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Volumn 41, Issue 6, 2013, Pages 1562-1568

Metabolic and cellular bases of sphingolipidoses

Author keywords

Endocytosis; Intraendolysosomal vesicle; Lipid transfer protein; Sphingolipid; Sphingolipidosis

Indexed keywords

ESCRT PROTEIN; GANGLIOSIDE GM2; LIPID BINDING PROTEIN; MEMBRANE LIPID; SPHINGOLIPID; SPHINGOLIPID ACTIVATOR PROTEIN; SPHINGOLIPID ACTIVATOR PROTEIN 1; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE;

EID: 84887928747     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20130083     Document Type: Conference Paper
Times cited : (42)

References (52)
  • 1
    • 84896723076 scopus 로고    scopus 로고
    • The role of sphingolipid metabolism in cutaneous permeability barrier formation
    • doi: 10.1016/j.bbalip.2013.08.010
    • Breiden, B. and Sandhoff, K. (2013) The role of sphingolipid metabolism in cutaneous permeability barrier formation. Biochim. Biophys. Acta, doi: 10.1016/j.bbalip.2013.08.010
    • (2013) Biochim. Biophys. Acta
    • Breiden, B.1    Sandhoff, K.2
  • 2
    • 77951886452 scopus 로고    scopus 로고
    • Very long chain sphingolipids: Tissue expression, function and synthesis
    • Sandhoff, R. (2010) Very long chain sphingolipids: tissue expression, function and synthesis. FEBS Lett. 584, 1907-1913
    • (2010) FEBS Lett , vol.584 , pp. 1907-1913
    • Sandhoff, R.1
  • 4
    • 77953561361 scopus 로고    scopus 로고
    • Mammalian ceramide synthases
    • Levy, M. and Futerman, A.H. (2010) Mammalian ceramide synthases. IUBMB Life 62, 347-356
    • (2010) IUBMB Life , vol.62 , pp. 347-356
    • Levy, M.1    Futerman, A.H.2
  • 5
    • 0033152727 scopus 로고    scopus 로고
    • Sphingolipids: Their metabolic pathways and the pathobiochemistry of neurodegenerative diseases
    • Kolter, T. and Sandhoff, K. (1999) Sphingolipids: their metabolic pathways and the pathobiochemistry of neurodegenerative diseases. Angew. Chem. Int. Ed. 38, 1532-1568
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 1532-1568
    • Kolter, T.1    Sandhoff, K.2
  • 6
    • 0037135608 scopus 로고    scopus 로고
    • Combinatorial ganglioside biosynthesis
    • Kolter, T., Proia, R.L. and Sandhoff, K. (2002) Combinatorial ganglioside biosynthesis. J. Biol. Chem. 277, 25859-25862
    • (2002) J. Biol. Chem. , vol.277 , pp. 25859-25862
    • Kolter, T.1    Proia, R.L.2    Sandhoff, K.3
  • 7
    • 0038100164 scopus 로고    scopus 로고
    • Glycosphingolipid functions: Insights from engineered mouse models
    • Proia, R.L. (2003) Glycosphingolipid functions: insights from engineered mouse models. Philos. Trans. R. Soc. London Ser. B 358, 879-883
    • (2003) Philos. Trans. R. Soc. London Ser. B , vol.358 , pp. 879-883
    • Proia, R.L.1
  • 11
    • 33749062163 scopus 로고    scopus 로고
    • Genetic diseases of sphingolipid metabolism: Pathological mechanisms and therapeutic options
    • Kacher, Y. and Futerman, A.H. (2006) Genetic diseases of sphingolipid metabolism: pathological mechanisms and therapeutic options. FEBS Lett. 580, 5510-5517
    • (2006) FEBS Lett , vol.580 , pp. 5510-5517
    • Kacher, Y.1    Futerman, A.H.2
  • 12
    • 33845343984 scopus 로고    scopus 로고
    • Sphingolipid metabolism diseases
    • Kolter, T. and Sandhoff, K. (2006) Sphingolipid metabolism diseases. Biochim. Biophys. Acta 1758, 2057-2079
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 2057-2079
    • Kolter, T.1    Sandhoff, K.2
  • 13
    • 77954225471 scopus 로고    scopus 로고
    • Common and uncommon pathogenic cascades in lysosomal storage diseases
    • Vitner, E.B., Platt, F.M. and Futerman, A.H. (2010) Common and uncommon pathogenic cascades in lysosomal storage diseases. J. Biol. Chem. 285, 20423-20427
    • (2010) J. Biol. Chem. , vol.285 , pp. 20423-20427
    • Vitner, E.B.1    Platt, F.M.2    Futerman, A.H.3
  • 15
    • 84862768394 scopus 로고    scopus 로고
    • Autophagy proteins in macroendocytic engulfment
    • Florey, O. and Overholtzer, M. (2012) Autophagy proteins in macroendocytic engulfment. Trends Cell Biol. 22, 374-380
    • (2012) Trends Cell Biol , vol.22 , pp. 374-380
    • Florey, O.1    Overholtzer, M.2
  • 16
    • 25444443570 scopus 로고    scopus 로고
    • Principles of lysosomal membrane digestion: Stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids
    • Kolter, T. and Sandhoff, K. (2005) Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids. Annu. Rev. Cell Dev. Biol. 21, 81-103
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 81-103
    • Kolter, T.1    Sandhoff, K.2
  • 17
    • 0343052042 scopus 로고    scopus 로고
    • Accumulation of sphingolipids in SAP-precursor (prosaposin)-deficient fibroblasts occurs as intralysosomal membrane structures and can be completely reversed by treatment with human SAP-precursor
    • Burkhardt, J.K., Huttler, S., Klein, A., Mobius, W., Habermann, A., Griffiths, G. and Sandhoff, K. (1997) Accumulation of sphingolipids in SAP-precursor (prosaposin)-deficient fibroblasts occurs as intralysosomal membrane structures and can be completely reversed by treatment with human SAP-precursor. Eur. J. Cell Biol. 73, 10-18
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 10-18
    • Burkhardt, J.K.1    Huttler, S.2    Klein, A.3    Mobius, W.4    Habermann, A.5    Griffiths, G.6    Sandhoff, K.7
  • 18
    • 0032799717 scopus 로고    scopus 로고
    • Intracellular distribution of a biotin-labeled ganglioside, GM1, by immunoelectron microscopy after endocytosis in fibroblasts
    • Mobius, W., Herzog, V., Sandhoff, K. and Schwarzmann, G. (1999) Intracellular distribution of a biotin-labeled ganglioside, GM1, by immunoelectron microscopy after endocytosis in fibroblasts. J. Histochem. Cytochem. 47, 1005-1014
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 1005-1014
    • Mobius, W.1    Herzog, V.2    Sandhoff, K.3    Schwarzmann, G.4
  • 19
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • Wollert, T. and Hurley, J.H. (2010) Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature 464, 864-869
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 20
    • 79851476846 scopus 로고    scopus 로고
    • Regulation of the NPC2 protein-mediated cholesterol trafficking by membrane lipids
    • Gallala, H.D., Breiden, B. and Sandhoff, K. (2011) Regulation of the NPC2 protein-mediated cholesterol trafficking by membrane lipids. J. Neurochem. 116, 702-707
    • (2011) J. Neurochem. , vol.116 , pp. 702-707
    • Gallala, H.D.1    Breiden, B.2    Sandhoff, K.3
  • 22
    • 80755163636 scopus 로고    scopus 로고
    • Biological function of the cellular lipid BMP: BMP as a key activator for cholesterol sorting and membrane digestion
    • Gallala, H. and Sandhoff, K. (2011) Biological function of the cellular lipid BMP: BMP as a key activator for cholesterol sorting and membrane digestion. Neurochem. Res. 36, 1594-1600
    • (2011) Neurochem. Res. , vol.36 , pp. 1594-1600
    • Gallala, H.1    Sandhoff, K.2
  • 23
    • 84869223682 scopus 로고    scopus 로고
    • Sensitivity to lysosome-dependent cell death is directly regulated by lysosomal cholesterol content
    • Appelqvist, H., Sandin, L., Bjornstrom, K., Saftig, P., Garner, B., Ollinger, K. and Kagedal, K. (2012) Sensitivity to lysosome-dependent cell death is directly regulated by lysosomal cholesterol content. PLoS ONE 7, e50262
    • (2012) PLoS ONE , vol.7
    • Appelqvist, H.1    Sandin, L.2    Bjornstrom, K.3    Saftig, P.4    Garner, B.5    Ollinger, K.6    Kagedal, K.7
  • 24
    • 0000223691 scopus 로고    scopus 로고
    • Interaction of the GM2-activator protein with phospholipid-ganglioside bilayer membranes and with monolayers at the air-water interface
    • Giehl, A., Lemm, T., Bartelsen, O., Sandhoff, K. and Blume, A. (1999) Interaction of the GM2-activator protein with phospholipid-ganglioside bilayer membranes and with monolayers at the air-water interface. Eur. J. Biochem. 261, 650-658
    • (1999) Eur. J. Biochem. , vol.261 , pp. 650-658
    • Giehl, A.1    Lemm, T.2    Bartelsen, O.3    Sandhoff, K.4    Blume, A.5
  • 25
    • 77951924919 scopus 로고    scopus 로고
    • Lysosomal degradation of membrane lipids
    • Kolter, T. and Sandhoff, K. (2010) Lysosomal degradation of membrane lipids. FEBS Lett. 584, 1700-1712
    • (2010) FEBS Lett , vol.584 , pp. 1700-1712
    • Kolter, T.1    Sandhoff, K.2
  • 26
    • 29244448306 scopus 로고    scopus 로고
    • Lipid-binding proteins in membrane digestion, antigen presentation, and antimicrobial defense
    • Kolter, T., Winau, F., Schaible, U.E., Leippe, M. and Sandhoff, K. (2005) Lipid-binding proteins in membrane digestion, antigen presentation, and antimicrobial defense. J. Biol. Chem. 280, 41125-41128
    • (2005) J. Biol. Chem. , vol.280 , pp. 41125-41128
    • Kolter, T.1    Winau, F.2    Schaible, U.E.3    Leippe, M.4    Sandhoff, K.5
  • 28
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • Kwon, H.J., Abi-Mosleh, L., Wang, M.L., Deisenhofer, J., Goldstein, J.L., Brown, M.S. and Infante, R.E. (2009) Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol. Cell 137, 1213-1224
    • (2009) Cell , vol.137 , pp. 1213-1224
    • Kwon, H.J.1    Abi-Mosleh, L.2    Wang, M.L.3    Deisenhofer, J.4    Goldstein, J.L.5    Brown, M.S.6    Infante, R.E.7
  • 29
    • 67649255316 scopus 로고    scopus 로고
    • Niemann-Pick C2 (NPC2) and intracellular cholesterol trafficking
    • Storch, J. and Xu, Z. (2009) Niemann-Pick C2 (NPC2) and intracellular cholesterol trafficking. Biochim. Biophys. Acta 1791, 671-678
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 671-678
    • Storch, J.1    Xu, Z.2
  • 31
    • 0020658595 scopus 로고
    • Biochemical studies in Niemann-Pick disease. I. Major sphingolipids of liver and spleen
    • Vanier, M. (1983) Biochemical studies in Niemann-Pick disease. I. Major sphingolipids of liver and spleen. Biochim. Biophys. Acta 750, 178-184
    • (1983) Biochim. Biophys. Acta , vol.750 , pp. 178-184
    • Vanier, M.1
  • 32
    • 80052510182 scopus 로고    scopus 로고
    • Endosomal/lysosomal processing of gangliosides affects neuronal cholesterol sequestration in Niemann-Pick disease type C
    • Zhou, S., Davidson, C., McGlynn, R., Stephney, G., Dobrenis, K., Vanier, M.T. and Walkley, S.U. (2011) Endosomal/lysosomal processing of gangliosides affects neuronal cholesterol sequestration in Niemann-Pick disease type C. Am. J. Pathol. 179, 890-902
    • (2011) Am. J. Pathol. , vol.179 , pp. 890-902
    • Zhou, S.1    Davidson, C.2    McGlynn, R.3    Stephney, G.4    Dobrenis, K.5    Vanier, M.T.6    Walkley, S.U.7
  • 33
    • 33845938485 scopus 로고    scopus 로고
    • Saposin A mobilizes lipids from low cholesterol and high bis(monoacylglycerol)phosphate-containing membranes: Patient variant saposin A lacks lipid extraction capacity
    • Locatelli-Hoops, S., Remmel, N., Klingenstein, R., Breiden, B., Rossocha, M., Schoeniger, M., Koenigs, C., Saenger, W. and Sandhoff, K. (2006) Saposin A mobilizes lipids from low cholesterol and high bis(monoacylglycerol)phosphate- containing membranes: patient variant saposin A lacks lipid extraction capacity. J. Biol. Chem. 281, 32451-32460
    • (2006) J. Biol. Chem. , vol.281 , pp. 32451-32460
    • Locatelli-Hoops, S.1    Remmel, N.2    Klingenstein, R.3    Breiden, B.4    Rossocha, M.5    Schoeniger, M.6    Koenigs, C.7    Saenger, W.8    Sandhoff, K.9
  • 34
    • 34347405277 scopus 로고    scopus 로고
    • Saposin B mobilizes lipids from cholesterol-poor and bis(monoacylglycero) phosphate-rich membranes at acidic pH: Unglycosylated patient variant saposin B lacks lipid-extraction capacity
    • Remmel, N., Locatelli-Hoops, S., Breiden, B., Schwarzmann, G. and Sandhoff, K. (2007) Saposin B mobilizes lipids from cholesterol-poor and bis(monoacylglycero)phosphate-rich membranes at acidic pH: unglycosylated patient variant saposin B lacks lipid-extraction capacity. FEBS J. 274, 3405-3420
    • (2007) FEBS J , vol.274 , pp. 3405-3420
    • Remmel, N.1    Locatelli-Hoops, S.2    Breiden, B.3    Schwarzmann, G.4    Sandhoff, K.5
  • 35
    • 0020686110 scopus 로고
    • Variant of GM2-gangliosidosis with hexosaminidase A having a severely changed substrate specificity
    • Kytzia, H.J., Hinrichs, U., Maire, I., Suzuki, K. and Sandhoff, K. (1983) Variant of GM2-gangliosidosis with hexosaminidase A having a severely changed substrate specificity. EMBO J. 2, 1201-1205
    • (1983) EMBO J , vol.2 , pp. 1201-1205
    • Kytzia, H.J.1    Hinrichs, U.2    Maire, I.3    Suzuki, K.4    Sandhoff, K.5
  • 38
    • 0021026543 scopus 로고
    • Activator protein for the degradation of globotriaosylceramide by human α-galactosidase
    • Gartner, S., Conzelmann, E. and Sandhoff, K. (1983) Activator protein for the degradation of globotriaosylceramide by human α-galactosidase. J. Biol. Chem. 258, 12378-12385
    • (1983) J. Biol. Chem. , vol.258 , pp. 12378-12385
    • Gartner, S.1    Conzelmann, E.2    Sandhoff, K.3
  • 40
    • 0023919106 scopus 로고
    • Characterization of a nonspecific activator protein for the enzymatic hydrolysis of glycolipids
    • Li, S.C., Sonnino, S., Tettamanti, G. and Li, Y.T. (1988) Characterization of a nonspecific activator protein for the enzymatic hydrolysis of glycolipids. J. Biol. Chem. 263, 6588-6591
    • (1988) J. Biol. Chem. , vol.263 , pp. 6588-6591
    • Li, S.C.1    Sonnino, S.2    Tettamanti, G.3    Li, Y.T.4
  • 41
    • 1442264832 scopus 로고    scopus 로고
    • Expression of the GM2-activator protein in the methylotrophic yeast Pichia pastoris, purification, isotopic labeling, and biophysical characterization
    • Wendeler, M., Hoernschemeyer, J., John, M., Werth, N., Schoeniger, M., Lemm, T., Hartmann, R., Kessler, H. and Sandhoff, K. (2004) Expression of the GM2-activator protein in the methylotrophic yeast Pichia pastoris, purification, isotopic labeling, and biophysical characterization. Protein Expression Purif. 34, 147-157
    • (2004) Protein Expression Purif , vol.34 , pp. 147-157
    • Wendeler, M.1    Hoernschemeyer, J.2    John, M.3    Werth, N.4    Schoeniger, M.5    Lemm, T.6    Hartmann, R.7    Kessler, H.8    Sandhoff, K.9
  • 42
    • 0034680858 scopus 로고    scopus 로고
    • Degradation of membrane-bound ganglioside GM1: Stimulation by bis(monoacylglycero)phosphate and the activator proteins SAP-B and GM2-AP
    • Wilkening, G., Linke, T., Uhlhorn-Dierks, G. and Sandhoff, K. (2000) Degradation of membrane-bound ganglioside GM1: stimulation by bis(monoacylglycero)phosphate and the activator proteins SAP-B and GM2-AP. J. Biol. Chem. 275, 35814-35819
    • (2000) J. Biol. Chem. , vol.275 , pp. 35814-35819
    • Wilkening, G.1    Linke, T.2    Uhlhorn-Dierks, G.3    Sandhoff, K.4
  • 43
    • 0035918181 scopus 로고    scopus 로고
    • Degradation of membrane-bound ganglioside GM2 by β-hexosaminidase A: Stimulation by GM2 activator protein and lysosomal lipids
    • Werth, N., Schuette, C.G., Wilkening, G., Lemm, T. and Sandhoff, K. (2001) Degradation of membrane-bound ganglioside GM2 by β-hexosaminidase A: stimulation by GM2 activator protein and lysosomal lipids. J. Biol. Chem. 276, 12685-12690
    • (2001) J. Biol. Chem. , vol.276 , pp. 12685-12690
    • Werth, N.1    Schuette, C.G.2    Wilkening, G.3    Lemm, T.4    Sandhoff, K.5
  • 44
    • 0032514902 scopus 로고    scopus 로고
    • Lysosomal degradation on vesicular membrane surfaces: Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators
    • Wilkening, G., Linke, T. and Sandhoff, K. (1998) Lysosomal degradation on vesicular membrane surfaces: enhanced glucosylceramide degradation by lysosomal anionic lipids and activators. J. Biol. Chem. 273, 30271-30278
    • (1998) J. Biol. Chem. , vol.273 , pp. 30271-30278
    • Wilkening, G.1    Linke, T.2    Sandhoff, K.3
  • 45
    • 0035937146 scopus 로고    scopus 로고
    • Interfacial regulation of acid ceramidase activity: Stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins
    • Linke, T., Wilkening, G., Sadeghlar, F., Mozcall, H., Bernardo, K., Schuchman, E. and Sandhoff, K. (2001) Interfacial regulation of acid ceramidase activity: stimulation of ceramide degradation by lysosomal lipids and sphingolipid activator proteins. J. Biol. Chem. 276, 5760-5768
    • (2001) J. Biol. Chem. , vol.276 , pp. 5760-5768
    • Linke, T.1    Wilkening, G.2    Sadeghlar, F.3    Mozcall, H.4    Bernardo, K.5    Schuchman, E.6    Sandhoff, K.7
  • 46
    • 84871368269 scopus 로고    scopus 로고
    • My journey into the world of sphingolipids and sphingolipidoses
    • Sandhoff, K. (2012) My journey into the world of sphingolipids and sphingolipidoses. Proc. Jpn. Acad., Ser. B 88, 554-582
    • (2012) Proc. Jpn. Acad., Ser. B , vol.88 , pp. 554-582
    • Sandhoff, K.1
  • 47
    • 0021085107 scopus 로고
    • Partial enzyme deficiencies: Residual activities and the development of neurological disorders
    • Conzelmann, E. and Sandhoff, K. (1983) Partial enzyme deficiencies: residual activities and the development of neurological disorders. Dev. Neurosci. 6, 58-71
    • (1983) Dev. Neurosci. , vol.6 , pp. 58-71
    • Conzelmann, E.1    Sandhoff, K.2
  • 48
    • 0026572112 scopus 로고
    • Quantitative correlation between the residual activity of β-hexosaminidase A and arylsulfatase A and the severity of the resulting lysosomal storage disease
    • Leinekugel, P., Michel, S., Conzelmann, E. and Sandhoff, K. (1992) Quantitative correlation between the residual activity of β-hexosaminidase A and arylsulfatase A and the severity of the resulting lysosomal storage disease. Hum. Genet. 88, 513-523
    • (1992) Hum. Genet. , vol.88 , pp. 513-523
    • Leinekugel, P.1    Michel, S.2    Conzelmann, E.3    Sandhoff, K.4
  • 49
    • 0027932927 scopus 로고
    • Accurate differentiation of neuronopathic and nonneuronopathic forms of Niemann-Pick disease by evaluation of the effective residual lysosomal sphingomyelinase activity in intact cells
    • Graber, D., Salvayre, R. and Levade, T. (1994) Accurate differentiation of neuronopathic and nonneuronopathic forms of Niemann-Pick disease by evaluation of the effective residual lysosomal sphingomyelinase activity in intact cells. J. Neurochem. 63, 1060-1068
    • (1994) J. Neurochem. , vol.63 , pp. 1060-1068
    • Graber, D.1    Salvayre, R.2    Levade, T.3
  • 50
    • 0027996444 scopus 로고
    • Analysis of glucocerebrosidase activity using N-(1-[14C]hexanoyl)-d- erythroglucosylsphingosine demonstrates a correlation between levels of residual enzyme activity and the type of Gaucher disease
    • Meivar-Levy, I., Horowitz, M. and Futerman, A.H. (1994) Analysis of glucocerebrosidase activity using N-(1-[14C]hexanoyl)-d- erythroglucosylsphingosine demonstrates a correlation between levels of residual enzyme activity and the type of Gaucher disease. Biochem. J. 303, 377-382
    • (1994) Biochem. J. , vol.303 , pp. 377-382
    • Meivar-Levy, I.1    Horowitz, M.2    Futerman, A.H.3
  • 51
    • 0042667012 scopus 로고    scopus 로고
    • Structural analysis of lipid complexes of GM2-activator protein
    • Wright, C.S., Zhao, Q. and Rastinejad, F. (2003) Structural analysis of lipid complexes of GM2-activator protein. J. Mol. Biol. 331, 951-964
    • (2003) J. Mol. Biol. , vol.331 , pp. 951-964
    • Wright, C.S.1    Zhao, Q.2    Rastinejad, F.3


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