메뉴 건너뛰기




Volumn 38, Issue 2, 2013, Pages 300-310

Bovine brain myelin glycerophosphocholine choline phosphodiesterase is an alkaline lysosphingomyelinase of the eNPP-family, regulated by lysosomal sorting

Author keywords

Brain; CNS; Glycoprotein; Lysosomal sorting; Lysosphingomyelin; Myelin; Trafficking

Indexed keywords

AMINO ACID; AUTOTAXIN; GLYCEROPHOSPHOCHOLINE PHOSPHODIESTERASE; GLYCEROPHOSPHORYLCHOLINE; GLYCOPROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL; HOMODIMER; HYDROLASE; LYSOPHOSPHATIDYLCHOLINE; MANNOSE; MONOMER; PHOSPHODIESTERASE VI; PHOSPHOLIPASE C;

EID: 84876415978     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-012-0921-z     Document Type: Article
Times cited : (10)

References (36)
  • 1
    • 0017143565 scopus 로고
    • Some characteristics of sn-glycero-3-phosphocholine diesterases from rat brain
    • 181064 10.1016/0005-2760(76)90227-7 1:CAS:528:DyaE28XksVaktL0%3D
    • Abra RM, Quinn PJ (1976) Some characteristics of sn-glycero-3- phosphocholine diesterases from rat brain. Biochim Biophys Acta 431:631-639
    • (1976) Biochim Biophys Acta , vol.431 , pp. 631-639
    • Abra, R.M.1    Quinn, P.J.2
  • 2
    • 0024436371 scopus 로고
    • Glycerophosphorylcholine phosphocholine phosphodiesterase activity of rat brain myelin
    • 2555532 10.1002/jnr.490240214 1:CAS:528:DyaK3cXltFSisw%3D%3D
    • Kanfer JN, McCartney DG (1989) Glycerophosphorylcholine phosphocholine phosphodiesterase activity of rat brain myelin. J Neurosci Res 24:231-240
    • (1989) J Neurosci Res , vol.24 , pp. 231-240
    • Kanfer, J.N.1    McCartney, D.G.2
  • 3
    • 0023765155 scopus 로고
    • Developmental and regional quantitation of glycerophosphorylcholine phosphodiesterase activities in rat brain
    • 2852307 10.1007/BF00970746 1:CAS:528:DyaL1cXmt1Ogt7o%3D
    • Kanfer JN, McCartney DG (1988) Developmental and regional quantitation of glycerophosphorylcholine phosphodiesterase activities in rat brain. Neurochem Res 13:803-806
    • (1988) Neurochem Res , vol.13 , pp. 803-806
    • Kanfer, J.N.1    McCartney, D.G.2
  • 4
    • 0024477423 scopus 로고
    • Regional and developmental estimations of glycerophosphorylcholine phosphodiesterase activities in rat brain
    • 2540950 10.1159/000111882 1:CAS:528:DyaL1MXhslSkt74%3D
    • Kanfer JN, McCartney DG (1989) Regional and developmental estimations of glycerophosphorylcholine phosphodiesterase activities in rat brain. Dev Neurosci 11:26-29
    • (1989) Dev Neurosci , vol.11 , pp. 26-29
    • Kanfer, J.N.1    McCartney, D.G.2
  • 5
    • 0026541245 scopus 로고
    • Glycerophosphocholine phosphocholine phosphodiesterase activity in cultured oligodendrocytes, astrocytes, and central nervous tissue of dysmyelinating rodent mutants
    • 1319506 10.1002/jnr.490310110 1:CAS:528:DyaK38Xht1KitrY%3D
    • Yuan J, McCartney DG, Monge M, Espinosa LMA, Zalc B, Vellis J, Kanfer JN (1992) Glycerophosphocholine phosphocholine phosphodiesterase activity in cultured oligodendrocytes, astrocytes, and central nervous tissue of dysmyelinating rodent mutants. J Neurosci Res 31:68-74
    • (1992) J Neurosci Res , vol.31 , pp. 68-74
    • Yuan, J.1    McCartney, D.G.2    Monge, M.3    Espinosa, L.M.A.4    Zalc, B.5    Vellis, J.6    Kanfer, J.N.7
  • 6
    • 0027429022 scopus 로고
    • Glycerophosphorylcholine phosphocholine phosphodiesterase activity during the differentiation of glial progenitor cells
    • 8271316 10.1002/jnr.490360410 1:CAS:528:DyaK2cXlslej
    • Monge M, Yuan J, Cabon F, Zalc B, Kanfer JN (1993) Glycerophosphorylcholine phosphocholine phosphodiesterase activity during the differentiation of glial progenitor cells. J Neurosci Res 36:441-445
    • (1993) J Neurosci Res , vol.36 , pp. 441-445
    • Monge, M.1    Yuan, J.2    Cabon, F.3    Zalc, B.4    Kanfer, J.N.5
  • 7
    • 0025039783 scopus 로고
    • Glycerophosphocholine phosphocholine phosphodiesterase is reduced in multiple sclerosis plaques
    • 2165915 10.1016/0014-4886(90)90079-8 1:CAS:528:DyaK3MXlvFyruw%3D%3D
    • Janzen L, Tourtellotte WW, Kanfer JN (1990) Glycerophosphocholine phosphocholine phosphodiesterase is reduced in multiple sclerosis plaques. Exp Neurol 109:243-246
    • (1990) Exp Neurol , vol.109 , pp. 243-246
    • Janzen, L.1    Tourtellotte, W.W.2    Kanfer, J.N.3
  • 8
    • 0026630993 scopus 로고
    • A spectrophotometric assay of Zn(2+)-glycerophosphorylcholine phosphocholine phosphodiesterase using p-nitrophenylphoshorylcholine
    • 1384383 10.1016/0003-2697(92)90303-O 1:CAS:528:DyaK38XlvVKqtbY%3D
    • Sok DE, Kim MR (1992) A spectrophotometric assay of Zn(2+)- glycerophosphorylcholine phosphocholine phosphodiesterase using p-nitrophenylphoshorylcholine. Anal Biochem 203:201-205
    • (1992) Anal Biochem , vol.203 , pp. 201-205
    • Sok, D.E.1    Kim, M.R.2
  • 9
    • 0028009912 scopus 로고
    • Brain myelin-bound Zn(2+)-glycerophosphocholine cholinephosphodiesterase is a glycosylphosphatidylinositol-anchored enzyme of two different molecular forms
    • 8139771 10.1007/BF00966735 1:CAS:528:DyaK2cXhvVGrs7o%3D
    • Sok DE, Kim MR (1994) Brain myelin-bound Zn(2+)-glycerophosphocholine cholinephosphodiesterase is a glycosylphosphatidylinositol-anchored enzyme of two different molecular forms. Neurochem Res 19:97-103
    • (1994) Neurochem Res , vol.19 , pp. 97-103
    • Sok, D.E.1    Kim, M.R.2
  • 10
    • 0029909177 scopus 로고    scopus 로고
    • Properties of a Zn(2+)-glycerophosphocholine cholinephosphodiesterase from bovine brain membranes
    • 8923480 10.1007/BF02532395 1:CAS:528:DyaK28XmtlKntLg%3D
    • Sok DE (1996) Properties of a Zn(2+)-glycerophosphocholine cholinephosphodiesterase from bovine brain membranes. Neurochem Res 21:1193-1199
    • (1996) Neurochem Res , vol.21 , pp. 1193-1199
    • Sok, D.E.1
  • 11
    • 20744450739 scopus 로고    scopus 로고
    • Biochemical and molecular characterisation of a novel choline-specific glycerophosphodiester phosphodiesterase belonging to the nucleotide pyrophosphatase/phosphodiesterase family
    • 15788404 10.1074/jbc.M413438200 1:CAS:528:DC%2BD2MXltVyhur4%3D
    • Sakagami H, Aoki J, Natori Y, Nishikawa K, Kakehi Y, Natori Y, Arai H (2005) Biochemical and molecular characterisation of a novel choline-specific glycerophosphodiester phosphodiesterase belonging to the nucleotide pyrophosphatase/phosphodiesterase family. J Biol Chem 280:23084-23093
    • (2005) J Biol Chem , vol.280 , pp. 23084-23093
    • Sakagami, H.1    Aoki, J.2    Natori, Y.3    Nishikawa, K.4    Kakehi, Y.5    Natori, Y.6    Arai, H.7
  • 12
    • 76849111331 scopus 로고    scopus 로고
    • Purification and characterization of lysophospholipase C from pig brain
    • 19588246 10.1007/s11064-009-0029-2 1:CAS:528:DC%2BD1MXot1Glsrg%3D
    • Hung ND, Kim MR, Sok DE (2010) Purification and characterization of lysophospholipase C from pig brain. Neurochem Res 35:50-59
    • (2010) Neurochem Res , vol.35 , pp. 50-59
    • Hung, N.D.1    Kim, M.R.2    Sok, D.E.3
  • 13
    • 0030921264 scopus 로고    scopus 로고
    • Purification of bovine lysosomal alpha-mannosidase, characterization of its gene and determination of two mutations that cause alpha-mannosidosis
    • 9208932 10.1111/j.1432-1033.1997.00410.x 1:CAS:528:DyaK2sXjvVKiu74%3D
    • Tollersrud OK, Berg T, Healy P, Evjen G, Ramachandran U, Nilssen O (1997) Purification of bovine lysosomal alpha-mannosidase, characterization of its gene and determination of two mutations that cause alpha-mannosidosis. Eur J Biochem 246:410-419
    • (1997) Eur J Biochem , vol.246 , pp. 410-419
    • Tollersrud, O.K.1    Berg, T.2    Healy, P.3    Evjen, G.4    Ramachandran, U.5    Nilssen, O.6
  • 14
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: Signalp 3.0
    • 15223320 10.1016/j.jmb.2004.05.028
    • Bendtsen JD, Nielsen H, von Heijne G, Brunak S (2004) Improved prediction of signal peptides: signalp 3.0. J Mol Biol 340:783-795
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Von Heijne, G.3    Brunak, S.4
  • 15
    • 33747517236 scopus 로고    scopus 로고
    • Structural and functional comparison of nucleotide pyrophosphatase/ phosphodiesterase and alkaline phosphatase: Implication for mechanism and evolution
    • 16893180 10.1021/bi060847t 1:CAS:528:DC%2BD28XntFKlurs%3D
    • Zalatan JG, Fenn TD, Brunger AT, Herschlag D (2006) Structural and functional comparison of nucleotide pyrophosphatase/phosphodiesterase and alkaline phosphatase: implication for mechanism and evolution. Biochemistry 45:9788-9803
    • (2006) Biochemistry , vol.45 , pp. 9788-9803
    • Zalatan, J.G.1    Fenn, T.D.2    Brunger, A.T.3    Herschlag, D.4
  • 17
    • 38449098625 scopus 로고    scopus 로고
    • The N-glycan profile of mouse myelin, a specialized central nervous system membrane
    • 17986136 10.1111/j.1471-4159.2007.04823.x 1:CAS:528:DC%2BD2sXhtl2jur3O
    • Ishii A, Ikenaka K, Pfeiffer SE (2007) The N-glycan profile of mouse myelin, a specialized central nervous system membrane. J Neurochem 103:25-31
    • (2007) J Neurochem , vol.103 , pp. 25-31
    • Ishii, A.1    Ikenaka, K.2    Pfeiffer, S.E.3
  • 18
    • 69849114213 scopus 로고    scopus 로고
    • Myelin proteonomics: Molecular anatomy of an insulating sheath
    • 19452287 10.1007/s12035-009-8071-2 1:CAS:528:DC%2BD1MXnsVyiu78%3D
    • Jahn O, Tenzer S, Werner HB (2009) Myelin proteonomics: molecular anatomy of an insulating sheath. Mol Neurobiol 40:55-72
    • (2009) Mol Neurobiol , vol.40 , pp. 55-72
    • Jahn, O.1    Tenzer, S.2    Werner, H.B.3
  • 19
    • 29144500411 scopus 로고    scopus 로고
    • Profiling of myelin proteins by 2D-gel electrophoresis and multidimensional liquid chromatography coupled to MALDI TOF-TOF mass spectrometry
    • 16335977 10.1021/pr050205c 1:CAS:528:DC%2BD2MXhtVKhtrzK
    • Vanrobaeys F, Van Coster R, Dhondt G, Devreese B, Beeumen J (2005) Profiling of myelin proteins by 2D-gel electrophoresis and multidimensional liquid chromatography coupled to MALDI TOF-TOF mass spectrometry. J Proteome Res 4:2283-2293
    • (2005) J Proteome Res , vol.4 , pp. 2283-2293
    • Vanrobaeys, F.1    Van Coster, R.2    Dhondt, G.3    Devreese, B.4    Beeumen, J.5
  • 20
    • 33751099047 scopus 로고    scopus 로고
    • Functional genomic analysis of oligodendrocyte differentiation
    • 17065439 10.1523/JNEUROSCI.2572-06.2006 1:CAS:528:DC%2BD28XhtFymsLjP
    • Dugas JC, Tai YC, Speed TP, Ngai J, Barres BA (2006) Functional genomic analysis of oligodendrocyte differentiation. J Neurosci 26:10967-10983
    • (2006) J Neurosci , vol.26 , pp. 10967-10983
    • Dugas, J.C.1    Tai, Y.C.2    Speed, T.P.3    Ngai, J.4    Barres, B.A.5
  • 22
    • 41149118457 scopus 로고    scopus 로고
    • On the interpretation of the observed linear free energy relationship in phosphate hydrolysis: A thorough computational study of phosphate diester hydrolysis in solution
    • 18307312 10.1021/bi702106m 1:CAS:528:DC%2BD1cXis1ekt7c%3D
    • Rosta E, Kamerlin SC, Warshel A (2008) On the interpretation of the observed linear free energy relationship in phosphate hydrolysis: a thorough computational study of phosphate diester hydrolysis in solution. Biochemistry 47:3725-3735
    • (2008) Biochemistry , vol.47 , pp. 3725-3735
    • Rosta, E.1    Kamerlin, S.C.2    Warshel, A.3
  • 23
    • 36749072778 scopus 로고    scopus 로고
    • The multifunctional role of sphingosylphosphorylcholine
    • 18042469 10.1016/j.plipres.2007.11.001 1:CAS:528:DC%2BD2sXhsVSmurbK
    • Nixon GM, Mathieson FA, Hunter I (2008) The multifunctional role of sphingosylphosphorylcholine. Prog Lipid Res 47:62-75
    • (2008) Prog Lipid Res , vol.47 , pp. 62-75
    • Nixon, G.M.1    Mathieson, F.A.2    Hunter, I.3
  • 24
    • 0032934036 scopus 로고    scopus 로고
    • Sphingosylphosphorylcholine in Nieman-Pick disease brain: Accumulation in type A but not in type B
    • 9972865 10.1023/A:1022501702403 1:CAS:528:DyaK1MXmt1Oltw%3D%3D
    • Rodriguez-Lafrasse C, Vanier MT (1999) Sphingosylphosphorylcholine in Nieman-Pick disease brain: accumulation in type A but not in type B. Neurochem Res 24:199-205
    • (1999) Neurochem Res , vol.24 , pp. 199-205
    • Rodriguez-Lafrasse, C.1    Vanier, M.T.2
  • 25
    • 0036191897 scopus 로고    scopus 로고
    • Purification, characterization and expression of rat intestinal alkaline sphingomyelinase
    • 11861674 1:CAS:528:DC%2BD38XitVegsL0%3D
    • Cheng Y, Nilsson A, Tomquist E, Duan RD (2002) Purification, characterization and expression of rat intestinal alkaline sphingomyelinase. J Lipid Res 43:316-324
    • (2002) J Lipid Res , vol.43 , pp. 316-324
    • Cheng, Y.1    Nilsson, A.2    Tomquist, E.3    Duan, R.D.4
  • 26
    • 0344053287 scopus 로고    scopus 로고
    • Oligodendrocytes direct glycosyl phosphatidylinositol-anchored proteins to the myelin sheath in glycosphingolipid-rich complexes
    • 9083015 10.1074/jbc.272.16.10558 1:STN:280:DyaK2s3jvVyiug%3D%3D
    • Kramer EM, Koch T, Niehaus A, Trotter J (1997) Oligodendrocytes direct glycosyl phosphatidylinositol-anchored proteins to the myelin sheath in glycosphingolipid-rich complexes. J Biol Chem 272:8937-8945
    • (1997) J Biol Chem , vol.272 , pp. 8937-8945
    • Kramer, E.M.1    Koch, T.2    Niehaus, A.3    Trotter, J.4
  • 27
    • 77949486537 scopus 로고    scopus 로고
    • Myelin, DIGs and membrane rafts in the central nervous system
    • 19379822 10.1016/j.prostaglandins.2009.04.005 1:CAS:528: DC%2BC3cXjslSiu7s%3D
    • Dupree JL, Pomicter AD (2010) Myelin, DIGs and membrane rafts in the central nervous system. Prostaglandins Other Lipid Mediat 91:118-129
    • (2010) Prostaglandins Other Lipid Mediat , vol.91 , pp. 118-129
    • Dupree, J.L.1    Pomicter, A.D.2
  • 28
    • 78649761056 scopus 로고    scopus 로고
    • Sphingolipids in multiple sclerosis
    • 20607622 10.1007/s12017-010-8128-4 1:CAS:528:DC%2BC3cXhsVegurjJ
    • Jana A, Pahan K (2010) Sphingolipids in multiple sclerosis. Neuromolecular Med 12:351-361
    • (2010) Neuromolecular Med , vol.12 , pp. 351-361
    • Jana, A.1    Pahan, K.2
  • 29
    • 34247495740 scopus 로고    scopus 로고
    • An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D
    • 17307740 10.1074/jbc.M611503200 1:CAS:528:DC%2BD2sXjvFagsLY%3D
    • Jansen S, Callewaert N, Dewerte I, Andries M, Ceulemans H, Bollen M (2007) An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D. J Biol Chem 282:11084-11091
    • (2007) J Biol Chem , vol.282 , pp. 11084-11091
    • Jansen, S.1    Callewaert, N.2    Dewerte, I.3    Andries, M.4    Ceulemans, H.5    Bollen, M.6
  • 31
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • 3896128 10.1146/annurev.bi.54.070185.003215 1:STN:280: DyaL2M3nvVSjsA%3D%3D
    • Kornfeld R, Kornfeld S (1985) Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem 54:631-664
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 32
    • 0023753261 scopus 로고
    • Biosynthesis of the mannose 6-phosphate recognition marker in transport-impaired mouse lymphoma cells. Demonstration of a two-step phosphorylation
    • 2968980 1:CAS:528:DyaL1cXkslSqtL8%3D
    • Lazzarino DA, Gabel CA (1988) Biosynthesis of the mannose 6-phosphate recognition marker in transport-impaired mouse lymphoma cells. Demonstration of a two-step phosphorylation. J Biol Chem 263:10118-10126
    • (1988) J Biol Chem , vol.263 , pp. 10118-10126
    • Lazzarino, D.A.1    Gabel, C.A.2
  • 33
    • 0030055178 scopus 로고    scopus 로고
    • Dephosphorylation of the mannose-6-phosphate recognition marker is localized in late compartments of the endocytic route
    • 10.1111/j.1432-1033.1996.0669w.x
    • Brescani R, von Figura K (1996) Dephosphorylation of the mannose-6-phosphate recognition marker is localized in late compartments of the endocytic route. Eur J Biochem 238:669-674
    • (1996) Eur J Biochem , vol.238 , pp. 669-674
    • Brescani, R.1    Von Figura, K.2
  • 34
    • 0032529137 scopus 로고    scopus 로고
    • The structures of asparagine-linked oligosaccharides of rat liver cathepsin L reflect the substrate specificity of lysosomal alpha-mannosidase
    • 9746360 10.1046/j.1432-1327.1998.2560163.x 1:CAS:528:DyaK1cXlslCmu7Y%3D
    • Towatari T, Miyamura T, Kondo A, Kato I, Inoue M, Kido H (1998) The structures of asparagine-linked oligosaccharides of rat liver cathepsin L reflect the substrate specificity of lysosomal alpha-mannosidase. Eur J Biochem 256:163-169
    • (1998) Eur J Biochem , vol.256 , pp. 163-169
    • Towatari, T.1    Miyamura, T.2    Kondo, A.3    Kato, I.4    Inoue, M.5    Kido, H.6
  • 35
    • 0030042401 scopus 로고    scopus 로고
    • Structural basis of trimannoside recognition by concanavalin A
    • 8557713 10.1074/jbc.271.2.972 1:CAS:528:DyaK28XksFOgug%3D%3D
    • Naismith JH, Field RA (1996) Structural basis of trimannoside recognition by concanavalin A. J Biol Chem 271:972-976
    • (1996) J Biol Chem , vol.271 , pp. 972-976
    • Naismith, J.H.1    Field, R.A.2
  • 36
    • 0032573201 scopus 로고    scopus 로고
    • Human DNase i contains mannose 6-phosphate and binds the cation-dependent mannose 6-phosphate receptor
    • 9790679 10.1021/bi981465t 1:CAS:528:DyaK1cXmsValtbg%3D
    • Cacia J, Quan CP, Pai R, Frenz J (1998) Human DNase I contains mannose 6-phosphate and binds the cation-dependent mannose 6-phosphate receptor. Biochemistry 37:15154-15161
    • (1998) Biochemistry , vol.37 , pp. 15154-15161
    • Cacia, J.1    Quan, C.P.2    Pai, R.3    Frenz, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.