase activity in the diagnosis of bovine GM1 gangliosidosis Vet. Rec. 100 1977 318 319
    • (1977) Vet. Rec. , vol.100 , pp. 318-319
    • Donnelly, W.J.1    Kelly, M.2
  • 168
    • 0029025305 scopus 로고
    • Retarded bone formation in GM1-gangliosidosis: A study of the infantile form and comparison with two canine models
    • J. Alroy, K. Knowles, S.H. Schelling, E.M. Kaye, and A.E. Rosenberg Retarded bone formation in GM1-gangliosidosis: a study of the infantile form and comparison with two canine models Virchows Arch. 426 1995 141 148
    • (1995) Virchows Arch. , vol.426 , pp. 141-148
    • Alroy, J.1    Knowles, K.2    Schelling, S.H.3    Kaye, E.M.4    Rosenberg, A.E.5
  • 170
    • 54049118799 scopus 로고    scopus 로고
    • Insights into post-translational processing of beta-galactosidase in an animal model resembling late infantile human G-gangliosidosis
    • R. Kreutzer, M. Kreutzer, M.J. Propsting, A.C. Sewell, T. Leeb, H.Y. Naim, and W. Baumgartner Insights into post-translational processing of beta-galactosidase in an animal model resembling late infantile human G-gangliosidosis J. Cell. Mol. Med. 12 2008 1661 1671
    • (2008) J. Cell. Mol. Med. , vol.12 , pp. 1661-1671
    • Kreutzer, R.1    Kreutzer, M.2    Propsting, M.J.3    Sewell, A.C.4    Leeb, T.5    Naim, H.Y.6    Baumgartner, W.7
  • 171
    • 0021948476 scopus 로고
    • In vitro establishment of human fibroblasts of lysosomal diseases, G(M1)-gangliosidosis and Sandhoff disease, by transformation with origin-minus SV40 DNA
    • DOI 10.1007/BF01119596
    • T. Momoi, T. Furuya, Y. Suzuki, H. Sato, and N. Yamaguchi In vitro establishment of human fibroblasts of lysosomal diseases, GM1-gangliosidosis and Sandhoff disease, by transformation with origin-minus SV40 DNA Biosci. Rep. 5 1985 267 273 (Pubitemid 15117471)
    • (1985) Bioscience Reports , vol.5 , Issue.3 , pp. 267-273
    • Momoi, T.1    Furuya, T.2    Suzuki, Y.3
  • 173
    • 20844457438 scopus 로고    scopus 로고
    • 2 gangliosidosis
    • DOI 10.1001/archneur.62.6.989
    • L.C. Frey, S.P. Ringel, and C.M. Filley The natural history of cognitive dysfunction in late-onset GM2 gangliosidosis Arch. Neurol. 62 2005 989 994 (Pubitemid 40973462)
    • (2005) Archives of Neurology , vol.62 , Issue.6 , pp. 989-994
    • Frey, L.C.1    Ringel, S.P.2    Filley, C.M.3
  • 179
    • 0031820977 scopus 로고    scopus 로고
    • Glycosphingolipid degradation and animal models of GM2-gangliosidoses
    • DOI 10.1023/A:1005419122018
    • T. Kolter, and K. Sandhoff Glycosphingolipid degradation and animal models of GM2-gangliosidoses J. Inherit. Metab. Dis. 21 1998 548 563 (Pubitemid 28391507)
    • (1998) Journal of Inherited Metabolic Disease , vol.21 , Issue.5 , pp. 548-563
    • Kolter, T.1    Sandhoff, K.2
  • 182
    • 10744226948 scopus 로고    scopus 로고
    • Late onset Tay-Sachs disease in mice with targeted disruption of the Hexa gene: Behavioral changes and pathology of the central nervous system
    • DOI 10.1016/j.brainres.2003.11.067
    • E.I. Miklyaeva, W. Dong, A. Bureau, R. Fattahie, Y. Xu, M. Su, G.H. Fick, J.Q. Huang, S. Igdoura, N. Hanai, and R.A. Gravel Late onset Tay-Sachs disease in mice with targeted disruption of the Hexa gene: behavioral changes and pathology of the central nervous system Brain Res. 1001 2004 37 50 (Pubitemid 38221526)
    • (2004) Brain Research , vol.1001 , Issue.1-2 , pp. 37-50
    • Miklyaeva, E.I.1    Dong, W.2    Bureau, A.3    Fattahie, R.4    Xu, Y.5    Su, M.6    Fick, G.H.7    Huang, J.-Q.8    Igdoura, S.9    Hanai, N.10    Gravel, R.A.11
  • 185
    • 0023146781 scopus 로고
    • Biochemical basis of type AB G(M2) gangliosidosis in a Japanese Spaniel
    • DOI 10.1111/j.1471-4159.1987.tb05596.x
    • Y. Ishikawa, S.C. Li, P.A. Wood, and Y.T. Li Biochemical basis of type AB GM2 gangliosidosis in a Japanese spaniel J. Neurochem. 48 1987 860 864 (Pubitemid 17018720)
    • (1987) Journal of Neurochemistry , vol.48 , Issue.3 , pp. 860-864
    • Ishikawa, Y.1    Li, S.-C.2    Wood, P.A.3    Li, Y.-T.4
  • 189
    • 33845238476 scopus 로고    scopus 로고
    • Nonsense mutation of feline β-hexosaminidase β-subunit (HEXB) gene causing Sandhoff disease in a family of Japanese domestic cats
    • DOI 10.1016/j.rvsc.2006.05.007, PII S0034528806001147
    • Y. Kanae, D. Endoh, O. Yamato, D. Hayashi, S. Matsunaga, H. Ogawa, Y. Maede, and M. Hayashi Nonsense mutation of feline beta-hexosaminidase beta-subunit (HEXB) gene causing Sandhoff disease in a family of Japanese domestic cats Res. Vet. Sci. 82 2007 54 60 (Pubitemid 44858078)
    • (2007) Research in Veterinary Science , vol.82 , Issue.1 , pp. 54-60
    • Kanae, Y.1    Endoh, D.2    Yamato, O.3    Hayashi, D.4    Matsunaga, S.5    Ogawa, H.6    Maede, Y.7    Hayashi, M.8
  • 190
    • 0018120341 scopus 로고
    • 2- gangliosidosis
    • S.D. Kosanke, K.R. Pierce, and W.W. Bay Clinical and biochemical abnormalities in porcine GM2-gangliosidosis Vet. Pathol. 15 1978 685 699 (Pubitemid 9073013)
    • (1978) Veterinary Pathology , vol.15 , Issue.6 , pp. 685-699
    • Kosanke, S.D.1    Pierce, K.R.2    Bay, W.W.3
  • 192
    • 0032611409 scopus 로고    scopus 로고
    • Naturally occurring G(M2) gangliosidosis in two Muntjak deer with pathological and biochemical features of human classical Tay-Sachs disease (type B G(M2) gangliosidosis)
    • DOI 10.1007/s004010050955
    • J. Fox, Y.T. Li, G. Dawson, A. Alleman, J. Johnsrude, J. Schumacher, and B. Homer Naturally occurring GM2 gangliosidosis in two Muntjak deer with pathological and biochemical features of human classical Tay-Sachs disease (type B GM2 gangliosidosis) Acta Neuropathol. 97 1999 57 62 (Pubitemid 29132646)
    • (1999) Acta Neuropathologica , vol.97 , Issue.1 , pp. 57-62
    • Fox, J.1    Li, Y.-T.2    Dawson, G.3    Alleman, A.4    Johnsrude, J.5    Schumacher, J.6    Homer, B.7
  • 195
    • 0029634358 scopus 로고
    • Bone marrow transplantation for lysosomal diseases
    • S.U. Walkley, and K. Dobrenis Bone marrow transplantation for lysosomal diseases Lancet 345 1995 1382 1383
    • (1995) Lancet , vol.345 , pp. 1382-1383
    • Walkley, S.U.1    Dobrenis, K.2
  • 196
    • 0028336694 scopus 로고
    • Characterization of the molecular defect in a feline model for type II GM2-gangliosidosis (Sandhoff disease)
    • L.L. Muldoon, E.A. Neuwelt, M.A. Pagel, and D.L. Weiss Characterization of the molecular defect in a feline model for type II GM2-gangliosidosis (Sandhoff disease) Am J Pathol 144 1994 1109 1118
    • (1994) Am J Pathol , vol.144 , pp. 1109-1118
    • Muldoon, L.L.1    Neuwelt, E.A.2    Pagel, M.A.3    Weiss, D.L.4
  • 197


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