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Volumn 25, Issue 6, 2005, Pages 2431-2440

The exon 8-containing prosaposin gene splice variant is dispensable for mouse development, lysosomal function, and secretion

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CERAMIDE; GANGLIOSIDE; GLUTAMINE; GLYCOSPHINGOLIPID; HYDROLASE; ISOPROTEIN; LYSOSOME ENZYME; NEUROTROPHIC FACTOR; PHOSPHOLIPID; PROSAPOSIN; SPHINGOLIPID; SPHINGOLIPID ACTIVATOR PROTEIN; SULFATIDE;

EID: 14844363960     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.6.2431-2440.2005     Document Type: Article
Times cited : (17)

References (68)
  • 2
    • 0033001385 scopus 로고    scopus 로고
    • Exposure of human, boar, or bull sperm to a synthetic peptide increases binding to an egg-membrane substrate
    • Amann, R. P., R. H. Hammerstedt, and R. B. Shabanowitz. 1999. Exposure of human, boar, or bull sperm to a synthetic peptide increases binding to an egg-membrane substrate. J. Androl. 20:34-41.
    • (1999) J. Androl. , vol.20 , pp. 34-41
    • Amann, R.P.1    Hammerstedt, R.H.2    Shabanowitz, R.B.3
  • 3
    • 1842558602 scopus 로고    scopus 로고
    • Molecular mechanisms of glutamate-dependent neurodegeneration in ischemia and traumatic brain injury
    • Arundine, M., and M. Tymianski. 2004. Molecular mechanisms of glutamate-dependent neurodegeneration in ischemia and traumatic brain injury. Cell. Mol. Life Sci. 61:657-668.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 657-668
    • Arundine, M.1    Tymianski, M.2
  • 4
    • 0033801428 scopus 로고    scopus 로고
    • A procedure for fractionation of sphingolipid classes by solid-phase extraction on aminopropyl cartridges
    • Bodennec, J., O. Koul, I. Aguado, G. Brichon, G. Zwingelstein, and J. Portoukalian. 2000. A procedure for fractionation of sphingolipid classes by solid-phase extraction on aminopropyl cartridges. J. Lipid Res. 41:1524-1531.
    • (2000) J. Lipid Res. , vol.41 , pp. 1524-1531
    • Bodennec, J.1    Koul, O.2    Aguado, I.3    Brichon, G.4    Zwingelstein, G.5    Portoukalian, J.6
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0017599450 scopus 로고
    • The activator of cerebroside sulphatase. Binding studies with enzyme and substrate demonstrating the detergent function of the activator protein
    • Fischer, G., and H. Jatzkewitz. 1977. The activator of cerebroside sulphatase. Binding studies with enzyme and substrate demonstrating the detergent function of the activator protein. Biochim. Biophys. Acta 481:561-572.
    • (1977) Biochim. Biophys. Acta , vol.481 , pp. 561-572
    • Fischer, G.1    Jatzkewitz, H.2
  • 9
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • Folch, J., M. Lees, and G. H. Sloane Stanley. 1957. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226:497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3
  • 11
    • 0029982572 scopus 로고    scopus 로고
    • Targeted disruption of the mouse sphingolipid activator protein gene: A complex phenotype, including severe leukodystrophy and wide-spread storage of multiple sphingolipids
    • Fujita, N., K. Suzuki, M. T. Vanier, B. Popko, N. Maeda, A. Klein, M. Henseler, K. Sandhoff, H. Nakayasu, and K. Suzuki. 1996. Targeted disruption of the mouse sphingolipid activator protein gene: a complex phenotype, including severe leukodystrophy and wide-spread 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    Suzuki, K.10
  • 12
    • 0038350695 scopus 로고    scopus 로고
    • Structural requirements for lysosomal targeting of the prosaposin precursor protein
    • Ham, D. 2003. Structural requirements for lysosomal targeting of the prosaposin precursor protein. Cell Biol. Int. 27:675-687.
    • (2003) Cell Biol. Int. , vol.27 , pp. 675-687
    • Ham, D.1
  • 13
    • 0035050467 scopus 로고    scopus 로고
    • A fragment of prosaposin (SGP-1) from rooster sperm promotes sperm-egg binding and improves fertility in chickens
    • Hammerstedt, R. H., P. G. Cramer, G. F. Barbate, R. P. Amann, J. S. O'Brien, and M. D. Griswold. 2001. A fragment of prosaposin (SGP-1) from rooster sperm promotes sperm-egg binding and improves fertility in chickens. J. Androl. 22:361-375.
    • (2001) J. Androl. , vol.22 , pp. 361-375
    • Hammerstedt, R.H.1    Cramer, P.G.2    Barbate, G.F.3    Amann, R.P.4    O'Brien, J.S.5    Griswold, M.D.6
  • 14
    • 0029059790 scopus 로고
    • Rescue of the En-1 mutant phenotype by replacement of En-1 with En-2
    • Hanks, M., W. Wurst, L. Anson-Cartwright, A. B. Auerbach, and A. L. Joyner. 1995. Rescue of the En-1 mutant phenotype by replacement of En-1 with En-2. Science 269:679-682.
    • (1995) Science , vol.269 , pp. 679-682
    • Hanks, M.1    Wurst, W.2    Anson-Cartwright, L.3    Auerbach, A.B.4    Joyner, A.L.5
  • 15
    • 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., B. C. Paton, A. Poulos, B. Kustermann-Kuhn, W. Roggendorf, T. Grisar, and M. Popp. 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
  • 16
    • 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., A. Klein, G. J. Glombitza, K. Suziki, and K. Sandhoff. 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
  • 18
    • 0033152846 scopus 로고    scopus 로고
    • Prosaposin: A myelinotrophic protein that promotes expression of myelin constituents and is secreted after nerve injury
    • Hiraiwa, M., W. M. Cam pana, A. P. Mizisin, L. Mohiuddin, and J. S. O'Brien. 1999. Prosaposin: a myelinotrophic protein that promotes expression of myelin constituents and is secreted after nerve injury. Glia 26:353-360.
    • (1999) Glia , vol.26 , pp. 353-360
    • Hiraiwa, M.1    Cam Pana, W.M.2    Mizisin, A.P.3    Mohiuddin, L.4    O'Brien, J.S.5
  • 19
    • 0043023931 scopus 로고    scopus 로고
    • Regulation of gene expression in response to brain injury: Enhanced expression and alternative splicing of rat prosaposin (SGP-1) mRNA in injured brain
    • Hiraiwa, M., J. Liu, A. G. Lu, C. Y. Wang, R. Misasi, T. Yamauchi, I. Hozumi, T. Inuzuka, and J. S. O'Brien. 2003. Regulation of gene expression in response to brain injury: enhanced expression and alternative splicing of rat prosaposin (SGP-1) mRNA in injured brain. J. Neurotrauma 20:755-765.
    • (2003) J. Neurotrauma , vol.20 , pp. 755-765
    • Hiraiwa, M.1    Liu, J.2    Lu, A.G.3    Wang, C.Y.4    Misasi, R.5    Yamauchi, T.6    Hozumi, I.7    Inuzuka, T.8    O'Brien, J.S.9
  • 20
    • 0027177509 scopus 로고
    • Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins)
    • Hiraiwa, M., J. S. O'Brien, Y. Kishimoto, M. Galdzicka, A. L. Fluharty, E. I. Ginns, and B. M. Martin. 1993. Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins). Arch. Biochem. Biophys. 304:110-116.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 110-116
    • Hiraiwa, M.1    O'Brien, J.S.2    Kishimoto, Y.3    Galdzicka, M.4    Fluharty, A.L.5    Ginns, E.I.6    Martin, B.M.7
  • 22
    • 0030971534 scopus 로고    scopus 로고
    • Cell death prevention, mitogen-activated protein kinase stimulation, and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptides
    • Hiraiwa, M., E. M. Taylor, W. M. Campana, S. J. Darin, and J. S. O'Brien. 1997. Cell death prevention, mitogen-activated protein kinase stimulation, and increased sulfatide concentrations in Schwann cells and oligodendrocytes by prosaposin and prosaptides. 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, S.J.4    O'Brien, J.S.5
  • 23
    • 0025743034 scopus 로고
    • Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease
    • Holtschmidt, H., K. Sandhoff, H. Y. Kwon, K. Harzer, T. Nakano, and K. Suzuki. 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
  • 25
    • 0141540782 scopus 로고    scopus 로고
    • Kainate receptors and synaptic transmission
    • Huettner, J. E. 2003. Kainate receptors and synaptic transmission. Prog. Neurobiol. 70:387-407.
    • (2003) Prog. Neurobiol. , vol.70 , pp. 387-407
    • Huettner, J.E.1
  • 26
    • 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., M. Cervenkova, J. Ledvinova, M. Tochackova, M. Hrebicek, H. Poupetova, A. Befekadu, L. Berna, B. C. Paton, K. Harzer, A. Boor, F. Smid, and M. Elleder. 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    Boor, A.11    Smid, F.12    Elleder, M.13
  • 27
    • 0026768211 scopus 로고
    • Saposins: Structure, function, distribution, and molecular genetics
    • Kishimoto, Y., M. Hiraiwa, and J. S. O'Brien. 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
  • 28
    • 0028275240 scopus 로고
    • Sphingolipid activator protein D (Sap-D) stimulates the lysosomal degradation of ceramide in-vivo
    • Klein, A., M. Henseler, C. Klein, K. Suzuki, K. Harzer, and K. Sandhoff. 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
  • 32
    • 0027967290 scopus 로고
    • Modulation of human saposin B sphingolipid-binding specificity by alternative splicing. A study with saposin B-derived synthetic peptides
    • Lamontagne, S., and M. Potier. 1994. Modulation of human saposin B sphingolipid-binding specificity by alternative splicing. A study with saposin B-derived synthetic peptides. J. Biol. Chem. 269:20528-20532.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20528-20532
    • Lamontagne, S.1    Potier, M.2
  • 33
    • 0030016109 scopus 로고    scopus 로고
    • Proteolytic processing patterns of prosaposin in insect and mammalian cells
    • Leonova, T., X. Qi, A. Bencosme, E. Ponce, Y. Sun, and G. A. Grabowski. 1996. Proteolytic processing patterns of prosaposin in insect and mammalian cells. J. Biol. Chem. 271:17312-17320.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17312-17320
    • Leonova, T.1    Qi, X.2    Bencosme, A.3    Ponce, E.4    Sun, Y.5    Grabowski, G.A.6
  • 34
    • 0033987611 scopus 로고    scopus 로고
    • Two Pax2/5/8-binding sites in Engrailed2 are required for proper initiation of endogenous mid-hindbrain expression
    • Li Song, D., and A. L. Joyner. 2000. Two Pax2/5/8-binding sites in Engrailed2 are required for proper initiation of endogenous mid-hindbrain expression. Mech. Dev. 90:155-165.
    • (2000) Mech. Dev. , vol.90 , pp. 155-165
    • Li Song, D.1    Joyner, A.L.2
  • 36
    • 8444224225 scopus 로고    scopus 로고
    • Mutation in saposin D domain of sphingolipid activator protein gene causes urinary system defects and cerebellar Purkinje cell degeneration with accumulation of hydroxy fatty acid-containing ceramide in the mouse
    • Matsuda, J., M. Kido, K. Tadano-Aritomi, I. Ishizuka, K. Tominaga, K. Toida, E. Takeda, K. Suzuki, and Y. Kuroda. 2004. Mutation in saposin D domain of sphingolipid activator protein gene causes urinary system defects and cerebellar Purkinje cell degeneration with accumulation of hydroxy fatty acid-containing ceramide in the mouse. Hum. Mol. Genet. 13:2709-2723.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2709-2723
    • Matsuda, J.1    Kido, M.2    Tadano-Aritomi, K.3    Ishizuka, I.4    Tominaga, K.5    Toida, K.6    Takeda, E.7    Suzuki, K.8    Kuroda, Y.9
  • 37
    • 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., M. T. Vanier, Y. Saito, J. Tohyama, and K. Suzuki. 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
  • 38
    • 0030831586 scopus 로고    scopus 로고
    • Regulation of the secretion and synthesis of rat Sertoli cell SGP-1, SGP-2 and CP-2 by elongate spermatids
    • McKinnell, C., and R. M. Sharpe. 1997. Regulation of the secretion and synthesis of rat Sertoli cell SGP-1, SGP-2 and CP-2 by elongate spermatids. Int. J. Androl. 20:171-179.
    • (1997) Int. J. Androl. , vol.20 , pp. 171-179
    • McKinnell, C.1    Sharpe, R.M.2
  • 40
    • 0037357780 scopus 로고    scopus 로고
    • Prosaposin ablation inactivates the MAPK and Akt signaling pathways and interferes with the development of the prostate gland
    • Morales, C. R., and H. Badran. 2003. Prosaposin ablation inactivates the MAPK and Akt signaling pathways and interferes with the development of the prostate gland. Asian J. Androl. 5:57-63.
    • (2003) Asian J. Androl. , vol.5 , pp. 57-63
    • Morales, C.R.1    Badran, H.2
  • 41
    • 14444269453 scopus 로고    scopus 로고
    • Distribution of mouse sulfated glycoprotein-1 (prosaposin) in the testis and other tissues
    • Morales, C. R., N. Hay, M. El-Alfy, and Q. Zhao. 1998. Distribution of mouse sulfated glycoprotein-1 (prosaposin) in the testis and other tissues. J. Androl. 19:156-164.
    • (1998) J. Androl. , vol.19 , pp. 156-164
    • Morales, C.R.1    Hay, N.2    El-Alfy, M.3    Zhao, Q.4
  • 42
    • 0033764584 scopus 로고    scopus 로고
    • Targeted drsruption of the mouse prosaposin gene affects the development of the prostate gland and other male reproductive organs
    • Morales, C. R., Q. Zhao, M. El-Alfy, and K. Suzuki. 2000. Targeted drsruption of the mouse prosaposin gene affects the development of the prostate gland and other male reproductive organs. J. Androl. 21:765-775.
    • (2000) J. Androl. , vol.21 , pp. 765-775
    • Morales, C.R.1    Zhao, Q.2    El-Alfy, M.3    Suzuki, K.4
  • 43
    • 0035203559 scopus 로고    scopus 로고
    • Protective effect of a prosaposin-derived. 18-mer peptide on slowly progressive neuronal degeneration after brief ischemia
    • Morita, F., T. C. Wen, J. Tanaka, R. Hata, J. Desaki, K. Sato, K. Nakata, Y. J. Ma, and M. Sakanaka. 2001. Protective effect of a prosaposin-derived. 18-mer peptide on slowly progressive neuronal degeneration after brief ischemia. J. Cereb. Blood Flow Metab. 21:1295-1302.
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 1295-1302
    • Morita, F.1    Wen, T.C.2    Tanaka, J.3    Hata, R.4    Desaki, J.5    Sato, K.6    Nakata, K.7    Ma, Y.J.8    Sakanaka, M.9
  • 44
    • 0024593996 scopus 로고
    • Structure of full-length cDNA coding for sulfatide activator, a co-beta-glucosidase and two other homologous proteins: Two alternate forms of the sulfatide activator
    • Tokyo
    • Nakano, T., K. Sandhoff, J. Stumper, H. Christomanou, and K. Suzuki. 1989. Structure of full-length cDNA coding for sulfatide activator, a co-beta-glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator. J. Biochem. (Tokyo) 105:152-154.
    • (1989) J. Biochem. , vol.105 , pp. 152-154
    • Nakano, T.1    Sandhoff, K.2    Stumper, J.3    Christomanou, H.4    Suzuki, K.5
  • 47
    • 0027192992 scopus 로고
    • Mutational analysis in a patient with a variant form of Gaucher disease caused by SAP-2 deficiency
    • Rafi, M. A., G. de Gala, X. L. Zhang, and D. A. Wenger. 1993. Mutational analysis in a patient with a variant form of Gaucher disease caused by SAP-2 deficiency. Somat. Cell Mol. Genet. 19:1-7.
    • (1993) Somat. Cell Mol. Genet. , vol.19 , pp. 1-7
    • Rafi, M.A.1    De Gala, G.2    Zhang, X.L.3    Wenger, D.A.4
  • 48
    • 0025017535 scopus 로고
    • Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy
    • Rafi, M. A., X. L. Zhang, G. DeGala, and D. A. Wenger. 1990. Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy. Biochem. Biophys. Res. Commun. 166:1017-1023.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 1017-1023
    • Rafi, M.A.1    Zhang, X.L.2    DeGala, G.3    Wenger, D.A.4
  • 49
    • 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., M. Filocamo, F. Corsolini, F. Caroli, J. L. Keulemans, O. P. van Diggelen, and R. Gatti. 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
  • 51
    • 0000956850 scopus 로고
    • Sphingolipid activator proteins
    • S. Scriber, A. Beaudet, W. Sly, and D. Valle (ed.), McGraw-Hill, New York, N.Y.
    • Sandhoff, K., K. Harzer, and W. Furst. 1995. Sphingolipid activator proteins, p. 2427-2441. In S. Scriber, A. Beaudet, W. Sly, and D. Valle (ed.), The metabolic and molecular basis of inherited disease, 7th ed. McGraw-Hill, New York, N.Y.
    • (1995) The Metabolic and Molecular Basis of Inherited Disease, 7th Ed. , pp. 2427-2441
    • Sandhoff, K.1    Harzer, K.2    Furst, W.3
  • 52
    • 0037762571 scopus 로고    scopus 로고
    • Biosynthesis and degradation of mammalian glycosphingolipids
    • Sandhoff, K., and T. Kolter. 2003. Biosynthesis and degradation of mammalian glycosphingolipids. Philos. Trans. R. Soc. Lond. B Biol. Sci. 358:847-861.
    • (2003) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.358 , pp. 847-861
    • Sandhoff, K.1    Kolter, T.2
  • 55
    • 20244362501 scopus 로고
    • Sphingolipid activator protein 1 deficiency in metachromatic leucodystrophy with normal arylsulphatase A activity. A clinical, morphological, biochemical, and immunological study
    • Schlote, W., K. Harzer, H. Christomanou, B. C. Paton, B. Kustermann-Kuhn, B. Schmid, J. Seeger, U. Beudt, I. Schuster, and U. Langenbeck. 1991. Sphingolipid activator protein 1 deficiency in metachromatic leucodystrophy with normal arylsulphatase A activity. A clinical, morphological, biochemical, and immunological study. Eur. J. Pediatr. 150:584-591.
    • (1991) Eur. J. Pediatr. , vol.150 , pp. 584-591
    • Schlote, W.1    Harzer, K.2    Christomanou, H.3    Paton, B.C.4    Kustermann-Kuhn, B.5    Schmid, B.6    Seeger, J.7    Beudt, U.8    Schuster, I.9    Langenbeck, U.10
  • 57
    • 0025762364 scopus 로고
    • Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease
    • Schnabel, D., M. Schroder, and K. Sandhoff. 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    Schroder, M.2    Sandhoff, K.3
  • 58
    • 0013650617 scopus 로고
    • Murine prosaposin: Expression in the reproductive system of a gene implicated in human genetic diseases
    • Sprecher-Levy, H., A. Orr-Urtreger, P. Lonai, and M. Horowitz. 1993. Murine prosaposin: expression in the reproductive system of a gene implicated in human genetic diseases. Cell. Mol. Biol. (Noisy-Le-Grand) 39:287-299.
    • (1993) Cell. Mol. Biol. (Noisy-Le-Grand) , vol.39 , pp. 287-299
    • Sprecher-Levy, H.1    Orr-Urtreger, A.2    Lonai, P.3    Horowitz, M.4
  • 59
    • 0024822494 scopus 로고
    • Sulfated glycoprotein-1 (saposin precursor) in the reproductive tract of the male rat
    • Sylvester, S. R., C. Morales, R. Oko, and M. D. Griswold. 1989. Sulfated glycoprotein-1 (saposin precursor) in the reproductive tract of the male rat. Biol. Reprod. 41:941-948.
    • (1989) Biol. Reprod. , vol.41 , pp. 941-948
    • Sylvester, S.R.1    Morales, C.2    Oko, R.3    Griswold, M.D.4
  • 60
    • 0032190625 scopus 로고    scopus 로고
    • Prosaposin prevents programmed cell death of rat cerebellar granule neurons in culture
    • Tsuboi, K., M. Hiraiwa, and J. S. O'Brien. 1998. Prosaposin prevents programmed cell death of rat cerebellar granule neurons in culture. Brain Res. Dev. Brain Res. 110:249-255.
    • (1998) Brain Res. Dev. Brain Res. , vol.110 , pp. 249-255
    • Tsuboi, K.1    Hiraiwa, M.2    O'Brien, J.S.3
  • 61
    • 33847517624 scopus 로고
    • The use of Sephadex for the removal of nonlipid contaminants from lipid extracts
    • Wells, M. A., and J. C. Dittmer. 1963. The use of Sephadex for the removal of nonlipid contaminants from lipid extracts. Biochemistry 172:1259-1263.
    • (1963) Biochemistry , vol.172 , pp. 1259-1263
    • Wells, M.A.1    Dittmer, J.C.2
  • 63
    • 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., M. Henseler, S. Huettler, S. I. Pascual Pascual, A. Chabas, and K. Sandhoff. 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
  • 64
    • 0002429430 scopus 로고
    • Production of targeted embryonic stem cell clones
    • A. L. Joyner (ed.), IRL Press, Oxford, United Kingdom
    • Wurst, W., and A. L. Joyner. 1993. Production of targeted embryonic stem cell clones, p. 33-61. In A. L. Joyner (ed.), Gene targeting: a practical approach. IRL Press, Oxford, United Kingdom.
    • (1993) Gene Targeting: A Practical Approach , pp. 33-61
    • Wurst, W.1    Joyner, A.L.2
  • 65
    • 0017759258 scopus 로고
    • Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle
    • Yaffe, D., and O. Saxel. 1977. Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle. Nature 270:725-727.
    • (1977) Nature , vol.270 , pp. 725-727
    • Yaffe, D.1    Saxel, O.2
  • 66
    • 3042841585 scopus 로고    scopus 로고
    • Comparative clinico-pathological study of saposin-A-deficient (SAP-A-/-) and Twitcher mice
    • Yagi, T., J. Matsuda, S. Takikita, I. Mohri, and K. Suzuki. 2004. Comparative clinico-pathological study of saposin-A-deficient (SAP-A-/-) and Twitcher mice. J. Neuropathol. Exp. Neurol. 63:721-734.
    • (2004) J. Neuropathol. Exp. Neurol. , vol.63 , pp. 721-734
    • Yagi, T.1    Matsuda, J.2    Takikita, S.3    Mohri, I.4    Suzuki, K.5
  • 67
    • 0025908730 scopus 로고
    • The mechanism for a 33-nucleotide insertion in mRNA causing sphingolipid activator protein (SAP-1)-deficient metachromatic leukodystrophy
    • Zhang, X. L., M. A. Rafi, G. DeGala, and D. A. Wenger. 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
  • 68
    • 0030745853 scopus 로고    scopus 로고
    • Structural analysis of the mouse prosaposin (SGP-1) gene reveals the presence of an exon that is alternatively spliced in transcribed mRNAs
    • Zhao, Q., N. Hay, and C. R. Morales. 1997. Structural analysis of the mouse prosaposin (SGP-1) gene reveals the presence of an exon that is alternatively spliced in transcribed mRNAs. Mol. Reprod. Dev. 48:1-8.
    • (1997) Mol. Reprod. Dev. , vol.48 , pp. 1-8
    • Zhao, Q.1    Hay, N.2    Morales, C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.