메뉴 건너뛰기




Volumn 358, Issue 1433, 2003, Pages 847-861

Biosynthesis and degradation of mammalian glycosphingolipids

Author keywords

Biosynthesis; Glycolipids; Lysosomes; Sphingolipid; Sphingolipid activator proteins

Indexed keywords

LIPID;

EID: 0037762571     PISSN: 09628436     EISSN: None     Source Type: Journal    
DOI: 10.1098/rstb.2003.1265     Document Type: Conference Paper
Times cited : (159)

References (186)
  • 1
    • 0033785675 scopus 로고    scopus 로고
    • Evidence supporting a late Golgi location for lactosylceramide to ganglioside GM3 conversion
    • Allende, M. L., Li, J., Darling, D. S., Worth, C. A. & Young Jr, W. W. 2000 Evidence supporting a late Golgi location for lactosylceramide to ganglioside GM3 conversion. Glycobiol. 10, 1025-1032.
    • (2000) Glycobiol. , vol.10 , pp. 1025-1032
    • Allende, M.L.1    Li, J.2    Darling, D.S.3    Worth, C.A.4    Young W.W., Jr.5
  • 2
    • 0029953488 scopus 로고    scopus 로고
    • Transacylase and phospholipases in the synthesis of bis(monoacylglycero)phosphate
    • Amidon, B., Brown, A. & Waite, M. 1996 Transacylase and phospholipases in the synthesis of bis(monoacylglycero)phosphate. Biochemistry 35, 13 995-14 002.
    • (1996) Biochemistry , vol.35 , pp. 13995-14002
    • Amidon, B.1    Brown, A.2    Waite, M.3
  • 4
    • 0019513677 scopus 로고
    • Mechanism of activation of glucocerebrosidase by co-β-glucosidase (glucosidase activator protein)
    • Berent, S. L. & Radin, N. S. 1981 Mechanism of activation of glucocerebrosidase by co-β-glucosidase (glucosidase activator protein). Biochim. Biophys. Acta 664, 572-582.
    • (1981) Biochim. Biophys. Acta , vol.664 , pp. 572-582
    • Berent, S.L.1    Radin, N.S.2
  • 5
    • 0033040971 scopus 로고    scopus 로고
    • Multi-enzyme kinetic analysis of glycolipid biosynthesis
    • Bieberich, E. & Yu, R. K. 1999 Multi-enzyme kinetic analysis of glycolipid biosynthesis. Biochim. Biophys. Acta 1432, 113-124.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 113-124
    • Bieberich, E.1    Yu, R.K.2
  • 6
    • 0029851157 scopus 로고    scopus 로고
    • Functional breakdown of the lipid bilayer of the myelin membrane in central and peripheral nervous system by disrupted galactocerebroside synthesis
    • Bosio, A., Binczek, E. & Stoffel, W. 1996 Functional breakdown of the lipid bilayer of the myelin membrane in central and peripheral nervous system by disrupted galactocerebroside synthesis. Proc. Natl Acad. Sci. USA 93, 13 280-13 285.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13280-13285
    • Bosio, A.1    Binczek, E.2    Stoffel, W.3
  • 7
    • 0027186175 scopus 로고
    • Prosaposin deficiency: Further characterization of the sphingolipid activator protein-deficient sibs. Multiple glycolipid elevations (including lactosylceramidosis), partial enzyme deficiencies and ultrastructure of the skin in this generalized sphingolipid storage disease
    • Bradova, V., Smid, F., Ulrich-Bott, B., Roggendorf, W., Paton, B. C. & Harzer, K. 1993 Prosaposin deficiency: further characterization of the sphingolipid activator protein-deficient sibs. Multiple glycolipid elevations (including lactosylceramidosis), partial enzyme deficiencies and ultrastructure of the skin in this generalized sphingolipid storage disease. Hum. Genet. 92, 143-152.
    • (1993) Hum. Genet. , vol.92 , pp. 143-152
    • Bradova, V.1    Smid, F.2    Ulrich-Bott, B.3    Roggendorf, W.4    Paton, B.C.5    Harzer, K.6
  • 8
    • 0014429876 scopus 로고
    • Biosynthesis of sphingolipid bases. II. Keto intermediates in synthesis of sphingosine and dihydrosphingosine by cell-free extracts of Hansenula ciferri
    • Braun, P. E. & Snell, E. E. 1968 Biosynthesis of sphingolipid bases. II. Keto intermediates in synthesis of sphingosine and dihydrosphingosine by cell-free extracts of Hansenula ciferri. J. Biol. Chem. 243, 3775-3783.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3775-3783
    • Braun, P.E.1    Snell, E.E.2
  • 9
    • 0017575390 scopus 로고
    • Subcellular distributions of lipids in cultured BHK cells: Evidence for the enrichment of lysobisphosphatidic acid and neutral lipids in lysosomes
    • Brotherus, J. & Renkonen, O. 1977 Subcellular distributions of lipids in cultured BHK cells: evidence for the enrichment of lysobisphosphatidic acid and neutral lipids in lysosomes. J. Lipid Res. 18, 191-202.
    • (1977) J. Lipid Res. , vol.18 , pp. 191-202
    • Brotherus, J.1    Renkonen, O.2
  • 10
    • 0343052042 scopus 로고    scopus 로고
    • Accumulation of sphingolipids in SAP-precursor (prosaposin) deficient fibroblasts occurs within lysosomes and can be completely reversed by treatment with human SAP-precursor
    • Burkhardt, J. K., Hüttler, S., Klein, A. M., Möbius, W., Habermann, A., Griffiths, G. & Sandhoff, K. 1997 Accumulation of sphingolipids in SAP-precursor (prosaposin) deficient fibroblasts occurs within lysosomes 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    Hüttler, S.2    Klein, A.M.3    Möbius, W.4    Habermann, A.5    Griffiths, G.6    Sandhoff, K.7
  • 11
    • 0024245391 scopus 로고
    • Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2
    • Carlsson, S. R., Roth, J., Piller, F. & Fukuda, M. 1988 Isolation and characterization of human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. J. Biol. Chem. 263, 18 911-18 919.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18911-18919
    • Carlsson, S.R.1    Roth, J.2    Piller, F.3    Fukuda, M.4
  • 12
    • 0033673678 scopus 로고    scopus 로고
    • A functional role for complex gangliosides: Motor deficits in GM2/GD2 synthase knockout mice
    • Chiavegatto, S., Sun, J., Nelson, R. J. & Schnaar, R. L. 2000 A functional role for complex gangliosides: motor deficits in GM2/GD2 synthase knockout mice. Exp. Neurol. 166, 227-234.
    • (2000) Exp. Neurol. , vol.166 , pp. 227-234
    • Chiavegatto, S.1    Sun, J.2    Nelson, R.J.3    Schnaar, R.L.4
  • 13
    • 0023886858 scopus 로고
    • The biological role of dolichol
    • Chojnacki, T. & Dallner, G. 1988 The biological role of dolichol. Biochem. J. 251, 1-9.
    • (1988) Biochem. J. , vol.251 , pp. 1-9
    • Chojnacki, T.1    Dallner, G.2
  • 14
    • 0022782844 scopus 로고
    • Immunochemical characterization of two activator proteins stimulating enzymic sphingomyelin degradation in vitro. Absence of one of them in a human Gaucher disease variant
    • Christomanou, H., Aignesberg, A. & Linke, R. P. 1986 Immunochemical characterization of two activator proteins stimulating enzymic sphingomyelin degradation in vitro. Absence of one of them in a human Gaucher disease variant. Biol. Chem. Hoppe-Seyler 367, 879-890.
    • (1986) Biol. Chem. Hoppe-Seyler , vol.367 , pp. 879-890
    • Christomanou, H.1    Aignesberg, A.2    Linke, R.P.3
  • 16
    • 0030602822 scopus 로고    scopus 로고
    • Myelination in the absence of galactocerebroside and sulfatide: Normal structure with abnormal function and regional instability
    • Coetzee, T., Fujita, N., Dupree, J., Shi, R., Blight, A., Suzuki, K., Suzuki, K. & Popko, B. 1996 Myelination in the absence of galactocerebroside and sulfatide: normal structure with abnormal function and regional instability. Cell 86, 209-219.
    • (1996) Cell , vol.86 , pp. 209-219
    • Coetzee, T.1    Fujita, N.2    Dupree, J.3    Shi, R.4    Blight, A.5    Suzuki, K.6    Suzuki, K.7    Popko, B.8
  • 17
    • 2642688117 scopus 로고
    • AB variant of infantile GM2-gangliosidosis: Deficiency of a factor necessary for stimulation of hexosaminidase A-catalyzed degradation of ganglioside GM2 and glycolipid GA2
    • Conzelmann, E. & Sandhoff, K. 1978 AB variant of infantile GM2-gangliosidosis: deficiency of a factor necessary for stimulation of hexosaminidase A-catalyzed degradation of ganglioside GM2 and glycolipid GA2. Proc. Natl Acad. Sci. USA 75, 3979-3983.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3979-3983
    • Conzelmann, E.1    Sandhoff, K.2
  • 18
    • 0018567163 scopus 로고
    • Purification and characterization of an activator protein for the degradation of glycolipids GM2 and GA2 by hexosaminidase A
    • Conzelmann, E. & Sandhoff, K. 1979 Purification and characterization of an activator protein for the degradation of glycolipids GM2 and GA2 by hexosaminidase A. Hoppe-Seyler Z. Physiol. Chem. 360, 1837-1849.
    • (1979) Hoppe-Seyler Z. Physiol. Chem. , vol.360 , pp. 1837-1849
    • Conzelmann, E.1    Sandhoff, K.2
  • 19
    • 0020321725 scopus 로고
    • Complexing of glycolipids and their transfer between membranes by the activator protein for degradation of lysosomal ganglioside GM2
    • Conzelmann, E., Burg, J., Stephan, G. & Sandhoff, K. 1982 Complexing of glycolipids and their transfer between membranes by the activator protein for degradation of lysosomal ganglioside GM2. Eur. J. Biochem. 123, 455-466.
    • (1982) Eur. J. Biochem. , vol.123 , pp. 455-466
    • Conzelmann, E.1    Burg, J.2    Stephan, G.3    Sandhoff, K.4
  • 20
    • 0022452207 scopus 로고
    • Topology of glucosylceramide synthesis in Golgi membranes from porcine sub-maxillary glands
    • Coste, H., Martel, M.-B. & Got, R. 1986 Topology of glucosylceramide synthesis in Golgi membranes from porcine sub-maxillary glands. Biochim. Biophys. Acta 858, 6-12.
    • (1986) Biochim. Biophys. Acta , vol.858 , pp. 6-12
    • Coste, H.1    Martel, M.-B.2    Got, R.3
  • 21
    • 0031662853 scopus 로고    scopus 로고
    • Sphingolipid functions in Saccharomyces cerevisiae: Comparison to mammals
    • Dickson, R. C. 1998 Sphingolipid functions in Saccharomyces cerevisiae: comparison to mammals. A. Rev. Biochem. 67, 27-48.
    • (1998) A. Rev. Biochem. , vol.67 , pp. 27-48
    • Dickson, R.C.1
  • 23
    • 0032970258 scopus 로고    scopus 로고
    • Accumulation of protein-bound epidermal glucosylceramides in β-glucocerebrosidase deficient type 2 Gaucher mice
    • Doering, T., Proia, R. L. & Sandhoff, K. 1999b Accumulation of protein-bound epidermal glucosylceramides in β-glucocerebrosidase deficient type 2 Gaucher mice. FEBS Lett. 447, 167-170.
    • (1999) FEBS Lett. , vol.447 , pp. 167-170
    • Doering, T.1    Proia, R.L.2    Sandhoff, K.3
  • 24
    • 0025824346 scopus 로고
    • Human acid β-glucosidase. Use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites
    • Fabbro, D. & Grabowski, D. A. 1991 Human acid β-glucosidase. Use of inhibitory and activating monoclonal antibodies to investigate the enzyme's catalytic mechanism and saposin A and C binding sites. J. Biol. Chem. 266, 15 021-15 027.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15021-15027
    • Fabbro, D.1    Grabowski, D.A.2
  • 25
    • 0026697936 scopus 로고
    • Degradation of gangliosides by the lysosomal sialidase requires an activator protein
    • Fingerhut, R., Van der Horst, G. T., Verheijen, F. W. & Conzelmann, E. 1992 Degradation of gangliosides by the lysosomal sialidase requires an activator protein. Eur. J. Biochem. 208, 623-629.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 623-629
    • Fingerhut, R.1    Van Der Horst, G.T.2    Verheijen, F.W.3    Conzelmann, E.4
  • 26
    • 0016734877 scopus 로고
    • The activator of cerebroside sulphatase. Purification from human liver and identification as a protein
    • Fischer, G. & Jatzkewitz, H. 1975 The activator of cerebroside sulphatase. Purification from human liver and identification as a protein. Hoppe-Seyler Z. Physiol. Chem. 356, 605-613.
    • (1975) Hoppe-Seyler Z. Physiol. Chem. , vol.356 , pp. 605-613
    • Fischer, G.1    Jatzkewitz, H.2
  • 27
    • 0034725645 scopus 로고    scopus 로고
    • Requirement of seminolipid in spermatogenesis revealed by UDP-galactose: Ceramide galactosyltransferase-deficient mice
    • Fujimoto, H., Tadano-Aritomi, K., Tokumasu, A., Ito, K., Hikita, T., Suzuki, K. & Ishizuka, I. 2000 Requirement of seminolipid in spermatogenesis revealed by UDP-galactose: ceramide galactosyltransferase-deficient mice. J. Biol. Chem. 275, 22 623-22 626.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22623-22626
    • Fujimoto, H.1    Tadano-Aritomi, K.2    Tokumasu, A.3    Ito, K.4    Hikita, T.5    Suzuki, K.6    Ishizuka, I.7
  • 28
    • 0026747197 scopus 로고
    • Activator proteins and topology of lysosomal sphingolipid catabolism
    • Fürst, W. & Sandhoff, K. 1992 Activator proteins and topology of lysosomal sphingolipid catabolism. Biochim. Biophys. Acta 1126, 1-16.
    • (1992) Biochim. Biophys. Acta , vol.1126 , pp. 1-16
    • Fürst, W.1    Sandhoff, K.2
  • 29
    • 0023947493 scopus 로고
    • The precursor of sulfatide activator protein is processed to three different proteins
    • Fürst, W., Machleidt, W. & Sandhoff, K. 1988 The precursor of sulfatide activator protein is processed to three different proteins. Biol. Chem. Hoppe-Seyler 369, 317-328.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 317-328
    • Fürst, W.1    Machleidt, W.2    Sandhoff, K.3
  • 30
    • 0025118444 scopus 로고
    • The complete amino-acid sequences of human ganglioside GM2-activator protein and cerebroside sulfate activator protein
    • Fürst, W., Schubert, J., Machleidt, W., Meyer, E. H. & Sandhoff, K. 1990 The complete amino-acid sequences of human ganglioside GM2-activator protein and cerebroside sulfate activator protein. Eur. J. Biochem. 192, 709-714.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 709-714
    • Fürst, W.1    Schubert, J.2    Machleidt, W.3    Meyer, E.H.4    Sandhoff, K.5
  • 31
    • 0035895782 scopus 로고    scopus 로고
    • Novel functions of complex carbohydrates elucidated by the mutant mice of glycosyltransferase genes
    • Furukawa, K., Takamiya, K., Okada, M., Inoue, M., Fukumoto, S. & Furukawa, K. 2001 Novel functions of complex carbohydrates elucidated by the mutant mice of glycosyltransferase genes. Biochim. Biophys. Acta 1525, 1-12.
    • (2001) Biochim. Biophys. Acta , vol.1525 , pp. 1-12
    • Furukawa, K.1    Takamiya, K.2    Okada, M.3    Inoue, M.4    Fukumoto, S.5    Furukawa, K.6
  • 32
    • 85007703923 scopus 로고
    • An update of sphingolipid synthesis and transport along the secretory pathway
    • Futerman, A. H. 1994 An update of sphingolipid synthesis and transport along the secretory pathway. Trends Glycosci. Glycotechnol. 6, 143-153.
    • (1994) Trends Glycosci. Glycotechnol. , vol.6 , pp. 143-153
    • Futerman, A.H.1
  • 33
    • 0025323167 scopus 로고
    • Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus
    • Futerman, A. H., Stieger, B., Hubbard, A. L. & Pagano, R. E. 1990 Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus. J. Biol. Chem. 265, 8650-8657.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8650-8657
    • Futerman, A.H.1    Stieger, B.2    Hubbard, A.L.3    Pagano, R.E.4
  • 34
    • 0021026543 scopus 로고
    • Activator protein for the degradation of globotriaosylceramide by human α-galactosidase
    • Gärtner, S., Conzelmann, E. & Sandhoff, K. 1983 Activator protein for the degradation of globotriaosylceramide by human α-galactosidase. J. Biol. Chem. 258, 12 378-12 385.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12378-12385
    • Gärtner, S.1    Conzelmann, E.2    Sandhoff, K.3
  • 35
    • 0030660670 scopus 로고    scopus 로고
    • Conversion of dihydroceramide into ceramide: Involvement of a desaturase
    • Geeraert, L., Mannaerts, G. P. & Van Veldhoven, P. P. 1997 Conversion of dihydroceramide into ceramide: involvement of a desaturase. Biochem. J. 327, 125-132.
    • (1997) Biochem. J. , vol.327 , pp. 125-132
    • Geeraert, L.1    Mannaerts, G.P.2    Van Veldhoven, P.P.3
  • 36
    • 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. & 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
  • 37
    • 0031661695 scopus 로고    scopus 로고
    • Variations among cell lines in the synthesis of sphingolipids in de novo and recycling pathways
    • Gillard, B. K., Clement, R. G. & Marcus, D. M. 1998 Variations among cell lines in the synthesis of sphingolipids in de novo and recycling pathways. Glycobiology 8, 885-889.
    • (1998) Glycobiology , vol.8 , pp. 885-889
    • Gillard, B.K.1    Clement, R.G.2    Marcus, D.M.3
  • 38
    • 0033568569 scopus 로고    scopus 로고
    • GA2/GM2/GD2 synthase localizes to the trans-golgi network of CHO-K1 cells
    • Giraudo, C. G., Rosales Fritz, V. M. & Maccioni, H. J. 1999 GA2/GM2/GD2 synthase localizes to the trans-golgi network of CHO-K1 cells. Biochem. J. 342, 633-640.
    • (1999) Biochem. J. , vol.342 , pp. 633-640
    • Giraudo, C.G.1    Rosales Fritz, V.M.2    Maccioni, H.J.3
  • 39
    • 0035852635 scopus 로고    scopus 로고
    • Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus
    • Giraudo, C. G., Daniotti, J. L. & Maccioni, H. J. F. 2001 Physical and functional association of glycolipid N-acetyl-galactosaminyl and galactosyl transferases in the Golgi apparatus. Proc. Natl Acad. Sci. USA 98, 1625-1630.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1625-1630
    • Giraudo, C.G.1    Daniotti, J.L.2    Maccioni, H.J.F.3
  • 40
    • 0030701535 scopus 로고    scopus 로고
    • Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p
    • Haak, D., Gable, K., Beeler, T. & Dunn, T. 1997 Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p. J. Biol. Chem. 272, 29 704-29 710.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29704-29710
    • Haak, D.1    Gable, K.2    Beeler, T.3    Dunn, T.4
  • 41
    • 0019363342 scopus 로고
    • Glycosphingolipids in cellular interaction, differentiation, and oncogenesis
    • Hakomori, S. 1981 Glycosphingolipids in cellular interaction, differentiation, and oncogenesis. A. Rev. Biochem. 50, 733-764.
    • (1981) A. Rev. Biochem. , vol.50 , pp. 733-764
    • Hakomori, S.1
  • 42
    • 0037135626 scopus 로고    scopus 로고
    • The ceramide-centric universe of lipid-mediated cell regulation: Stress encounters of the lipid kind
    • Hannun, Y. A. & Obeid, L. M. 2002 The ceramide-centric universe of lipid-mediated cell regulation: stress encounters of the lipid kind. J. Biol. Chem. 277, 25 847-25 850.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25847-25850
    • Hannun, Y.A.1    Obeid, L.M.2
  • 43
    • 0024420051 scopus 로고
    • Sphingolipid activator protein (SAP) deficiency in a 16-week-old atypical Gaucher disease patient and his fetal sibling; biochemical signs of combined sphingolipidosis
    • Harzer, K., Paton, B. C. & Poulos, A. 1989 Sphingolipid activator protein (SAP) deficiency in a 16-week-old atypical Gaucher disease patient and his fetal sibling; biochemical signs of combined sphingolipidosis. Eur. J. Pediatr. 149, 31-39.
    • (1989) Eur. J. Pediatr. , vol.149 , pp. 31-39
    • Harzer, K.1    Paton, B.C.2    Poulos, A.3
  • 46
    • 0028324129 scopus 로고
    • In vitro synthesis of disialoganglioside (GD1 alpha) from asialo-GM1 using sialyltransferases in rat liver Golgi vesicles
    • Hidari, K., Kawashima, I., Tai, T., Inagaki, F., Nagai, Y. & Sanai, Y. 1994 In vitro synthesis of disialoganglioside (GD1 alpha) from asialo-GM1 using sialyltransferases in rat liver Golgi vesicles. Eur. J. Biochem. 221, 603-609.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 603-609
    • Hidari, K.1    Kawashima, I.2    Tai, T.3    Inagaki, F.4    Nagai, Y.5    Sanai, Y.6
  • 47
    • 0032541422 scopus 로고    scopus 로고
    • Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP)
    • Hiesberger, T., Hüttler, S., Rohlmann, A., Schneider, W., Sandhoffm, K. & Herz, J. 1998 Cellular uptake of saposin (SAP) precursor and lysosomal delivery by the low density lipoprotein receptor-related protein (LRP). EMBO J. 17, 4617-4625.
    • (1998) EMBO J. , vol.17 , pp. 4617-4625
    • Hiesberger, T.1    Hüttler, S.2    Rohlmann, A.3    Schneider, W.4    Sandhoffm, K.5    Herz, J.6
  • 50
    • 0030971534 scopus 로고    scopus 로고
    • Cell death preventions, mitogen-activated protein kinase stimulation and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptide
    • Hiraiwa, M., Taylor, E. M., Campana, W. M., Darin, J. S. & O'Brien, J. S. 1997 Cell death preventions, mitogen-activated protein kinase stimulation and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptide. Proc. Natl Acad. Sci. USA 94, 4778-4781.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4778-4781
    • Hiraiwa, M.1    Taylor, E.M.2    Campana, W.M.3    Darin, J.S.4    O'Brien, J.S.5
  • 51
    • 0015154711 scopus 로고
    • Gaucher's disease: Deficiency of 'acid' β-glucosidase and reconstruction of enzyme activity in vitro
    • Ho, M. W. & O'Brien, J. S. 1971 Gaucher's disease: deficiency of 'acid' β-glucosidase and reconstruction of enzyme activity in vitro. Proc. Natl Acad. Sci. USA 68, 2810-2813.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2810-2813
    • Ho, M.W.1    O'Brien, J.S.2
  • 52
    • 0037007067 scopus 로고    scopus 로고
    • Paranodal junction formation and spermatogenesis require sulfoglycolipids
    • Honke, K. (and 10 others) 2002 Paranodal junction formation and spermatogenesis require sulfoglycolipids. Proc. Natl Acad. Sci. USA 99, 4227-4232.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4227-4232
    • Honke, K.1
  • 53
    • 0035871255 scopus 로고    scopus 로고
    • A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation
    • Hulkova, H. (and 12 others) 2001 A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation. Hum. Mol. Genet. 10, 927-940.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 927-940
    • Hulkova, H.1
  • 54
  • 56
    • 0025146326 scopus 로고
    • pH-dependent changes of ganglioside biosynthesis in neuronal cell culture
    • Iber, H., van Echten, G., Klein, R. A. & Sandhoff, K. 1990 pH-dependent changes of ganglioside biosynthesis in neuronal cell culture. Eur. J. Cell Biol. 52, 236-240.
    • (1990) Eur. J. Cell Biol. , vol.52 , pp. 236-240
    • Iber, H.1    Van Echten, G.2    Klein, R.A.3    Sandhoff, K.4
  • 57
    • 0026544882 scopus 로고
    • The c-series gangliosides GT3, GT2 and GP1c are formed in rat liver Golgi by the same set of glycosyltransferases that catalyse the biosynthesis of asialo-, a- and b-series gangliosides
    • Iber, H., Zacharias, C. & Sandhoff, K. 1992 The c-series gangliosides GT3, GT2 and GP1c are formed in rat liver Golgi by the same set of glycosyltransferases that catalyse the biosynthesis of asialo-, a- and b-series gangliosides. Glycobiol. 2, 137-142.
    • (1992) Glycobiol. , vol.2 , pp. 137-142
    • Iber, H.1    Zacharias, C.2    Sandhoff, K.3
  • 58
    • 0032080795 scopus 로고    scopus 로고
    • Glucosylceramide synthase and glycosphingolipid synthesis
    • Ichikawa, S. & Hirabayashi, Y. 1998 Glucosylceramide synthase and glycosphingolipid synthesis. Trends Cell Biol. 8, 198-202.
    • (1998) Trends Cell Biol. , vol.8 , pp. 198-202
    • Ichikawa, S.1    Hirabayashi, Y.2
  • 60
    • 0029861715 scopus 로고    scopus 로고
    • Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis
    • Ichikawa, S., Sakiyama, H., Suzuki, G., Hidari, K. & Hirabayashi, Y. 1996 Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. Proc. Natl Acad. Sci. USA 93, 4638-4643.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4638-4643
    • Ichikawa, S.1    Sakiyama, H.2    Suzuki, G.3    Hidari, K.4    Hirabayashi, Y.5
  • 61
    • 0028129708 scopus 로고
    • Biosynthetic pathway for a new series of gangliosides, GT1a alpha and GQ1b alpha
    • Irie, F., Hidari, K. I., Tai, T., Li, Y. T., Seyama, Y. & Hirabayashi, Y. 1994 Biosynthetic pathway for a new series of gangliosides, GT1a alpha and GQ1b alpha. FEBS Lett. 351, 291-294.
    • (1994) FEBS Lett. , vol.351 , pp. 291-294
    • Irie, F.1    Hidari, K.I.2    Tai, T.3    Li, Y.T.4    Seyama, Y.5    Hirabayashi, Y.6
  • 62
    • 0032532863 scopus 로고    scopus 로고
    • Nomenclature of glycolipids. Recommendations 1997
    • IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN) 1998 Nomenclature of glycolipids. Recommendations 1997. Eur. J. Biochem. 257, 293-298.
    • Eur. J. Biochem. , vol.257 , pp. 293-298
  • 63
    • 0026552908 scopus 로고
    • Glucosylceramide is synthesized at the cytosolic surface of various Golgi subfractions
    • Jeckel, D., Karrenbauer, A., Burger, K. N. J., Van Meer, G. & Wieland, F. 1992 Glucosylceramide is synthesized at the cytosolic surface of various Golgi subfractions. J. Cell Biol. 117, 259-267.
    • (1992) J. Cell Biol. , vol.117 , pp. 259-267
    • Jeckel, D.1    Karrenbauer, A.2    Burger, K.N.J.3    Van Meer, G.4    Wieland, F.5
  • 64
    • 0032844594 scopus 로고    scopus 로고
    • Conserved domains of glycosyltransferases
    • Kapitonov, D. & Yu, R. K. 1999 Conserved domains of glycosyltransferases. Glycobiol. 9, 961-978.
    • (1999) Glycobiol. , vol.9 , pp. 961-978
    • Kapitonov, D.1    Yu, R.K.2
  • 65
    • 0014410166 scopus 로고
    • Enzymatic synthesis of disialogangliosides from monosialogangliosides by sialyltransferases from embryonic chicken brain
    • Kaufman, B., Basu, S. & Roseman, S. 1968 Enzymatic synthesis of disialogangliosides from monosialogangliosides by sialyltransferases from embryonic chicken brain. J. Biol. Chem. 243, 5804-5807.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5804-5807
    • Kaufman, B.1    Basu, S.2    Roseman, S.3
  • 66
    • 0032584657 scopus 로고    scopus 로고
    • Embryonic stem cells with a disrupted GD3 synthase gene undergo neuronal differentiation in the absence of b-series gangliosides
    • Kawai, H., Sango, K., Mullin, K. A. & Proia, R. L. 1998 Embryonic stem cells with a disrupted GD3 synthase gene undergo neuronal differentiation in the absence of b-series gangliosides. J. Biol. Chem. 273, 19 634-19 638.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19634-19638
    • Kawai, H.1    Sango, K.2    Mullin, K.A.3    Proia, R.L.4
  • 67
    • 0035831502 scopus 로고    scopus 로고
    • Mice expressing only monosialoganglioside GM3 exhibit lethal audiogenic seizures
    • Kawai, H. (and 11 others) 2001 Mice expressing only monosialoganglioside GM3 exhibit lethal audiogenic seizures. J. Biol. Chem. 276, 6885-6888.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6885-6888
    • Kawai, H.1
  • 68
    • 0026768211 scopus 로고
    • Saposins: Structure, function, distribution and molecular genetics
    • Kishimoto, Y., Hiraiwa, M. & O'Brien, J. S. 1992 Saposins: structure, function, distribution and molecular genetics. J. Lipid Res. 33, 1255-1267.
    • (1992) J. Lipid Res. , vol.33 , pp. 1255-1267
    • Kishimoto, Y.1    Hiraiwa, M.2    O'Brien, J.S.3
  • 69
    • 0028275240 scopus 로고
    • Sphingolipid activator protein D (sap-D) stimulates the lysosomal degradation of ceramide in vivo
    • Klein, A., Henseler, M., Klein, C., Suzuki, K., Harzer, K. & Sandhoff, K. 1994 Sphingolipid activator protein D (sap-D) stimulates the lysosomal degradation of ceramide in vivo. Biochem. Biophys. Res. Commun. 200, 1440-1448.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 1440-1448
    • Klein, A.1    Henseler, M.2    Klein, C.3    Suzuki, K.4    Harzer, K.5    Sandhoff, K.6
  • 70
    • 0025775852 scopus 로고
    • Characterization of full-length cDNA and the gene coding for the human GM2-activator protein
    • Klima, H., Tanaka, A., Schnabel, D., Suzuki, K. & Sandhoff, K. 1991 Characterization of full-length cDNA and the gene coding for the human GM2-activator protein. FEBS Lett. 289, 260-264.
    • (1991) FEBS Lett. , vol.289 , pp. 260-264
    • Klima, H.1    Tanaka, A.2    Schnabel, D.3    Suzuki, K.4    Sandhoff, K.5
  • 71
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the anti-phospholipid syndrome regulates endosome structure and function
    • Kobayashi, T., Strang, E., Fang, K., de Moerloose, P., Parton, R. G. & Gruenberg, J. 1998 A lipid associated with the anti-phospholipid syndrome regulates endosome structure and function. Nature 392, 193-237.
    • (1998) Nature , vol.392 , pp. 193-237
    • Kobayashi, T.1    Strang, E.2    Fang, K.3    De Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 72
    • 0033152727 scopus 로고    scopus 로고
    • Sphingolipids: Their metabolic pathways and the pathobiochemistry of neurodegenerative diseases
    • Kolter, T. & 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
  • 73
    • 0034304915 scopus 로고    scopus 로고
    • Biomolecule function: No reliable prediction from cell culture
    • Kolter, T., Magin, T. & Sandhoff, K. 2000 Biomolecule function: no reliable prediction from cell culture. Traffic 1, 803-804.
    • (2000) Traffic , vol.1 , pp. 803-804
    • Kolter, T.1    Magin, T.2    Sandhoff, K.3
  • 74
    • 0037135608 scopus 로고    scopus 로고
    • Minireview: Combinatorial ganglioside biosynthesis
    • Kolter, T., Proia, R. L. & Sandhoff, K. 2002 Minireview: combinatorial ganglioside biosynthesis. J. Biol. Chem. 277, 25 859-25 862.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25859-25862
    • Kolter, T.1    Proia, R.L.2    Sandhoff, K.3
  • 76
    • 0002468538 scopus 로고    scopus 로고
    • Glyoclipids: Structure and function
    • ed. H. J. Gabius & S. Gabius. Wiley-VCh, Germany
    • Kopitz, J. 1997 Glyoclipids: structure and function. In Glycosciences (ed. H. J. Gabius & S. Gabius), pp. 163-189. Wiley-VCh, Germany.
    • (1997) Glycosciences , pp. 163-189
    • Kopitz, J.1
  • 78
    • 0021885280 scopus 로고
    • Evidence for two different active sites on human hexosaminidase A: Interaction of GM2 activator protein with hexosaminidase
    • Kytzia, H.-J. & Sandhoff, K. 1985 Evidence for two different active sites on human hexosaminidase A: interaction of GM2 activator protein with hexosaminidase. J. Biol. Chem. 260, 7568-7572.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7568-7572
    • Kytzia, H.-J.1    Sandhoff, K.2
  • 79
    • 0032579266 scopus 로고    scopus 로고
    • Functional organization of the Golgi apparatus in glycosphingolipid biosynthesis. Lactosylceramide and subsequent glycosphingolipids are formed in the lumen of the late Golgi
    • Lannert, H., Gorgas, K., Meißner, I., Wieland, F. T. & Jeckel, D. 1996 Functional organization of the Golgi apparatus in glycosphingolipid biosynthesis. Lactosylceramide and subsequent glycosphingolipids are formed in the lumen of the late Golgi. J. Biol. Chem. 273, 2939-2946.
    • (1996) J. Biol. Chem. , vol.273 , pp. 2939-2946
    • Lannert, H.1    Gorgas, K.2    Meißner, I.3    Wieland, F.T.4    Jeckel, D.5
  • 80
    • 0032579266 scopus 로고    scopus 로고
    • Functional organization of the Golgi apparatus in glycosphingolipid biosynthesis. Lactosylceramide and subsequent glycosphingolipids are formed in the lumen of the late Golgi
    • Lannert, H., Gorgas, K., Meißner, I., Wieland, F. T. & Jeckel, D. 1998 Functional organization of the Golgi apparatus in glycosphingolipid biosynthesis. Lactosylceramide and subsequent glycosphingolipids are formed in the lumen of the late Golgi. J. Biol. Chem. 273, 2939-2946.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2939-2946
    • Lannert, H.1    Gorgas, K.2    Meißner, I.3    Wieland, F.T.4    Jeckel, D.5
  • 81
    • 0034736222 scopus 로고    scopus 로고
    • Prosaptide exacerbates ischemia-induced behavioral deficits in vivo: An effect that does not involve mitogen-activated protein kinase activation
    • Lapchak, P. A., Araujo, D. M., Shackelford, D. A. & Zivin, J. A. 2000 Prosaptide exacerbates ischemia-induced behavioral deficits in vivo: an effect that does not involve mitogen-activated protein kinase activation. Neuroscience 101, 811-814.
    • (2000) Neuroscience , vol.101 , pp. 811-814
    • Lapchak, P.A.1    Araujo, D.M.2    Shackelford, D.A.3    Zivin, J.A.4
  • 83
    • 0015822234 scopus 로고
    • Gangliosides of human myelin: Sialosylgalactosylceramide (G7) as a major component
    • Ledeen, R. W., Yu, R. K. & Eng, L. F. 1973 Gangliosides of human myelin: sialosylgalactosylceramide (G7) as a major component. J. Neurochem. 21, 829-839.
    • (1973) J. Neurochem. , vol.21 , pp. 829-839
    • Ledeen, R.W.1    Yu, R.K.2    Eng, L.F.3
  • 86
    • 0035077616 scopus 로고    scopus 로고
    • Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins
    • Linke, T., Wilkening, G., Lansmann, S., Moczall, H., Bartelsen, O., Weisgerber, J. & Sandhoff, K. 2001a Stimulation of acid sphingomyelinase activity by lysosomal lipids and sphingolipid activator proteins. Biol. Chem. 382, 283-290.
    • (2001) Biol. Chem. , vol.382 , pp. 283-290
    • Linke, T.1    Wilkening, G.2    Lansmann, S.3    Moczall, H.4    Bartelsen, O.5    Weisgerber, J.6    Sandhoff, K.7
  • 90
    • 0031820071 scopus 로고    scopus 로고
    • Biosynthesis and functions of gangliosides: Recent advances
    • Lloyd, K. O. & Furukawa, K. 1998 Biosynthesis and functions of gangliosides: recent advances. Glycoconjugate J. 15, 627-636.
    • (1998) Glycoconjugate J. , vol.15 , pp. 627-636
    • Lloyd, K.O.1    Furukawa, K.2
  • 91
    • 0028172235 scopus 로고
    • Cloned beta 1,4 N-acetylgalactosaminyltransferase synthesizes GA2 as well as gangliosides GM2 and GD2. GM3 synthesis has priority, over GA2 synthesis for utilization of lactosylceramide substrate in vivo
    • Lutz, M. S., Jaskiewicz, E., Darling, D. S., Furukawa, K. & Young Jr, W. W. 1994 Cloned beta 1,4 N-acetylgalactosaminyltransferase synthesizes GA2 as well as gangliosides GM2 and GD2. GM3 synthesis has priority, over GA2 synthesis for utilization of lactosylceramide substrate in vivo. J. Biol. Chem. 269, 29 227-29 231.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29227-29231
    • Lutz, M.S.1    Jaskiewicz, E.2    Darling, D.S.3    Furukawa, K.4    Young W.W., Jr.5
  • 92
    • 0033602111 scopus 로고    scopus 로고
    • Organization of ganglioside synthesis in the Golgi apparatus
    • Maccioni, H. J., Daniotti, J. L. & Martina, J. A. 1999 Organization of ganglioside synthesis in the Golgi apparatus. Biochim. Biophys. Acta 1437, 101-118.
    • (1999) Biochim. Biophys. Acta , vol.1437 , pp. 101-118
    • Maccioni, H.J.1    Daniotti, J.L.2    Martina, J.A.3
  • 93
    • 0037788982 scopus 로고    scopus 로고
    • Sphingolipid activator deficiencies and Niemann-Pick type C
    • ed. F. Platt & S. U. Walkley. In the press.
    • Macheleidt, O., Kolter, T. & Sandhoff, K. 2003 Sphingolipid activator deficiencies and Niemann-Pick type C. In Lysosomal disorders of the brain (ed. F. Platt & S. U. Walkley). (In the press.)
    • (2003) Lysosomal Disorders of the Brain
    • Macheleidt, O.1    Kolter, T.2    Sandhoff, K.3
  • 94
    • 0032584510 scopus 로고    scopus 로고
    • The GM2 activator protein, its roles as a co-factor in GM2 hydrolysis and as a general glycolipid transport protein
    • Mahuran, D. J. 1998 The GM2 activator protein, its roles as a co-factor in GM2 hydrolysis and as a general glycolipid transport protein. Biochim. Biophys. Acta 1393, 1-18.
    • (1998) Biochim. Biophys. Acta , vol.1393 , pp. 1-18
    • Mahuran, D.J.1
  • 95
    • 0025796981 scopus 로고
    • Sphingolipid biosynthesis in cultured neurons: Down-regulation of serine palmitoyltransferase by sphingoid bases
    • Mandon, E. C., van Echten, G., Birk, R., Schmidt, R. R. & Sandhoff, K. 1991 Sphingolipid biosynthesis in cultured neurons: down-regulation of serine palmitoyltransferase by sphingoid bases. Eur. J. Biochem. 198, 667-674.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 667-674
    • Mandon, E.C.1    Van Echten, G.2    Birk, R.3    Schmidt, R.R.4    Sandhoff, K.5
  • 96
    • 0026712872 scopus 로고
    • Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase and sphinganine N-acyltransferase in mouse liver
    • Mandon, E. C., Ehses, I., Rother, J., van Echten, G. & Sandhoff, K. 1992 Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase and sphinganine N-acyltransferase in mouse liver. J. Biol. Chem. 267, 11 144-11 148.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11144-11148
    • Mandon, E.C.1    Ehses, I.2    Rother, J.3    Van Echten, G.4    Sandhoff, K.5
  • 97
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressures in membranes
    • Marsh, D. 1996 Lateral pressures in membranes. Biochim. Biophys. Acta 1286, 183-223.
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 183-223
    • Marsh, D.1
  • 98
    • 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
    • Matsuda, J., Vanier, M. T., Saito, Y., Tohyama, J., Suzuki, K. & Suzuki, K. 2001 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, 1191-1199.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1191-1199
    • Matsuda, J.1    Vanier, M.T.2    Saito, Y.3    Tohyama, J.4    Suzuki, K.5    Suzuki, K.6
  • 99
    • 0018786885 scopus 로고
    • Degradation of bis(monoacylglycero)phosphate by an acid phosphodiesterase in rat liver lysosomes
    • Matsuzawa, Y. & Hostetler, K. Y. 1979 Degradation of bis(monoacylglycero)phosphate by an acid phosphodiesterase in rat liver lysosomes. J. Biol. Chem. 254, 5997-6001.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5997-6001
    • Matsuzawa, Y.1    Hostetler, K.Y.2
  • 100
  • 101
    • 0025924830 scopus 로고
    • The human GM2 activator protein: A substrate specific cofactor of hexosaminidase A
    • Meier, E. M., Schwarzmann, G., Fürst, W. & Sandhoff, K. 1991 The human GM2 activator protein: a substrate specific cofactor of hexosaminidase A. J. Biol. Chem. 266, 1879-1887.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1879-1887
    • Meier, E.M.1    Schwarzmann, G.2    Fürst, W.3    Sandhoff, K.4
  • 102
    • 0037135536 scopus 로고    scopus 로고
    • De novo sphingolipid biosynthesis: A necessary, but dangerous, pathway
    • Merrill Jr, A. H. 2002 De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway. J. Biol. Chem. 277, 25 843-25 846.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25843-25846
    • Merrill A.H., Jr.1
  • 103
    • 0023036582 scopus 로고
    • Biosynthesis of long-chain (sphingoid) bases from serine by LM cells. Evidence for introduction of the 4-trans-double bond after de novo biosynthesis of N-acylsphinganine(s)
    • Merrill Jr, A. H. & Wang, E. 1986 Biosynthesis of long-chain (sphingoid) bases from serine by LM cells. Evidence for introduction of the 4-trans-double bond after de novo biosynthesis of N-acylsphinganine(s). J. Biol. Chem. 261, 3764-3769.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3764-3769
    • Merrill A.H., Jr.1    Wang, E.2
  • 104
    • 0030844101 scopus 로고    scopus 로고
    • Conversion of dihydroceramide to ceramide occurs at the cytosolic face of the endoplasmic reticulum
    • Michel, C. & van Echten-Deckert, G. 1997 Conversion of dihydroceramide to ceramide occurs at the cytosolic face of the endoplasmic reticulum. FEBS Lett. 416, 153-155.
    • (1997) FEBS Lett. , vol.416 , pp. 153-155
    • Michel, C.1    Van Echten-Deckert, G.2
  • 105
    • 0030963660 scopus 로고    scopus 로고
    • Characterization of ceramide synthesis. A dihydroceramide desaturase introduces the 4,5-trans-double bond of sphingosine at the level of dihydroceramide
    • Michel, C., Van Echten-Deckert, G., Rother, J., Sandhoff, K., Wang, E. & Merrill Jr, A. H. 1997 Characterization of ceramide synthesis. A dihydroceramide desaturase introduces the 4,5-trans-double bond of sphingosine at the level of dihydroceramide. J. Biol. Chem. 272, 22 432-22 435.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22432-22435
    • Michel, C.1    Van Echten-Deckert, G.2    Rother, J.3    Sandhoff, K.4    Wang, E.5    Merrill A.H., Jr.6
  • 106
    • 0031980787 scopus 로고    scopus 로고
    • Substrate specificity and some other enzymatic properties of dihydroceramide desaturase (ceramide synthase) in fetal rat skin
    • Mikami, T., Kashiwagi, M., Tsuchihashi, K., Akino, T. & Gasa, S. 1998 Substrate specificity and some other enzymatic properties of dihydroceramide desaturase (ceramide synthase) in fetal rat skin. J. Biochem. 123, 906-911.
    • (1998) J. Biochem. , vol.123 , pp. 906-911
    • Mikami, T.1    Kashiwagi, M.2    Tsuchihashi, K.3    Akino, T.4    Gasa, S.5
  • 108
    • 0032799717 scopus 로고    scopus 로고
    • Intracellular distribution of a biotin-labeled ganglioside GM1 by immunoelectron microscopy after endocytosis in fibroblasts
    • Möbius, W., Herzog, V., Sandhoff, K. & 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
    • Möbius, W.1    Herzog, V.2    Sandhoff, K.3    Schwarzmann, G.4
  • 109
    • 0014961287 scopus 로고
    • Specificity in ceramide biosynthesis from long chain bases and various fatty acyl coenzyme A's by brain microsomes
    • Morell, P. & Radin, N. S. 1970 Specificity in ceramide biosynthesis from long chain bases and various fatty acyl coenzyme A's by brain microsomes. J. Biol. Chem. 245, 342-350.
    • (1970) J. Biol. Chem. , vol.245 , pp. 342-350
    • Morell, P.1    Radin, N.S.2
  • 113
    • 0033052188 scopus 로고    scopus 로고
    • Ganglioside GM2-activator protein and vesicular transport in collecting duct intercalated cells
    • Mundel, T. M., Heid, H. W., Mahuran, D. J., Kriz, W. & Mundel, P. 1999 Ganglioside GM2-activator protein and vesicular transport in collecting duct intercalated cells. J. Am. Soc. Nephrol. 10, 435-443.
    • (1999) J. Am. Soc. Nephrol. , vol.10 , pp. 435-443
    • Mundel, T.M.1    Heid, H.W.2    Mahuran, D.J.3    Kriz, W.4    Mundel, P.5
  • 114
    • 0029126584 scopus 로고
    • Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
    • Munford, R. S., Sheppard, P. O. & O'Hara, P. J. 1995 Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure. J. Lipid Res. 36, 1653-1663.
    • (1995) J. Lipid Res. , vol.36 , pp. 1653-1663
    • Munford, R.S.1    Sheppard, P.O.2    O'Hara, P.J.3
  • 115
    • 0027980277 scopus 로고
    • The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis
    • Nagiec, M. M., Baltisberger, J. A., Wells, G. B., Lester, R. L. & Dickson, R. C. 1994 The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis. Proc. Natl Acad. Sci. USA 91, 7899-7902.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7899-7902
    • Nagiec, M.M.1    Baltisberger, J.A.2    Wells, G.B.3    Lester, R.L.4    Dickson, R.C.5
  • 116
    • 0032514598 scopus 로고    scopus 로고
    • Requirement of GM2 ganglioside activator for phospholipase D activation
    • Nakamura, S.-I. (and 10 others) 1998 Requirement of GM2 ganglioside activator for phospholipase D activation. Proc. Natl Acad. Sci. USA 95, 12 249-12 253.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12249-12253
    • Nakamura, S.-I.1
  • 117
    • 0024593996 scopus 로고
    • Structure of full length cDNA coding for sulfatide activator, a co-β glucosidase and two other homologous proteins: Two alternate forms of the sulfatide activator
    • Nakano, T., Sandhoff, K., Stümper, J., Christomanou, H. & Suzuki, K. 1989 Structure of full length cDNA coding for sulfatide activator, a co-β glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator. J. Biochem. 105, 152-154.
    • (1989) J. Biochem. , vol.105 , pp. 152-154
    • Nakano, T.1    Sandhoff, K.2    Stümper, J.3    Christomanou, H.4    Suzuki, K.5
  • 119
    • 15644371731 scopus 로고    scopus 로고
    • Purification, cDNA cloning, and expression of UDP-Gal: Glucosylceramide beta-1,4-galactosyltransferase from rat brain
    • Nomura, T. (and 11 others) 1998 Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide beta-1,4-galactosyltransferase from rat brain. J. Biol. Chem. 273, 13 570-13 577.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13570-13577
    • Nomura, T.1
  • 120
    • 0024297787 scopus 로고
    • Coding of two sphingolipid activator proteins (SAP1 and SAP2) by same genetic locus
    • O'Brien, J. S., Kretz, K. A., Dewji, N., Wenger, D. A., Esch, F. & Fluharty, A. L. 1988 Coding of two sphingolipid activator proteins (SAP1 and SAP2) by same genetic locus. Science 241, 1098-1101.
    • (1988) Science , vol.241 , pp. 1098-1101
    • O'Brien, J.S.1    Kretz, K.A.2    Dewji, N.3    Wenger, D.A.4    Esch, F.5    Fluharty, A.L.6
  • 121
    • 0030048470 scopus 로고    scopus 로고
    • Purification and characterization of UDP-glucose:ceramide glucosyltransferase from rat liver Golgi membranes
    • Paul, P., Kamisaka, Y., Marks, D. L. & Pagano, R. E. 1996 Purification and characterization of UDP-glucose:ceramide glucosyltransferase from rat liver Golgi membranes. J. Biol. Chem. 271, 2287-2293.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2287-2293
    • Paul, P.1    Kamisaka, Y.2    Marks, D.L.3    Pagano, R.E.4
  • 122
    • 0028232681 scopus 로고
    • Biogenesis of lysosomal membranes
    • Peters, C. & von Figura, K. 1994 Biogenesis of lysosomal membranes. FEBS Lett. 346, 108-114.
    • (1994) FEBS Lett. , vol.346 , pp. 108-114
    • Peters, C.1    Von Figura, K.2
  • 123
    • 0001117169 scopus 로고
    • Both GA2, GM2 and GD2 synthases and GM1b, GD1a and GT1b synthases are single enzymes in Golgi vesicles from rat liver
    • Pohlentz, G., Klein, D., Schwarzmann, G., Schmitz, D. & Sandhoff, K. 1988 Both GA2, GM2 and GD2 synthases and GM1b, GD1a and GT1b synthases are single enzymes in Golgi vesicles from rat liver. Proc. Natl Acad. Sci. USA 85, 7044-7048.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7044-7048
    • Pohlentz, G.1    Klein, D.2    Schwarzmann, G.3    Schmitz, D.4    Sandhoff, K.5
  • 124
    • 0029000740 scopus 로고
    • Swaposins: Circular permutations within genes encoding saposin homologues
    • Ponting, C. P. & Russell, R. B. 1995 Swaposins: circular permutations within genes encoding saposin homologues. Trends Biochem. Sci. 20, 179-180.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 179-180
    • Ponting, C.P.1    Russell, R.B.2
  • 125
    • 0038100164 scopus 로고    scopus 로고
    • Glycosphingolipid functions: Insights from engineered mouse models
    • DOI 10.1098/rstb.2003.1268
    • Proia, R. L. 2003 Glycosphingolipid functions: insights from engineered mouse models. Phil. Trans. R. Soc. Lond. B 358, 879-883. (DOI 10.1098/rstb.2003.1268.)
    • (2003) Phil. Trans. R. Soc. Lond. B , vol.358 , pp. 879-883
    • Proia, R.L.1
  • 126
    • 0014867207 scopus 로고
    • The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intercellular adhesion
    • Roseman, S. 1970 The synthesis of complex carbohydrates by multiglycosyltransferase systems and their potential function in intercellular adhesion. Chem. Phys. Lipids 5, 270-297.
    • (1970) Chem. Phys. Lipids , vol.5 , pp. 270-297
    • Roseman, S.1
  • 127
    • 0027074149 scopus 로고
    • Biosynthesis of sphingolipids: Dihydroceramide and not sphinganine is desaturated by cultured cells
    • Rother, J., van Echten, G., Schwarzmann, G. & Sandhoff, K. 1992 Biosynthesis of sphingolipids: dihydroceramide and not sphinganine is desaturated by cultured cells. Biochem. Biophys. Res. Commun. 189, 14-20.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 14-20
    • Rother, J.1    Van Echten, G.2    Schwarzmann, G.3    Sandhoff, K.4
  • 128
    • 0034697239 scopus 로고    scopus 로고
    • Further studies on the reconstitution of glucosylceramidase activity, by Sap C and anionic phospholipids
    • Salvioli, R., Tatti, M., Ciaffoni, F. & Vaccaro, A. M. 2000 Further studies on the reconstitution of glucosylceramidase activity, by Sap C and anionic phospholipids. FEBS Lett. 472, 17-21.
    • (2000) FEBS Lett. , vol.472 , pp. 17-21
    • Salvioli, R.1    Tatti, M.2    Ciaffoni, F.3    Vaccaro, A.M.4
  • 129
    • 0017492554 scopus 로고
    • The biochemistry of sphingolipid storage diseases
    • Sandhoff, K. 1977 The biochemistry of sphingolipid storage diseases. Angew Chem. Int. Ed. 16, 273-285.
    • (1977) Angew Chem. Int. Ed. , vol.16 , pp. 273-285
    • Sandhoff, K.1
  • 130
    • 0029670774 scopus 로고    scopus 로고
    • Topology of glycosphingolipid degradation
    • Sandhoff, K. & Kolter, T. 1996 Topology of glycosphingolipid degradation. Trends Cell Biol. 6, 98-103.
    • (1996) Trends Cell Biol. , vol.6 , pp. 98-103
    • Sandhoff, K.1    Kolter, T.2
  • 131
    • 0015179162 scopus 로고
    • Enzyme alterations and lipid storage in three variants of Tay-Sachs disease
    • Sandhoff, K., Harzer, K., Wässle, W. & Jatzkewitz, H. 1971 Enzyme alterations and lipid storage in three variants of Tay-Sachs disease. J. Neurochem. 18, 2469-2489.
    • (1971) J. Neurochem. , vol.18 , pp. 2469-2489
    • Sandhoff, K.1    Harzer, K.2    Wässle, W.3    Jatzkewitz, H.4
  • 132
    • 0000857916 scopus 로고    scopus 로고
    • Sphingolipid activator proteins
    • 8th edn (ed. C. R. Scriver, A. L. Beaudet, W. S. Sly & D. Valle). New York: McGraw-Hill
    • Sandhoff, K., Kolter, T. & Harzer, K. 2001 Sphingolipid activator proteins. In The metabolic and molecular bases of inherited disease, vol 3, 8th edn (ed. C. R. Scriver, A. L. Beaudet, W. S. Sly & D. Valle), pp. 3371-3388. New York: McGraw-Hill.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , vol.3 , pp. 3371-3388
    • Sandhoff, K.1    Kolter, T.2    Harzer, K.3
  • 134
    • 0022894809 scopus 로고
    • Specificity of human glucosylceramide beta-glucosidase towards synthetic glucosylsphingolipids inserted into liposomes. Kinetic studies in a detergent-free assay system
    • Sarmientos, F., Schwarzmann, G. & Sandhoff, K. 1986 Specificity of human glucosylceramide beta-glucosidase towards synthetic glucosylsphingolipids inserted into liposomes. Kinetic studies in a detergent-free assay system. Eur. J. Biochem. 160, 527-535.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 527-535
    • Sarmientos, F.1    Schwarzmann, G.2    Sandhoff, K.3
  • 135
  • 136
    • 0033837965 scopus 로고    scopus 로고
    • Characterization of regulatory elements in the 5′-flanking region of the GM2 activator gene
    • Schepers, U., Lemm, T., Herzog, V. & Sandhoff, K. 2000 Characterization of regulatory elements in the 5′-flanking region of the GM2 activator gene. Biol. Chem. 381, 531-544.
    • (2000) Biol. Chem. , vol.381 , pp. 531-544
    • Schepers, U.1    Lemm, T.2    Herzog, V.3    Sandhoff, K.4
  • 137
    • 0025762364 scopus 로고
    • Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease
    • Schnabel, D., Schröder, M. & Sandhoff, K. 1991 Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease. FEBS Lett. 284, 57-59.
    • (1991) FEBS Lett. , vol.284 , pp. 57-59
    • Schnabel, D.1    Schröder, M.2    Sandhoff, K.3
  • 138
    • 0026705846 scopus 로고
    • Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene
    • Schnabel, D. (and 11 others) 1992 Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene. J. Biol. Chem. 267, 3312-3315.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3312-3315
    • Schnabel, D.1
  • 139
    • 0025737830 scopus 로고
    • A mutation in the gene of a glycolipid binding protein (GM2-activator) that causes GM2-gangliosidosis variant AB
    • Schröder, M., Schnabel, D., Suzuki, K. & Sandhoff, K. 1991 A mutation in the gene of a glycolipid binding protein (GM2-activator) that causes GM2-gangliosidosis variant AB. FEBS Lett. 290, 1-3.
    • (1991) FEBS Lett. , vol.290 , pp. 1-3
    • Schröder, M.1    Schnabel, D.2    Suzuki, K.3    Sandhoff, K.4
  • 140
    • 0027500852 scopus 로고
    • Molecular genetics of GM2-gangliosidosis AB variant: A novel mutation and expression in BHK cells
    • Schröder, M., Schnabel, D., Hurwitz, R., Young, E., Suzuki, K. & Sandhoff, K. 1993 Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation and expression in BHK cells. Hum. Genet. 92, 437-440.
    • (1993) Hum. Genet. , vol.92 , pp. 437-440
    • Schröder, M.1    Schnabel, D.2    Hurwitz, R.3    Young, E.4    Suzuki, K.5    Sandhoff, K.6
  • 141
    • 0039703311 scopus 로고    scopus 로고
    • Complete localization of disulfide bonds in GM2-activator protein
    • Schuette, C. G., Lemm, T., Glombitza, G. J. & Sandhoff, K. 1998 Complete localization of disulfide bonds in GM2-activator protein. Protein Sci. 7, 1039-1045.
    • (1998) Protein Sci. , vol.7 , pp. 1039-1045
    • Schuette, C.G.1    Lemm, T.2    Glombitza, G.J.3    Sandhoff, K.4
  • 142
    • 0034939951 scopus 로고    scopus 로고
    • Sphingolipid activator proteins: Proteins with complex functions in lipid degradation and skin biogenesis
    • Schuette, C. G., Pierstorff, B., Huettler, S. & Sandhoff, K. 2001 Sphingolipid activator proteins: proteins with complex functions in lipid degradation and skin biogenesis. Glycobiology 11, 81R-90R.
    • (2001) Glycobiology , vol.11
    • Schuette, C.G.1    Pierstorff, B.2    Huettler, S.3    Sandhoff, K.4
  • 144
    • 0031800791 scopus 로고    scopus 로고
    • Partial purification and characterization of sphingosine N-acyltransferase (ceramide synthase) from bovine liver mitochondrion-rich fraction
    • Shimeno, H., Soeda, S., Sakamoto, M., Kouchi, T., Kowakame, T. & Kihara, T. 1998 Partial purification and characterization of sphingosine N-acyltransferase (ceramide synthase) from bovine liver mitochondrion-rich fraction. Lipids 33, 601-605.
    • (1998) Lipids , vol.33 , pp. 601-605
    • Shimeno, H.1    Soeda, S.2    Sakamoto, M.3    Kouchi, T.4    Kowakame, T.5    Kihara, T.6
  • 145
    • 0031004540 scopus 로고    scopus 로고
    • Characterization of the affinity of the GM2 activator protein for glycolipids by a fluorescence dequenching assay
    • Smiljanic-Georgijev, N., Rigat, B., Leung, A. & Mahuran, D. J. 1997 Characterization of the affinity of the GM2 activator protein for glycolipids by a fluorescence dequenching assay. Biochim. Biophys. Acta 1339, 192-202.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 192-202
    • Smiljanic-Georgijev, N.1    Rigat, B.2    Leung, A.3    Mahuran, D.J.4
  • 146
    • 0037135572 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate, a key cell signaling molecule
    • Spiegel, S. & Milstien, S. 2002 Sphingosine 1-phosphate, a key cell signaling molecule. J. Biol. Chem. 277, 25 851-25 854.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25851-25854
    • Spiegel, S.1    Milstien, S.2
  • 147
    • 0035282804 scopus 로고    scopus 로고
    • A ganglioside-specific sialyltransferase localizes to axons and non-Golgi structures in neurons
    • Stern, C. A. & Tiemeyer, M. 2001 A ganglioside-specific sialyltransferase localizes to axons and non-Golgi structures in neurons. J. Neurosci. 21, 1434-1443.
    • (2001) J. Neurosci. , vol.21 , pp. 1434-1443
    • Stern, C.A.1    Tiemeyer, M.2
  • 148
    • 0034125540 scopus 로고    scopus 로고
    • Molecular identification, tissue distribution and subcellular localization of mST3GalV/GM3 synthase
    • Stern, C. A., Braverman, T. R. & Tiemeyer, M. 2000 Molecular identification, tissue distribution and subcellular localization of mST3GalV/GM3 synthase. Glycobiol. 10, 365-374.
    • (2000) Glycobiol. , vol.10 , pp. 365-374
    • Stern, C.A.1    Braverman, T.R.2    Tiemeyer, M.3
  • 149
    • 84942961893 scopus 로고
    • Metabolism of sphingosine bases. 8. Distribution, isolation and properties of D-3-oxosphinganine reductase. Stereospecificity of the NADPH-dependent reaction of 3-oxodihydrospingosine (2-amino-1-hydroxyoctadecane-3-one)
    • Stoffel, W., LeKim, D. & Sticht, G. 1968 Metabolism of sphingosine bases. 8. Distribution, isolation and properties of D-3-oxosphinganine reductase. Stereospecificity of the NADPH-dependent reaction of 3-oxodihydrospingosine (2-amino-1-hydroxyoctadecane-3-one). Hoppe Seyler Z. Physiol. Chem. 349, 1637-1644.
    • (1968) Hoppe Seyler Z. Physiol. Chem. , vol.349 , pp. 1637-1644
    • Stoffel, W.1    LeKim, D.2    Sticht, G.3
  • 150
    • 0027368628 scopus 로고
    • Regional localisation of the gene coding for the GM2 activator protein (GM2A) to chromosome 5q32-33 and confirmation of the assignment of GM2AP to chromosome 3
    • Swallow, D. M., Islam, I., Fox, M. F., Povey, S., Klima, H., Schepers, U. & Sandhoff, K. 1993 Regional localisation of the gene coding for the GM2 activator protein (GM2A) to chromosome 5q32-33 and confirmation of the assignment of GM2AP to chromosome 3. Ann. Hum. Genet. 57, 187-193.
    • (1993) Ann. Hum. Genet. , vol.57 , pp. 187-193
    • Swallow, D.M.1    Islam, I.2    Fox, M.F.3    Povey, S.4    Klima, H.5    Schepers, U.6    Sandhoff, K.7
  • 151
    • 0036479215 scopus 로고    scopus 로고
    • Ganglioside GM3 participates in the pathological conditions of insulin resistance
    • Tagami, S. (and 11 others) 2002 Ganglioside GM3 participates in the pathological conditions of insulin resistance. J. Biol. Chem. 277, 3085-3092.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3085-3092
    • Tagami, S.1
  • 152
    • 0010492680 scopus 로고    scopus 로고
    • Mice with disrupted GM2/GD2 synthase gene lack complex gangliosides but exhibit only subtle defects in their nervous system
    • Takamiya, K. (and 14 others) 1996 Mice with disrupted GM2/GD2 synthase gene lack complex gangliosides but exhibit only subtle defects in their nervous system. Proc. Natl Acad. Sci. USA 93, 10 662-10 667.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10662-10667
    • Takamiya, K.1
  • 153
    • 13144255753 scopus 로고    scopus 로고
    • Complex gangliosides are essential in spermatogenesis of mice: Possible roles in the transport of testosterone
    • Takamiya, K. (and 12 others) 1998 Complex gangliosides are essential in spermatogenesis of mice: possible roles in the transport of testosterone. Proc. Natl Acad. Sci. USA 95, 12 147-12 152.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12147-12152
    • Takamiya, K.1
  • 155
    • 0029417339 scopus 로고
    • pH-dependent conformational properties of saposins and their interactions with phospholipid membranes
    • Vaccaro, A. M., Ciaffoni, F., Tatti, M., Salvioli, R., Barca, A., Tognozzi, D. & Scerch, C. 1995a pH-dependent conformational properties of saposins and their interactions with phospholipid membranes. J. Biol. Chem. 270, 30 576-30 580.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30576-30580
    • Vaccaro, A.M.1    Ciaffoni, F.2    Tatti, M.3    Salvioli, R.4    Barca, A.5    Tognozzi, D.6    Scerch, C.7
  • 157
    • 0030878138 scopus 로고    scopus 로고
    • Effect of saposins A and C on the enzymatic hydrolysis of liposomal glucosylceramide
    • Vaccaro, A. M., Tatti, M., Ciaffoni, F., Salvioli, R., Barca, A. & Scerch, C. 1997 Effect of saposins A and C on the enzymatic hydrolysis of liposomal glucosylceramide. J. Biol. Chem. 272, 16 862-16 867.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16862-16867
    • Vaccaro, A.M.1    Tatti, M.2    Ciaffoni, F.3    Salvioli, R.4    Barca, A.5    Scerch, C.6
  • 159
    • 0036633299 scopus 로고    scopus 로고
    • Oiling the wheels of the endocytic pathway
    • Van der Goot, F. G. & Gruenberg, J. 2002 Oiling the wheels of the endocytic pathway. Trends Cell Biol. 12, 296-299.
    • (2002) Trends Cell Biol. , vol.12 , pp. 296-299
    • Van Der Goot, F.G.1    Gruenberg, J.2
  • 160
    • 0027467490 scopus 로고
    • Ganglioside metabolism: Enzymology, topology and regulation, minireview
    • van Echten, G. & Sandhoff, K. 1993 Ganglioside metabolism: enzymology, topology and regulation, minireview. J. Biol. Chem. 268, 5341-5344.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5341-5344
    • Van Echten, G.1    Sandhoff, K.2
  • 161
    • 0025316462 scopus 로고
    • Modulation of sphingolipid biosynthesis in primary cultured neurons by long-chain bases
    • van Echten, G., Birk, R., Brenner-Weiß, G., Schmidt, R. R. & Sandhoff, K. 1990 Modulation of sphingolipid biosynthesis in primary cultured neurons by long-chain bases. J. Biol. Chem. 265, 9333-9339.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9333-9339
    • Van Echten, G.1    Birk, R.2    Brenner-Weiß, G.3    Schmidt, R.R.4    Sandhoff, K.5
  • 162
    • 0037135518 scopus 로고    scopus 로고
    • Sphingolipid transport: Rafts and translocators
    • Van Meer, G. & Lisman, Q. 2002 Sphingolipid transport: rafts and translocators. J. Biol. Chem. 277, 25 855-25 858.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25855-25858
    • Van Meer, G.1    Lisman, Q.2
  • 163
    • 0029730641 scopus 로고    scopus 로고
    • Biosynthesis, processing, and targeting of sphingolipid activator protein (SAP-) precursor in cultured human fibroblasts. Mannose 6-phosphate receptor-independent endocytosis of SAP-precursor
    • Vielhaber, G., Hurwitz, R. & Sandhoff, K. 1997 Biosynthesis, processing, and targeting of sphingolipid activator protein (SAP-) precursor in cultured human fibroblasts. Mannose 6-phosphate receptor-independent endocytosis of SAP-precursor. J. Biol. Chem. 271, 32 438-32 446.
    • (1997) J. Biol. Chem. , vol.271 , pp. 32438-32446
    • Vielhaber, G.1    Hurwitz, R.2    Sandhoff, K.3
  • 164
    • 0025787230 scopus 로고
    • Glycosphingolipid specificity of the human sulfatide activator protein
    • Vogel, A., Schwarzmann, G. & Sandhoff, K. 1991 Glycosphingolipid specificity of the human sulfatide activator protein. Eur. J. Biochem. 200, 591-597.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 591-597
    • Vogel, A.1    Schwarzmann, G.2    Sandhoff, K.3
  • 165
  • 166
    • 0032540237 scopus 로고    scopus 로고
    • Up-regulation of glucosylceramide synthase expression and activity during human keratinocyte differentiation
    • Watanabe, R., Wu, K., Paul, P., Marks, D. L., Kobayashi, T., Pittelkow, M. R. & Pagano, R. E. 1998 Up-regulation of glucosylceramide synthase expression and activity during human keratinocyte differentiation. J. Biol. Chem. 273, 9651-9655.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9651-9655
    • Watanabe, R.1    Wu, K.2    Paul, P.3    Marks, D.L.4    Kobayashi, T.5    Pittelkow, M.R.6    Pagano, R.E.7
  • 167
    • 0030755002 scopus 로고    scopus 로고
    • Human and murine serine-palmitoyl-CoA transferase - cloning,
    • Weiss, B. & Stoffel, W. 1997 Human and murine serine-palmitoyl-CoA transferase - cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur. J. Biochem. 249, 239-247.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 239-247
    • Weiss, B.1    Stoffel, W.2
  • 168
    • 0020482329 scopus 로고
    • A protein activator of galactosylceramide-β-galactosidase
    • Wenger, D. A., Sattler, M. & Roth, S. 1982 A protein activator of galactosylceramide-β-galactosidase. Biochim. Biophys. Acta 712, 639-649.
    • (1982) Biochim. Biophys. Acta , vol.712 , pp. 639-649
    • Wenger, D.A.1    Sattler, M.2    Roth, S.3
  • 169
    • 0035918181 scopus 로고    scopus 로고
    • Degradation of membrane-bound ganglioside GM2 by β-hexosaminidase A
    • Werth, N., Schuette, C. G., Wilkening, G., Lemm, T. & Sandhoff, K. 2001 Degradation of membrane-bound ganglioside GM2 by β-hexosaminidase A. J. Biol. Chem. 276, 12 685-12 690.
    • (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
  • 170
    • 0023068117 scopus 로고
    • Covalently bound omega-hydroxyacylsphingosine in the stratum corneum
    • Wertz, P. W. & Downing, D. T. 1987 Covalently bound omega-hydroxyacylsphingosine in the stratum corneum. Biochim. Biophys. Acta 917, 108-111.
    • (1987) Biochim. Biophys. Acta , vol.917 , pp. 108-111
    • Wertz, P.W.1    Downing, D.T.2
  • 171
    • 0031891166 scopus 로고    scopus 로고
    • The physical, chemical and functional properties of lipids in the skin and other biological barriers
    • Wertz, P. W. & Van den Bergh, B. 1998 The physical, chemical and functional properties of lipids in the skin and other biological barriers. Chem. Phys. Lipids 91, 85-96.
    • (1998) Chem. Phys. Lipids , vol.91 , pp. 85-96
    • Wertz, P.W.1    Van Den Bergh, B.2
  • 172
    • 0032514902 scopus 로고    scopus 로고
    • Lysosomal degradation on vesicular membrane surfaces. Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators
    • Wilkening, G., Linke, T. & Sandhoff, K. 1998 Lysosomal degradation on vesicular membrane surfaces. Enhanced glucosylceramide degradation by lysosomal anionic lipids and activators. J. Biol. Chem. 273, 30 271-30 278.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30271-30278
    • Wilkening, G.1    Linke, T.2    Sandhoff, K.3
  • 174
    • 0034406526 scopus 로고    scopus 로고
    • Crystal structure of human GM2-activator protein with a novel β-cup topology
    • Wright, C., Li, S.-C. & Rastinejad, F. 2000 Crystal structure of human GM2-activator protein with a novel β-cup topology. J. Mol. Biol. 304, 411-422.
    • (2000) J. Mol. Biol. , vol.304 , pp. 411-422
    • Wright, C.1    Li, S.-C.2    Rastinejad, F.3
  • 175
    • 0033971433 scopus 로고    scopus 로고
    • A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD)
    • Wrobe, D., Henseler, M., Huettler, S., Pascual Pascual, S. I., Chabas, A. & Sandhoff, K. 2000 A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD). J. Inherit. Metab. Dis. 23, 63-76.
    • (2000) J. Inherit. Metab. Dis. , vol.23 , pp. 63-76
    • Wrobe, D.1    Henseler, M.2    Huettler, S.3    Pascual Pascual, S.I.4    Chabas, A.5    Sandhoff, K.6
  • 177
    • 0029962089 scopus 로고    scopus 로고
    • Characterization of an alternatively spliced GM2 activator protein, GM2A protein. An activator protein which stimulates the enzymatic hydrolysis of N-acetylneuraminic acid, but not N-acetylgalactosamine, from GM2
    • Wu, Y. Y., Sonnino, S., Li, Y.-T. & Li, S.-C. 1996 Characterization of an alternatively spliced GM2 activator protein, GM2A protein. An activator protein which stimulates the enzymatic hydrolysis of N-acetylneuraminic acid, but not N-acetylgalactosamine, from GM2. J. Biol. Chem. 271, 10611-10615.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10611-10615
    • Wu, Y.Y.1    Sonnino, S.2    Li, Y.-T.3    Li, S.-C.4
  • 178
    • 0026566895 scopus 로고
    • Identification of a processed pseudogene related to the functional gene encoding the GM2 activator protein: Localization of the pseudogene to human chromosome 3 and the functional gene to human chromosome 5
    • Xie, B., Kennedy, J. L., McInnes, B., Auger, D. & Mahuran, D. 1992 Identification of a processed pseudogene related to the functional gene encoding the GM2 activator protein: localization of the pseudogene to human chromosome 3 and the functional gene to human chromosome 5. Genomics 14, 796-798.
    • (1992) Genomics , vol.14 , pp. 796-798
    • Xie, B.1    Kennedy, J.L.2    McInnes, B.3    Auger, D.4    Mahuran, D.5
  • 180
    • 0014544746 scopus 로고
    • The enzymic synthesis of ganglioside. 1. Brain uridine diphosphate D-galactose: N-acetyl-galactosaminyl-galactosyl-glucosyl-ceramide galactosyl transferase
    • Yip, M. C. M. & Dain, J. A. 1969 The enzymic synthesis of ganglioside. 1. Brain uridine diphosphate D-galactose: N-acetyl-galactosaminyl-galactosyl-glucosyl-ceramide galactosyl transferase. Lipids 4, 270-277.
    • (1969) Lipids , vol.4 , pp. 270-277
    • Yip, M.C.M.1    Dain, J.A.2
  • 181
    • 0345189536 scopus 로고    scopus 로고
    • Reevaluating the effect of Brefeldin A (BFA) on ganglioside synthesis: The location of GM2 synthase cannot be deduced from the inhibition of GM2 synthesis by BFA
    • Young, W. W., Allende, M. L. & Jaskiewicz, W. 1999 Reevaluating the effect of Brefeldin A (BFA) on ganglioside synthesis: the location of GM2 synthase cannot be deduced from the inhibition of GM2 synthesis by BFA. Glycobiol. 9, 689-695.
    • (1999) Glycobiol. , vol.9 , pp. 689-695
    • Young, W.W.1    Allende, M.L.2    Jaskiewicz, W.3
  • 182
    • 0023338194 scopus 로고
    • Oligosialogangliosides inhibit GM2- and GD3-synthesis in isolated Golgi vesicles from rat liver
    • Yusuf, H., Schwarzmann, G., Pohlentz, G. & Sandhoff, K. 1987 Oligosialogangliosides inhibit GM2- and GD3-synthesis in isolated Golgi vesicles from rat liver. Biol. Chem. 368, 455-462.
    • (1987) Biol. Chem. , vol.368 , pp. 455-462
    • Yusuf, H.1    Schwarzmann, G.2    Pohlentz, G.3    Sandhoff, K.4
  • 183
    • 0032512712 scopus 로고    scopus 로고
    • Secondary structure and limited proteolysis give experimental evidence that the precursor of pulmonary surfactant protein B contains three saposin-like domains
    • Zaltash, S. & Johansson, J. 1998 Secondary structure and limited proteolysis give experimental evidence that the precursor of pulmonary surfactant protein B contains three saposin-like domains. FEBS Lett. 423, 1-4.
    • (1998) FEBS Lett. , vol.423 , pp. 1-4
    • Zaltash, S.1    Johansson, J.2
  • 184
    • 0028168830 scopus 로고
    • Suppressors of the Ca(2+)-sensitive yeast mutant (csg2) identify genes involved in sphingolipid biosynthesis. Cloning and characterization of SCS1, a gene required for serine palmitoyltransferase activity
    • Zhao, V., Beeler, V. & Dunn, V. 1994 Suppressors of the Ca(2+)-sensitive yeast mutant (csg2) identify genes involved in sphingolipid biosynthesis. Cloning and characterization of SCS1, a gene required for serine palmitoyltransferase activity. J. Biol. Chem. 34, 21 480-21 488.
    • (1994) J. Biol. Chem. , vol.34 , pp. 21480-21488
    • Zhao, V.1    Beeler, V.2    Dunn, V.3
  • 186
    • 0028303294 scopus 로고
    • Hydrolysis of lactosylceramide by human galactosylceramidase and GM1-β-galactosidase in a detergent-free system and its stimulation by sphingolipid activator proteins, sap-B and sap-C
    • Zschoche, A., Fürst, W., Schwarzmann, G. & Sandhoff, K. 1994 Hydrolysis of lactosylceramide by human galactosylceramidase and GM1-β-galactosidase in a detergent-free system and its stimulation by sphingolipid activator proteins, sap-B and sap-C. Eur. J. Biochem. 222, 83-90.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 83-90
    • Zschoche, A.1    Fürst, W.2    Schwarzmann, G.3    Sandhoff, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.