메뉴 건너뛰기




Volumn 20, Issue 2, 2009, Pages 248-259

Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines

Author keywords

Arylsulfatase A; Enzyme replacement therapy; Mannose 6 phosphate; Metachromatic leukodystrophy

Indexed keywords

MANNOSE; MANNOSE 6 PHOSPHATE; OLIGOSACCHARIDE; RECOMBINANT ENZYME; RECOMBINANT LYSOSOMAL ARYLSULFATASE A; UNCLASSIFIED DRUG; CEREBROSIDE SULFATASE; RECOMBINANT PROTEIN;

EID: 77649219919     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwp171     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 0035087502 scopus 로고    scopus 로고
    • Do rodent and human brains have different N-glycosylation patterns?
    • Albach C, Klein RA, Schmitz B. 2001. Do rodent and human brains have different N-glycosylation patterns? Biol Chem. 382(2):187-194.
    • (2001) Biol Chem , vol.382 , Issue.2 , pp. 187-194
    • Albach, C.1    Klein, R.A.2    Schmitz, B.3
  • 2
    • 0028061380 scopus 로고
    • The effect of cell culture conditions on oligosaccharide structures of secreted glycoproteins
    • Andersen DC, Goochee CF. 1994. The effect of cell culture conditions on oligosaccharide structures of secreted glycoproteins. Current Opin Biotech. 5(5):546-549.
    • (1994) Current Opin Biotech , vol.5 , Issue.5 , pp. 546-549
    • Andersen, D.C.1    Goochee, C.F.2
  • 3
    • 9144261693 scopus 로고    scopus 로고
    • The glycosylation of human serum IgD and IgE and the accessibility of identified oligomannose structures for interaction with mannan-binding lectin1
    • Arnold JN, Radcliffe CM, Wormald MR, Royle L, Harvey DJ, Crispin M, Dwek RA, Sim RB, Rudd PM. 2004. The glycosylation of human serum IgD and IgE and the accessibility of identified oligomannose structures for interaction with mannan-binding lectin1. J Immunol. 173(11):6831-6840.
    • (2004) J Immunol , vol.173 , Issue.11 , pp. 6831-6840
    • Arnold, J.N.1    Radcliffe, C.M.2    Wormald, M.R.3    Royle, L.4    Harvey, D.J.5    Crispin, M.6    Dwek, R.A.7    Sim, R.B.8    Rudd, P.M.9
  • 4
    • 33947198645 scopus 로고    scopus 로고
    • New therapeutic options for lysosomal storage disorders: Enzyme replacement, small molecules and gene therapy
    • Beck M. 2007. New therapeutic options for lysosomal storage disorders: Enzyme replacement, small molecules and gene therapy. Hum Genet. 121(1):1-22.
    • (2007) Hum Genet , vol.121 , Issue.1 , pp. 1-22
    • Beck, M.1
  • 5
    • 0033579440 scopus 로고    scopus 로고
    • Advantages of using the same species for enzyme replacement therapy in a feline model of mucopolysaccharidosis VI
    • Bielicki J, Crawley AC, Davey RC, Varnai JC, Hopwood JJ. 1999. Advantages of using the same species for enzyme replacement therapy in a feline model of mucopolysaccharidosis VI. J Biol Chem. 274(51):36335-36343.
    • (1999) J Biol Chem , vol.274 , Issue.51 , pp. 36335-36343
    • Bielicki, J.1    Crawley, A.C.2    Davey, R.C.3    Varnai, J.C.4    Hopwood, J.J.5
  • 6
    • 0020643218 scopus 로고
    • Measurement of chemical phosphate in proteins
    • Buss JE, Stull JT. 1983. Measurement of chemical phosphate in proteins. Methods Enzymol. 99, 7-14.
    • (1983) Methods Enzymol , vol.99 , pp. 7-14
    • Buss, J.E.1    Stull, J.T.2
  • 9
    • 33646159287 scopus 로고    scopus 로고
    • Site-specific glycosylation analysis of the bovine lysosomal alpha-mannosidase
    • Faid V, Evjen G, Tollersrud OK, Michalski JC, Morelle W. 2006. Site-specific glycosylation analysis of the bovine lysosomal alpha-mannosidase. Glycobiology. 16(5):440-461.
    • (2006) Glycobiology , vol.16 , Issue.5 , pp. 440-461
    • Faid, V.1    Evjen, G.2    Tollersrud, O.K.3    Michalski, J.C.4    Morelle, W.5
  • 10
    • 0023373075 scopus 로고
    • Carbohydrates as antigenic determinants of glycoproteins
    • Feizi T, Childs RA. 1987. Carbohydrates as antigenic determinants of glycoproteins. Biochem J. 245(1):1-11.
    • (1987) Biochem J , vol.245 , Issue.1 , pp. 1-11
    • Feizi, T.1    Childs, R.A.2
  • 11
    • 0024497455 scopus 로고
    • Survival of recombinant erythrpoetin in the circulation: The role of carbohydrates
    • Fukuda MN, Sasaki H, Lopez H, Fukuda M. 1986. Survival of recombinant erythrpoetin in the circulation: The role of carbohydrates. Blood. 73(1):84-89.
    • (1986) Blood , vol.73 , Issue.1 , pp. 84-89
    • Fukuda, M.N.1    Sasaki, H.2    Lopez, H.3    Fukuda, M.4
  • 12
    • 0029014545 scopus 로고
    • Effect of different cell culture conditions on the polypeptide integrity andN-glycosylation of a recombinant model protein
    • Gawlitzek M, Conradt HS, Wagner R. 1995. Effect of different cell culture conditions on the polypeptide integrity andN-glycosylation of a recombinant model protein. Biotechnol Bioeng. 46(6):536-544.
    • (1995) Biotechnol Bioeng , vol.46 , Issue.6 , pp. 536-544
    • Gawlitzek, M.1    Conradt, H.S.2    Wagner, R.3
  • 13
    • 0026776768 scopus 로고
    • In vitromutagenesis of potential N-glycosylation sites of arylsulfatase A. Effects on glycosylation, phosphorylation, and intracellular sorting
    • Gieselmann V, Schmidt B, von Figura K. 1992. In vitromutagenesis of potential N-glycosylation sites of arylsulfatase A. Effects on glycosylation, phosphorylation, and intracellular sorting. J Biol Chem. 267(19):13262-13266.
    • (1992) J Biol Chem , vol.267 , Issue.19 , pp. 13262-13266
    • Gieselmann, V.1    Schmidt, B.2    von Figura, K.3
  • 14
    • 0027628305 scopus 로고
    • Glycosidase activities in Chinese hamster ovary cell lysate and cell culture supernatant
    • Gramer MJ, Goochee CF. 1993. Glycosidase activities in Chinese hamster ovary cell lysate and cell culture supernatant. Biotechnol Prog. 9(4):366-373.
    • (1993) Biotechnol Prog , vol.9 , Issue.4 , pp. 366-373
    • Gramer, M.J.1    Goochee, C.F.2
  • 15
    • 0029053768 scopus 로고
    • Removal of sialic acid from a glycoprotein in CHO cell culture supernatant by action of an extracellular CHO cell sialidase
    • Gramer MJ, Goochee CF, Chock VY, Brousseau DT, Sliwkowski MB. 1995. Removal of sialic acid from a glycoprotein in CHO cell culture supernatant by action of an extracellular CHO cell sialidase. Biotechnology (NY). 13(7):692-698.
    • (1995) Biotechnology (NY) , vol.13 , Issue.7 , pp. 692-698
    • Gramer, M.J.1    Goochee, C.F.2    Chock, V.Y.3    Brousseau, D.T.4    Sliwkowski, M.B.5
  • 16
    • 40649102937 scopus 로고    scopus 로고
    • Chemically modified beta-glucuronidase crosses blood-brain barrier and clears neuronal storage in murine mucopolysaccharidosis VII
    • Grubb JH, Vogler C, Levy B, Galvin N, Tan Y, Sly WS. 2008. Chemically modified beta-glucuronidase crosses blood-brain barrier and clears neuronal storage in murine mucopolysaccharidosis VII. Proc Natl Acad Sci USA. 105(7):2616-2621.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.7 , pp. 2616-2621
    • Grubb, J.H.1    Vogler, C.2    Levy, B.3    Galvin, N.4    Tan, Y.5    Sly, W.S.6
  • 17
    • 0030571019 scopus 로고    scopus 로고
    • A rapid highresolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles
    • Guile GR, Rudd PM, Wing DR, Prime SB, Dwek RA. 1996. A rapid highresolution high-performance liquid chromatographic method for separating glycan mixtures and analyzing oligosaccharide profiles. Anal Biochem. 240(2):210-226.
    • (1996) Anal Biochem , vol.240 , Issue.2 , pp. 210-226
    • Guile, G.R.1    Rudd, P.M.2    Wing, D.R.3    Prime, S.B.4    Dwek, R.A.5
  • 18
    • 0343963050 scopus 로고    scopus 로고
    • High mannose type oligosaccharides from human placental arylsulfatase A are core fucosylated as confirmed by MALDI MS
    • Hoja-Lukowicz D, Ciolczyk D, Bergquist J, Litynska A, Laidler P. 2000. High mannose type oligosaccharides from human placental arylsulfatase A are core fucosylated as confirmed by MALDI MS. Glycobiology. 10(6):551-557.
    • (2000) Glycobiology , vol.10 , Issue.6 , pp. 551-557
    • Hoja-Lukowicz, D.1    Ciolczyk, D.2    Bergquist, J.3    Litynska, A.4    Laidler, P.5
  • 19
    • 0020491102 scopus 로고
    • Structural studies of the endoglycosidase H-resistant oligosaccharides present on human beta-glucuronidase
    • Howard DR, Natowicz M, Baenziger JU. 1982. Structural studies of the endoglycosidase H-resistant oligosaccharides present on human beta-glucuronidase. J Biol Chem. 257(18):10861-10868.
    • (1982) J Biol Chem , vol.257 , Issue.18 , pp. 10861-10868
    • Howard, D.R.1    Natowicz, M.2    Baenziger, J.U.3
  • 20
    • 17644422131 scopus 로고    scopus 로고
    • Gaucher disease: Pathological mechanisms and modern management
    • Jmoudiak M, Futerman AH. 2005. Gaucher disease: Pathological mechanisms and modern management. Br J Haematol. 129(2):178-88.
    • (2005) Br J Haematol , vol.129 , Issue.2 , pp. 178-188
    • Jmoudiak, M.1    Futerman, A.H.2
  • 23
    • 0030906665 scopus 로고    scopus 로고
    • Arylsulfatase A from human placenta possesses only high mannose-type glycans
    • Laidler P, Litynska A. 1997. Arylsulfatase A from human placenta possesses only high mannose-type glycans. Int J Biochem Cell Biol. 29(3):475-483.
    • (1997) Int J Biochem Cell Biol , vol.29 , Issue.3 , pp. 475-483
    • Laidler, P.1    Litynska, A.2
  • 26
    • 0033810516 scopus 로고    scopus 로고
    • Infusion of recombinant human acid sphingomyelinase into niemann-pick disease mice leads to visceral, but not neurological, correction of the pathophysiology
    • Miranda SR, He X, Simonaro CM, Gatt S, Dagan A, Desnick RJ, Schuchman EH. 2000. Infusion of recombinant human acid sphingomyelinase into niemann-pick disease mice leads to visceral, but not neurological, correction of the pathophysiology. FASEB J. 14(13):1988-1995.
    • (2000) FASEB J , vol.14 , Issue.13 , pp. 1988-1995
    • Miranda, S.R.1    He, X.2    Simonaro, C.M.3    Gatt, S.4    Dagan, A.5    Desnick, R.J.6    Schuchman, E.H.7
  • 27
    • 68149132035 scopus 로고    scopus 로고
    • Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases
    • Pohl S, Marschner K, Storch S, Braulke T. 2009. Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases. Biol Chem. 390(7):521-527.
    • (2009) Biol Chem , vol.390 , Issue.7 , pp. 521-527
    • Pohl, S.1    Marschner, K.2    Storch, S.3    Braulke, T.4
  • 30
    • 0035900762 scopus 로고    scopus 로고
    • Biodistribution, kinetics and efficacy of highly phosphorylated and non-phospharylated β-glucuronidase in the murine model of mucopolysaccharidosis VII
    • Sands MS, Vogler CA, Ohlemiller KK, RobertsMS, Grubb JH, Levy B, Sly WS. 2001. Biodistribution, kinetics and efficacy of highly phosphorylated and non-phospharylated β-glucuronidase in the murine model of mucopolysaccharidosis VII. J Biol Chem. 276(46):43160-43165.
    • (2001) J Biol Chem , vol.276 , Issue.46 , pp. 43160-43165
    • Sands, M.S.1    Vogler, C.A.2    Ohlemiller, K.K.3    Roberts, M.S.4    Grubb, J.H.5    Levy, B.6    Sly, W.S.7
  • 31
    • 0033525178 scopus 로고    scopus 로고
    • Interaction of arylsulfatase A with UDP-N-acetylglucosamine: Lysosomal enzyme-N-acetylglucosamine-1-1-phosphotransferase
    • Schierau A, Dietz F, Lange H, Schestag F, Parastar A, Gieselmann V. 1999. Interaction of arylsulfatase A with UDP-N-acetylglucosamine: Lysosomal enzyme-N-acetylglucosamine-1-1-phosphotransferase. J Biol Chem. 274(6):3651-3658.
    • (1999) J Biol Chem , vol.274 , Issue.6 , pp. 3651-3658
    • Schierau, A.1    Dietz, F.2    Lange, H.3    Schestag, F.4    Parastar, A.5    Gieselmann, V.6
  • 32
    • 0029130352 scopus 로고
    • A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
    • Schmidt B, Selmer T, Ingendoh A, von Figura K. 1995. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 82(2):271-278.
    • (1995) Cell , vol.82 , Issue.2 , pp. 271-278
    • Schmidt, B.1    Selmer, T.2    Ingendoh, A.3    von Figura, K.4
  • 33
    • 0036980794 scopus 로고    scopus 로고
    • Enzyme replacement therapy: From concept to clinical practice
    • Sly WS. 2002. Enzyme replacement therapy: From concept to clinical practice. Acta Paediatr Suppl. 439:71-78.
    • (2002) Acta Paediatr Suppl , vol.439 , pp. 71-78
    • Sly, W.S.1
  • 35
    • 24344441296 scopus 로고    scopus 로고
    • Transport of lysosomal enzymes
    • Saftig P, editor. Georgetown (USA): Landes Bioscience
    • Storch S, Braulke T. 2005. Transport of lysosomal enzymes. In: Saftig P, editor. Lysosomes. Georgetown (USA): Landes Bioscience p. 17-26.
    • (2005) Lysosomes , pp. 17-26
    • Storch, S.1    Braulke, T.2
  • 36
    • 55949098538 scopus 로고    scopus 로고
    • Acid phosphatase 5 is responsible for removing the mannose 6-phosphate recognition marker from lysosomal proteins
    • Sun P, Sleat DE, Lecocq M, Hayman AR, Jadot M, Lobel P. 2008. Acid phosphatase 5 is responsible for removing the mannose 6-phosphate recognition marker from lysosomal proteins. Proc Natl Acad Sci USA. 105(43):16590-16595.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.43 , pp. 16590-16595
    • Sun, P.1    Sleat, D.E.2    Lecocq, M.3    Hayman, A.R.4    Jadot, M.5    Lobel, P.6
  • 37
    • 0021099335 scopus 로고
    • Oligosaccharide units of lysosomal cathepsin D from porcine spleen. Amino acid sequence and carbohydrate structure of the glycopeptides
    • Takahashi T, Schmidt PG, Tang J. 1983. Oligosaccharide units of lysosomal cathepsin D from porcine spleen. Amino acid sequence and carbohydrate structure of the glycopeptides. J Biol Chem. 258(5):2819-2830.
    • (1983) J Biol Chem , vol.258 , Issue.5 , pp. 2819-2830
    • Takahashi, T.1    Schmidt, P.G.2    Tang, J.3
  • 38
    • 0021949477 scopus 로고
    • Structural studies on the carbohydrate moieties of rat liver cathepsins B and H
    • Taniguchi T, Mizuochi T, Towatari T, Katunuma N, Kobata A. 1985. Structural studies on the carbohydrate moieties of rat liver cathepsins B and H. J Biochem (Tokyo). 97(3):973-976.
    • (1985) J Biochem (Tokyo) , vol.97 , Issue.3 , pp. 973-976
    • Taniguchi, T.1    Mizuochi, T.2    Towatari, T.3    Katunuma, N.4    Kobata, A.5
  • 39
    • 0000497407 scopus 로고    scopus 로고
    • Metachromatic leukodystrophy
    • Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW, Vogelstein B, editors. New York (USA): McGraw-Hill
    • von Figura K, Gieselmann V, Jaeken J. 2001. Metachromatic leukodystrophy. In: Scriver CR, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW, Vogelstein B, editors. The Metabolic and Molecular Bases of Inherited Disease. New York (USA): McGraw-Hill. p. 3695-3724.
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3695-3724
    • von Figura, K.1    Gieselmann, V.2    Jaeken, J.3
  • 40
    • 0025789667 scopus 로고
    • Purification and characterization of GDP-L-fucose-N-acetyl β-D-glucosaminde a 1,6 fucosyltransferase
    • VOYNOW AA, KAISER RS, SCANLIN TF, GLICK MC. 1991. Purification and characterization of GDP-L-fucose-N-acetyl β-D-glucosaminde a 1,6 fucosyltransferase. J Biol Chem. 266(32):21572-21577.
    • (1991) J Biol Chem , vol.266 , Issue.32 , pp. 21572-21577
    • Voynow, A.A.1    Kaiser, R.S.2    Scanlin, T.F.3    Glick, M.C.4
  • 41
    • 0024368285 scopus 로고
    • The asialoglycoprotein receptor: Properties and modulation by ligand
    • Weiss P, Ashwell G. 1989. The asialoglycoprotein receptor: Properties and modulation by ligand. Prog Clin Biol Res. 300:169-184.
    • (1989) Prog Clin Biol Res , vol.300 , pp. 169-184
    • Weiss, P.1    Ashwell, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.