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Volumn 274, Issue 13, 2007, Pages 3405-3420

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

Author keywords

Glycosphingolipid; Lipid binding protein; Lysosome; Sap; Saposin

Indexed keywords

ASPARTIC ACID; BIS(MONOACYLGLYCERO)PHOSPHATE; CHOLESTEROL; GLYCOSPHINGOLIPID; HISTIDINE; LIPID; LIPID BINDING PROTEIN; LIPOSOME; PHOSPHORUS DERIVATIVE; RECOMBINANT PROTEIN; SAPOSIN B; SPHINGOLIPID ACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 34347405277     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.05873.x     Document Type: Article
Times cited : (53)

References (72)
  • 1
    • 25444443570 scopus 로고    scopus 로고
    • Principles of lysosomal membrane digestion: Stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids
    • Kolter T 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
  • 2
    • 0037334339 scopus 로고    scopus 로고
    • At the acidic edge: Emerging functions for lysosomal membrane proteins
    • Eskelinen EL, Tanaka Y Saftig P (2003) At the acidic edge: emerging functions for lysosomal membrane proteins. Trends Cell Biol 13, 137 145.
    • (2003) Trends Cell Biol , vol.13 , pp. 137-145
    • Eskelinen, E.L.1    Tanaka, Y.2    Saftig, P.3
  • 3
    • 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
  • 4
    • 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 BC 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
  • 5
    • 0000223691 scopus 로고    scopus 로고
    • Interaction of the GM2-activator protein with phospholipids-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 phospholipids-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
  • 6
    • 0038620205 scopus 로고    scopus 로고
    • Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway
    • Möbius W, van Donselaar E, Ohno-Iwashita Y, Shimada Y, Heijnen HF, Slot JW Geuze HJ (2003) Recycling compartments and the internal vesicles of multivesicular bodies harbor most of the cholesterol found in the endocytic pathway. Traffic 4, 222 231.
    • (2003) Traffic , vol.4 , pp. 222-231
    • Möbius, W.1    Van Donselaar, E.2    Ohno-Iwashita, Y.3    Shimada, Y.4    Heijnen, H.F.5    Slot, J.W.6    Geuze, H.J.7
  • 7
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • Kobayashi T, Stang E, Fang KS, de Moerloose P, Parton RG Gruenberg J (1998) A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 392, 193 197.
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    De Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 8
    • 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
  • 9
    • 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, 455 464.
    • (1982) Eur J Biochem , vol.123 , pp. 455-464
    • Conzelmann, E.1    Burg, J.2    Stephan, G.3    Sandhoff, K.4
  • 10
    • 0018277513 scopus 로고
    • The activator of cerebroside-sulphatase. a model of the activation
    • Fischer G Jatzkewitz H (1978) The activator of cerebroside-sulphatase. A model of the activation. Biochim Biophys Acta 528, 69 76.
    • (1978) Biochim Biophys Acta , vol.528 , pp. 69-76
    • Fischer, G.1    Jatzkewitz, H.2
  • 17
    • 22544463623 scopus 로고    scopus 로고
    • A short guided tour through functional and structural features of saposin-like proteins
    • Bruhn H (2005) A short guided tour through functional and structural features of saposin-like proteins. Biochem J 389, 249 257.
    • (2005) Biochem J , vol.389 , pp. 249-257
    • Bruhn, H.1
  • 18
    • 0029126584 scopus 로고
    • Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure
    • Munford RS, Sheppard PO O'Hara PJ (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
  • 20
    • 29244448306 scopus 로고    scopus 로고
    • Lipid-binding proteins in membrane digestion, antigen presentation, and antimicrobial defense
    • Kolter T, Winau F, Schaible UE, Leippe M 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
  • 23
    • 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, Schröder M, Fürst W, Klein A, Hurwitz R, Zenk T, Weber J, Harzer K, Paton BC, Poulos A et al. (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    Schröder, M.2    Fürst, W.3    Klein, A.4    Hurwitz, R.5    Zenk, T.6    Weber, J.7    Harzer, K.8    Paton, B.C.9    Poulos, A.10
  • 24
    • 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, Cervenkova M, Ledvinova J, Tochackova M, Hrebicek M, Poupetova H, Befekadu A, Berna L, Paton BC, Harzer K et al. (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    Cervenkova, M.2    Ledvinova, J.3    Tochackova, M.4    Hrebicek, M.5    Poupetova, H.6    Befekadu, A.7    Berna, L.8    Paton, B.C.9    Harzer, K.10
  • 26
    • 0029982572 scopus 로고    scopus 로고
    • Targeted disruption of the mouse sphingolipid activator protein gene: A complex phenotype, including severe leukodystrophy and widespread storage of multiple sphingolipids
    • Fujita N, Suzuki K, Vanier MT, Popko B, Maeda N, Klein A, Henseler M, Sandhoff K Nakayasu H (1996) Targeted disruption of the mouse sphingolipid activator protein gene: a complex phenotype, including severe leukodystrophy and widespread storage of multiple sphingolipids. Hum Mol Genet 5, 711 725.
    • (1996) Hum Mol Genet , vol.5 , pp. 711-725
    • Fujita, N.1    Suzuki, K.2    Vanier, M.T.3    Popko, B.4    Maeda, N.5    Klein, A.6    Henseler, M.7    Sandhoff, K.8    Nakayasu, H.9
  • 27
    • 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 JK, Hüttler S, Klein A, Möbius W, Habermann A, Griffiths G 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    Hüttler, S.2    Klein, A.3    Möbius, W.4    Habermann, A.5    Griffiths, G.6    Sandhoff, K.7
  • 28
    • 0021026543 scopus 로고
    • Activator protein for the degradation of globotriaosylceramide by human alpha-galactosidase
    • Gärtner S, Conzelmann E Sandhoff K (1983) Activator protein for the degradation of globotriaosylceramide by human alpha-galactosidase. J Biol Chem 258, 12378 12385.
    • (1983) J Biol Chem , vol.258 , pp. 12378-12385
    • Gärtner, S.1    Conzelmann, E.2    Sandhoff, K.3
  • 29
    • 0018178960 scopus 로고
    • Enzymic hydrolysis of sulphosphingolipids and sulphoglycerolipids by sulphatase a in the presence and absence of activator protein
    • Fischer G, Reiter S Jatzkewitz H (1978) Enzymic hydrolysis of sulphosphingolipids and sulphoglycerolipids by sulphatase A in the presence and absence of activator protein. Hoppe Seylers Z Physiol Chem 359, 863 866.
    • (1978) Hoppe Seylers Z Physiol Chem , vol.359 , pp. 863-866
    • Fischer, G.1    Reiter, S.2    Jatzkewitz, H.3
  • 31
    • 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 SI, 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
  • 32
    • 0025908730 scopus 로고
    • The mechanism for a 33-nucleotide insertion in mRNA causing sphingolipid activator protein (SAP-1)-deficient metachromatic leukodystrophy
    • Zhang XL, Rafi MA, DeGala G Wenger DA (1991) The mechanism for a 33-nucleotide insertion in mRNA causing sphingolipid activator protein (SAP-1)-deficient metachromatic leukodystrophy. Hum Genet 87, 211 215.
    • (1991) Hum Genet , vol.87 , pp. 211-215
    • Zhang, X.L.1    Rafi, M.A.2    Degala, G.3    Wenger, D.A.4
  • 33
    • 0025743034 scopus 로고
    • Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease
    • Holtschmidt H, Sandhoff K, Kwon HY, Harzer K, Nakano T Suzuki K (1991) Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease. J Biol Chem 266, 7556 7560.
    • (1991) J Biol Chem , vol.266 , pp. 7556-7560
    • Holtschmidt, H.1    Sandhoff, K.2    Kwon, H.Y.3    Harzer, K.4    Nakano, T.5    Suzuki, K.6
  • 34
    • 0033061033 scopus 로고    scopus 로고
    • An Asn ? Lys substitution in saposin B involving a conserved amino acidic residue and leading to the loss of the single N-glycosylation site in a patient with metachromatic leukodystrophy and normal arylsulphatase a activity
    • Regis S, Filocamo M, Corsolini F, Caroli F, Keulemans JL, van Diggelen OP Gatti R (1999) An Asn ? Lys substitution in saposin B involving a conserved amino acidic residue and leading to the loss of the single N-glycosylation site in a patient with metachromatic leukodystrophy and normal arylsulphatase A activity. Eur J Hum Genet 7, 125 130.
    • (1999) Eur J Hum Genet , vol.7 , pp. 125-130
    • Regis, S.1    Filocamo, M.2    Corsolini, F.3    Caroli, F.4    Keulemans, J.L.5    Van Diggelen, O.P.6    Gatti, R.7
  • 36
    • 0000857916 scopus 로고    scopus 로고
    • Shingolipid activator proteins
    • In. Scriver, C.R., Beaudet, A.L., Sly, W.S. Valle, D., eds), Vol. 3, pp. McGraw-Hill, New York.
    • Sandhoff K, Kolter T Harzer K (2001) Shingolipid activator proteins. In The Metabolic and Molecular Bases of Inherited Disease (Scriver CR, Beaudet AL, Sly WS Valle D, eds), Vol. 3, pp. 3371 3388. McGraw-Hill, New York.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3371-3388
    • Sandhoff, K.1    Kolter, T.2    Harzer, K.3
  • 37
    • 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 Sandhoff K (2004) Expression of the GM2-activator protein in the methylotrophic yeast Pichia pastoris, purification, isotopic labeling, and biophysical characterization. Protein Expr Purif 34, 147 157.
    • (2004) Protein Expr 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
  • 39
    • 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 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
  • 40
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H von Jagow G (1987) Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166, 368 379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 42
    • 0034650303 scopus 로고    scopus 로고
    • A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors
    • Cooper MA, Hansson A, Löfås S Williams DH (2000) A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors. Anal Biochem 277, 196 205.
    • (2000) Anal Biochem , vol.277 , pp. 196-205
    • Cooper, M.A.1    Hansson, A.2    Löfås, S.3    Williams, D.H.4
  • 44
    • 0035503913 scopus 로고    scopus 로고
    • Roles of calcium ions in the membrane binding of C2 domains
    • Stahelin RV Cho W (2001) Roles of calcium ions in the membrane binding of C2 domains. Biochem J 359, 679 685.
    • (2001) Biochem J , vol.359 , pp. 679-685
    • Stahelin, R.V.1    Cho, W.2
  • 45
    • 0017115403 scopus 로고
    • Bis(monoacylglycero)phosphate - A marker lipid of secondary lysosomes?
    • Stremmel W Debuch H (1976) Bis(monoacylglycero)phosphate - a marker lipid of secondary lysosomes? Hoppe Seylers Z Physiol Chem 357, 803 810.
    • (1976) Hoppe Seylers Z Physiol Chem , vol.357 , pp. 803-810
    • Stremmel, W.1    Debuch, H.2
  • 46
    • 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 Seylers Z Physiol Chem 356, 605 613.
    • (1975) Hoppe Seylers Z Physiol Chem , vol.356 , pp. 605-613
    • Fischer, G.1    Jatzkewitz, H.2
  • 47
    • 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, 13995 14002.
    • (1996) Biochemistry , vol.35 , pp. 13995-14002
    • Amidon, B.1    Brown, A.2    Waite, M.3
  • 48
    • 0024420051 scopus 로고
    • Sphingolipid activator protein deficiency in a 16-week-old atypical Gaucher disease patient and his fetal sibling: Biochemical signs of combined sphingolipidoses
    • Harzer K, Paton BC, Poulos A, Kustermann-Kuhn B, Roggendorf W, Grisar T Popp M (1989) Sphingolipid activator protein deficiency in a 16-week-old atypical Gaucher disease patient and his fetal sibling: biochemical signs of combined sphingolipidoses. 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    Kustermann-Kuhn, B.4    Roggendorf, W.5    Grisar, T.6    Popp, M.7
  • 49
    • 33748474944 scopus 로고    scopus 로고
    • Direct visualization of saposin remodelling of lipid bilayers
    • Alattia JR, Shaw JE, Yip CM Prive GG (2006) Direct visualization of saposin remodelling of lipid bilayers. J Mol Biol 362, 943 953.
    • (2006) J Mol Biol , vol.362 , pp. 943-953
    • Alattia, J.R.1    Shaw, J.E.2    Yip, C.M.3    Prive, G.G.4
  • 50
    • 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 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
  • 51
    • 0016442556 scopus 로고
    • Comparison of the cerebroside sulphatase and the arylsulphatase activity of human sulphatase a in the absence of activators
    • Stinshoff K Jatzkewitz H (1975) Comparison of the cerebroside sulphatase and the arylsulphatase activity of human sulphatase A in the absence of activators. Biochim Biophys Acta 377, 126 138.
    • (1975) Biochim Biophys Acta , vol.377 , pp. 126-138
    • Stinshoff, K.1    Jatzkewitz, H.2
  • 52
    • 0034939951 scopus 로고    scopus 로고
    • Sphingolipid activator proteins: Proteins with complex functions in lipid degradation and skin biogenesis
    • Schuette CG, 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
  • 54
    • 0029417339 scopus 로고
    • PH-dependent conformational properties of saposins and their interactions with phospholipid membranes
    • Vaccaro AM, Ciaffoni F, Tatti M, Salvioli R, Barca A, Tognozzi D Scerch C (1995) pH-dependent conformational properties of saposins and their interactions with phospholipid membranes. J Biol Chem 270, 30576 30580.
    • (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
  • 55
    • 0027263105 scopus 로고
    • Studies on glucosylceramidase binding to phosphatidylserine liposomes: The role of bilayer curvature
    • Vaccaro AM, Tatti M, Ciaffoni F, Salvioli R, Barca A Roncaioli P (1993) Studies on glucosylceramidase binding to phosphatidylserine liposomes: the role of bilayer curvature. Biochim Biophys Acta 1149, 55 62.
    • (1993) Biochim Biophys Acta , vol.1149 , pp. 55-62
    • Vaccaro, A.M.1    Tatti, M.2    Ciaffoni, F.3    Salvioli, R.4    Barca, A.5    Roncaioli, P.6
  • 56
    • 0027494660 scopus 로고
    • Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes
    • Vaccaro AM, Tatti M, Ciaffoni F, Salvioli R, Maras B Barca A (1993) Function of saposin C in the reconstitution of glucosylceramidase by phosphatidylserine liposomes. FEBS Lett 336, 159 162.
    • (1993) FEBS Lett , vol.336 , pp. 159-162
    • Vaccaro, A.M.1    Tatti, M.2    Ciaffoni, F.3    Salvioli, R.4    Maras, B.5    Barca, A.6
  • 58
    • 0018786885 scopus 로고
    • Degradation of bis(monoacylglycero)phosphate by an acid phosphodiesterase in rat liver lysosomes
    • Matsuzawa Y Hostetler KY (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
  • 60
    • 0037468403 scopus 로고    scopus 로고
    • Concurrent increase of cholesterol, sphingomyelin and glucosylceramide in the spleen from non-neurologic Niemann-Pick type C patients but also patients possibly affected with other lipid trafficking disorders
    • Harzer K, Massenkeil G Fröhlich E (2003) Concurrent increase of cholesterol, sphingomyelin and glucosylceramide in the spleen from non-neurologic Niemann-Pick type C patients but also patients possibly affected with other lipid trafficking disorders. FEBS Lett 537, 177 181.
    • (2003) FEBS Lett , vol.537 , pp. 177-181
    • Harzer, K.1    Massenkeil, G.2    Fröhlich, E.3
  • 61
    • 33750318425 scopus 로고    scopus 로고
    • Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport
    • Cheruku SR, Xu Z, Dutia R, Lobel P Storch J (2006) Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport. J Biol Chem 281, 31594 31604.
    • (2006) J Biol Chem , vol.281 , pp. 31594-31604
    • Cheruku, S.R.1    Xu, Z.2    Dutia, R.3    Lobel, P.4    Storch, J.5
  • 63
    • 0023812877 scopus 로고
    • Vectors for efficient expression in mammalian fibroblastoid, myeloid and lymphoid cells via transfection or infection
    • Artelt P, Morelle C, Ausmeier M, Fitzek M Hauser H (1988) Vectors for efficient expression in mammalian fibroblastoid, myeloid and lymphoid cells via transfection or infection. Gene 68, 213 219.
    • (1988) Gene , vol.68 , pp. 213-219
    • Artelt, P.1    Morelle, C.2    Ausmeier, M.3    Fitzek, M.4    Hauser, H.5
  • 64
    • 0029988339 scopus 로고    scopus 로고
    • Expression of the three alternative forms of the sphingolipid activator protein precursor in baby hamster kidney cells and functional assays in a cell culture system
    • Henseler M, Klein A, Glombitza GJ, Suziki K Sandhoff K (1996) Expression of the three alternative forms of the sphingolipid activator protein precursor in baby hamster kidney cells and functional assays in a cell culture system. J Biol Chem 271, 8416 8423.
    • (1996) J Biol Chem , vol.271 , pp. 8416-8423
    • Henseler, M.1    Klein, A.2    Glombitza, G.J.3    Suziki, K.4    Sandhoff, K.5
  • 65
    • 0037753507 scopus 로고    scopus 로고
    • Rapid isolation of yeast chromosomal DNA
    • In. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. Struhl, K., eds), pp. Wiley, New York.
    • Hoffman CS (1997) Rapid isolation of yeast chromosomal DNA. In Current Protocols (Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA Struhl K, eds), pp. 13.112 13.11.4. Wiley, New York.
    • (1997) Current Protocols , pp. 13112-13114
    • Hoffman, C.S.1
  • 66
    • 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
  • 67
    • 0031734879 scopus 로고    scopus 로고
    • A general approach to desalting oligosaccharides released from glycoproteins
    • Packer NH, Lawson MA, Jardine DR Redmond JW (1998) A general approach to desalting oligosaccharides released from glycoproteins. Glycoconj J 15, 737 747.
    • (1998) Glycoconj J , vol.15 , pp. 737-747
    • Packer, N.H.1    Lawson, M.A.2    Jardine, D.R.3    Redmond, J.W.4
  • 69
    • 0028303294 scopus 로고
    • Hydrolysis of lactosylceramide by human galactosylceramidase and GM1-beta-galactosidase in a detergent-free system and its stimulation by sphingolipid activator proteins, sap-B and sap-C. Activator proteins stimulate lactosylceramide hydrolysis
    • Zschoche A, Fürst W, Schwarzmann G Sandhoff K (1994) Hydrolysis of lactosylceramide by human galactosylceramidase and GM1-beta-galactosidase in a detergent-free system and its stimulation by sphingolipid activator proteins, sap-B and sap-C. Activator proteins stimulate lactosylceramide hydrolysis. 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
  • 72
    • 0026153423 scopus 로고
    • Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins
    • Stenberg E, Persson B, Roos H Urbaniczky C (1991) Quantitative determination of surface concentration of protein with surface plasmon resonance using radiolabeled proteins. J Colloid Interface Sci 143, 513 526.
    • (1991) J Colloid Interface Sci , vol.143 , pp. 513-526
    • Stenberg, E.1    Persson, B.2    Roos, H.3    Urbaniczky, C.4


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