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Volumn 4, Issue 2, 2006, Pages 169-181

Synthesis of enzymatically active human α-L-iduronidase in Arabidopsis cgl (complex glycan-deficient) seeds

Author keywords

Enzyme replacement therapy; Human L iduronidase; Lysosomal storage diseases; Molecular farming; N linked glycosylation

Indexed keywords

ALPHA 1,3 MANNOSYL GLYCOPROTEIN BETA 1,2 N ACETYLGLUCOSAMINYLTRANSFERASE I; ALPHA-1,3-MANNOSYL-GLYCOPROTEIN BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE I; HYBRID PROTEIN; LEVO IDURONIDASE; MANNOSE; N ACETYLGLUCOSAMINYLTRANSFERASE; POLYSACCHARIDE;

EID: 33645112692     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1111/j.1467-7652.2005.00166.x     Document Type: Article
Times cited : (45)

References (50)
  • 3
    • 0022199680 scopus 로고
    • Human α
    • l-iduronidase. 1. Purification, monoclonal antibody production, native and subunit molecular mass
    • Clements P.R. Brooks D.A. Saccone G.T.P. Hopwood J.J. 1985 Human α- l -iduronidase. 1. Purification, monoclonal antibody production, native and subunit molecular mass EurJBiochem 152 21 28
    • (1985) EurJBiochem , vol.152 , pp. 21-28
    • Clements, P.R.1    Brooks, D.A.2    Saccone, G.T.P.3    Hopwood, J.J.4
  • 4
    • 0024557985 scopus 로고
    • Immunopurification and characterization of human α
    • l-iduronidase with the use of monoclonal antibodies
    • Clements P.R. Brooks D.A. McCourt P.A.G. Hopwood J.J. 1989 Immunopurification and characterization of human α- l -iduronidase with the use of monoclonal antibodies BiochemJ 259 199 208
    • (1989) BiochemJ , vol.259 , pp. 199-208
    • Clements, P.R.1    Brooks, D.A.2    McCourt, P.A.G.3    Hopwood, J.J.4
  • 5
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough S.J. Bent A.F. 1998 Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana Plant J 16 735 743
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 6
    • 0036901291 scopus 로고    scopus 로고
    • Boosting heterologous protein production in transgenic dicotyledonous seeds using Phaseolus vulgaris regulatory sequences
    • De Jaeger G. Scheffer S. Jacobs A. Zambre M. Zobell O. Goossens A. Depicker A. Angenon G. 2002 Boosting heterologous protein production in transgenic dicotyledonous seeds using Phaseolus vulgaris regulatory sequences NatBiotechnol 20 1265 1268
    • (2002) NatBiotechnol , vol.20 , pp. 1265-1268
    • De Jaeger, G.1    Scheffer, S.2    Jacobs, A.3    Zambre, M.4    Zobell, O.5    Goossens, A.6    Depicker, A.7    Angenon, G.8
  • 7
    • 0036895451 scopus 로고    scopus 로고
    • Enzyme replacement and enhancement therapies: Lessons from lyosomal disorders
    • Desnick R.J. Schuchman E.H. 2002 Enzyme replacement and enhancement therapies: Lessons from lyosomal disorders NatRevGenet 3 954 966
    • (2002) NatRevGenet , vol.3 , pp. 954-966
    • Desnick, R.J.1    Schuchman, E.H.2
  • 8
    • 0000479431 scopus 로고
    • Isolation of plant DNA from fresh tissue
    • Doyle J.J. Doyle J.L. 1990 Isolation of plant DNA from fresh tissue Focus 12 13 15
    • (1990) Focus , vol.12 , pp. 13-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 10
    • 84989674553 scopus 로고
    • Structure, biosynthesis and function of asparagine-linked glycans on plant glycoproteins
    • Faye L. Johnson K.D. Sturm A. Chrispeels M.J. 1989 Structure, biosynthesis and function of asparagine-linked glycans on plant glycoproteins PhysiolPlant 75 309 314
    • (1989) PhysiolPlant , vol.75 , pp. 309-314
    • Faye, L.1    Johnson, K.D.2    Sturm, A.3    Chrispeels, M.J.4
  • 12
    • 0033758021 scopus 로고    scopus 로고
    • Transgenic plants as factories for biopharmaceuticals
    • Giddings G. Allison H. Brooks D. Carter A. 2000 Transgenic plants as factories for biopharmaceuticals NatBiotechnol 18 1151 1155
    • (2000) NatBiotechnol , vol.18 , pp. 1151-1155
    • Giddings, G.1    Allison, H.2    Brooks, D.3    Carter, A.4
  • 13
    • 1542291118 scopus 로고    scopus 로고
    • Posttranslational modification of therapeutic proteins in plants
    • Gomord V. Faye L. 2004 Posttranslational modification of therapeutic proteins in plants CurrOpinPlant Biol 7 171 181
    • (2004) CurrOpinPlant Biol , vol.7 , pp. 171-181
    • Gomord, V.1    Faye, L.2
  • 14
    • 0012081069 scopus 로고
    • Nucleotide sequence of an arcelin 5-I genomic clone from wild Phaseolus vulgaris (accession no. )
    • Goossens A. Ardiles Diaz W. De Keyser A. Van Montagu M. Angenon G. 1995 Nucleotide sequence of an arcelin 5-I genomic clone from wild Phaseolus vulgaris (accession no. ) Plant Physiol 109 722
    • (1995) Plant Physiol , vol.109 , pp. 722
    • Goossens, A.1    Ardiles Diaz, W.2    De Keyser, A.3    Van Montagu, M.4    Angenon, G.5
  • 15
    • 0033179948 scopus 로고    scopus 로고
    • The arcelin-5 gene of Phaseolus vulgaris directs high seed-specific expression in transgenic Phaseolus acutifolius and Arabidopsis plants
    • Goossens A. Dillen W. De Clercq J. Van Montagu M. Angenon G. 1999 The arcelin-5 gene of Phaseolus vulgaris directs high seed-specific expression in transgenic Phaseolus acutifolius and Arabidopsis plants Plant Physiol 20 1095 1104
    • (1999) Plant Physiol , vol.20 , pp. 1095-1104
    • Goossens, A.1    Dillen, W.2    De Clercq, J.3    Van Montagu, M.4    Angenon, G.5
  • 16
    • 0042695870 scopus 로고    scopus 로고
    • Proteases associated with programmed cell death of megagametophyte cells after germination of white spruce (Picea glauca) seeds
    • He X. Kermode A.R. 2003 Proteases associated with programmed cell death of megagametophyte cells after germination of white spruce (Picea glauca) seeds Plant MolBiol 52 729 744
    • (2003) Plant MolBiol , vol.52 , pp. 729-744
    • He, X.1    Kermode, A.R.2
  • 18
    • 0032031347 scopus 로고    scopus 로고
    • Nuclear matrix attachment regions and plant gene expression
    • Holmes-Davis R. Comai L. 1998 Nuclear matrix attachment regions and plant gene expression Trends Plant Sci 3 91 97
    • (1998) Trends Plant Sci , vol.3 , pp. 91-97
    • Holmes-Davis, R.1    Comai, L.2
  • 19
    • 0031460023 scopus 로고    scopus 로고
    • Context sequences of translation initiation codon in plants
    • Joshi C.P. Zhou H. Huang X. Chiang V.L. 1997 Context sequences of translation initiation codon in plants Plant MolBiol 35 993 1001
    • (1997) Plant MolBiol , vol.35 , pp. 993-1001
    • Joshi, C.P.1    Zhou, H.2    Huang, X.3    Chiang, V.L.4
  • 20
    • 0028449393 scopus 로고
    • Overexpression of the human lysosomal enzyme alpha-L-iduronidase in Chinese hamster ovary cells
    • Kakkis E.D. Matynia A. Jonas A.J. Neufeld E.F. 1994 Overexpression of the human lysosomal enzyme alpha-L-iduronidase in Chinese hamster ovary cells Protein ExprPurif 5 225 232
    • (1994) Protein ExprPurif , vol.5 , pp. 225-232
    • Kakkis, E.D.1    Matynia, A.2    Jonas, A.J.3    Neufeld, E.F.4
  • 21
    • 33645111860 scopus 로고
    • Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts
    • Kaplan A. Achord D.T. Sly W.S. 1977 Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts ProcNatlAcadSciU S A 75 1399 1403
    • (1977) ProcNatlAcadSciU S a , vol.75 , pp. 1399-1403
    • Kaplan, A.1    Achord, D.T.2    Sly, W.S.3
  • 23
    • 0036779335 scopus 로고    scopus 로고
    • Regulation of translation initiation in plants
    • Kawaguchi R. Bailey-Serres J. 2002 Regulation of translation initiation in plants CurrOpinPlant Biol 5 460 465
    • (2002) CurrOpinPlant Biol , vol.5 , pp. 460-465
    • Kawaguchi, R.1    Bailey-Serres, J.2
  • 24
    • 0000360614 scopus 로고    scopus 로고
    • Mechanisms of intracellular protein transport and targeting
    • Kermode A.R. 1996 Mechanisms of intracellular protein transport and targeting CritRevPlant Sci 15 285 423
    • (1996) CritRevPlant Sci , vol.15 , pp. 285-423
    • Kermode, A.R.1
  • 25
    • 0028815044 scopus 로고
    • Accumulation and proteolytic processing of vicilin deletion mutant proteins in the leaf and seed of transgenic tobacco
    • Kermode A.R. Fisher S.A. Polishchuk E. Wandelt C. Spencer D. Higgins T.J.V. 1995 Accumulation and proteolytic processing of vicilin deletion mutant proteins in the leaf and seed of transgenic tobacco Planta 197 501 513
    • (1995) Planta , vol.197 , pp. 501-513
    • Kermode, A.R.1    Fisher, S.A.2    Polishchuk, E.3    Wandelt, C.4    Spencer, D.5    Higgins, T.J.V.6
  • 26
    • 0001200134 scopus 로고
    • L-DNA gene 5 controls the tissue-specific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector
    • L-DNA gene 5 controls the tissue-specific expression of chimaeric genes carried by a novel type of Agrobacterium binary vector MolGenGenet 204 383 396
    • (1986) MolGenGenet , vol.204 , pp. 383-396
    • Koncz, C.1    Schell, J.2
  • 28
    • 0000406542 scopus 로고
    • Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins
    • Lauriere M. Lauriere C. Chrispeels M.J. Johnson K.D. Sturm A. 1989 Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins Plant Physiol 90 1182 1188
    • (1989) Plant Physiol , vol.90 , pp. 1182-1188
    • Lauriere, M.1    Lauriere, C.2    Chrispeels, M.J.3    Johnson, K.D.4    Sturm, A.5
  • 31
    • 0141706699 scopus 로고    scopus 로고
    • The production of recombinant pharmacentical proteins in plants
    • Ma J.K. 2003 The production of recombinant pharmacentical proteins in plants Nature Rev. Genet. 4 794 803
    • (2003) Nature Rev. Genet. , vol.4 , pp. 794-803
    • Ma, J.K.1
  • 32
    • 0000869162 scopus 로고    scopus 로고
    • The mucopolysaccharidoses
    • In. McGraw-Hill, Medical Publishing Division New York pp
    • Neufeld E.F. Muenzer J. 2001 The mucopolysaccharidoses In Metabolic and Molecular Bases of Inherited Disease Vol. III 8th edn Scriver C.R. Beaudet A.L. Sly W.S. Valle D. Childs B. Kinzler K.W. Vogelstein B. eds) pp 3421 3452 New York McGraw-Hill, Medical Publishing Division
    • (2001) Metabolic and Molecular Bases of Inherited Disease , vol.3 , pp. 3421-3452
    • Neufeld, E.F.1    Muenzer, J.2
  • 33
    • 0024553944 scopus 로고
    • Purification, characterization and subcellular localization of pig liver alpha-L-iduronidase
    • Ohshita T. Sakuda H. Nakasone S. Iwamasa T. 1989 Purification, characterization and subcellular localization of pig liver alpha-L-iduronidase EurJBiochem 179 201 207
    • (1989) EurJBiochem , vol.179 , pp. 201-207
    • Ohshita, T.1    Sakuda, H.2    Nakasone, S.3    Iwamasa, T.4
  • 34
    • 0034903585 scopus 로고    scopus 로고
    • Processing and localization of bovine β-casein expressed in transgenic soybean seeds under control of a soybean lectin expression cassette
    • Philip R. Darnowski D.W. Maughan P.J. Vodkin L.O. 2001 Processing and localization of bovine β-casein expressed in transgenic soybean seeds under control of a soybean lectin expression cassette Plant Sci 161 323 335
    • (2001) Plant Sci , vol.161 , pp. 323-335
    • Philip, R.1    Darnowski, D.W.2    Maughan, P.J.3    Vodkin, L.O.4
  • 35
    • 33645125207 scopus 로고    scopus 로고
    • Radin D.N. Cramer C.L. Oishi K.K. Weissenborn D.L. 1996 ) Production of lysosomal enzymes in plant-based expression systems. U.S. patent 5929304, filed 13 September 1996, issued 27 July 1999
    • (1996)
    • Radin, D.N.1    Cramer, C.L.2    Oishi, K.K.3    Weissenborn, D.L.4
  • 38
    • 0034871857 scopus 로고    scopus 로고
    • Sequence architecture downstream of the initiator codon enhances gene expression and protein stability in plants
    • Sawant S.V. Kiran K. Singh P.K. Tuli R. 2001 Sequence architecture downstream of the initiator codon enhances gene expression and protein stability in plants Plant Physiol 126 1630 1636
    • (2001) Plant Physiol , vol.126 , pp. 1630-1636
    • Sawant, S.V.1    Kiran, K.2    Singh, P.K.3    Tuli, R.4
  • 39
    • 0027640147 scopus 로고
    • Isolation of a mutant Arabidopsis that lacks N-acetyl glucosaminyl transferase I and is unable to synthesize Golgi-mediated complex N-linked glycans
    • von Schaewen A. Sturm A. O'Neill J. Chrispeels M.J. 1993 Isolation of a mutant Arabidopsis that lacks N-acetyl glucosaminyl transferase I and is unable to synthesize Golgi-mediated complex N-linked glycans Plant Physiol 102 1109 1118
    • (1993) Plant Physiol , vol.102 , pp. 1109-1118
    • Von Schaewen, A.1    Sturm, A.2    O'Neill, J.3    Chrispeels, M.J.4
  • 40
    • 0021343875 scopus 로고
    • Human alpha
    • l-iduronidase. I. Purification and properties of the high uptake (higher molecular weight) and the low uptake (processed) forms
    • Schuchman E.H. Guzman N.A. Desnick R.J. 1984 Human alpha- l -iduronidase. I. Purification and properties of the high uptake (higher molecular weight) and the low uptake (processed) forms JBiolChem 259 3132 3140
    • (1984) JBiolChem , vol.259 , pp. 3132-3140
    • Schuchman, E.H.1    Guzman, N.A.2    Desnick, R.J.3
  • 43
    • 0344094038 scopus 로고
    • Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages
    • Stahl P.D. Rodman J.S. Miller M.J. Schlesinger P.H. 1978 Evidence for receptor-mediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages ProcNatlAcadSciU S A 75 1399 1403
    • (1978) ProcNatlAcadSciU S a , vol.75 , pp. 1399-1403
    • Stahl, P.D.1    Rodman, J.S.2    Miller, M.J.3    Schlesinger, P.H.4
  • 44
    • 17044406723 scopus 로고    scopus 로고
    • Sowing the seeds of success: Pharmaceutical proteins from plants
    • Stoger E. Ma J.K. 2005 Sowing the seeds of success: pharmaceutical proteins from plants Curr. Opin. Biotechnol. 16 167 173
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 167-173
    • Stoger, E.1    Ma, J.K.2
  • 45
    • 17644423487 scopus 로고    scopus 로고
    • Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis plants lacking complex N-glycans
    • Strasser R. Stadlmann J. Svoboda B. Altmann F. Glössl J. Mach L. 2004 Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis plants lacking complex N-glycans BiochemJ. 387 385 391
    • (2004) BiochemJ. , vol.387 , pp. 385-391
    • Strasser, R.1    Stadlmann, J.2    Svoboda, B.3    Altmann, F.4    Glössl, J.5    MacH, L.6
  • 47
    • 0001143106 scopus 로고
    • The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport
    • Vitale A. Ceriotti A. Denecke J. 1993 The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport JExpBot 44 1417 1444
    • (1993) JExpBot , vol.44 , pp. 1417-1444
    • Vitale, A.1    Ceriotti, A.2    Denecke, J.3
  • 49
    • 0347135830 scopus 로고    scopus 로고
    • Lysosomal storage diseases market
    • Werber Y. 2004 Lysosomal storage diseases market NatRev 3 9 10
    • (2004) NatRev , vol.3 , pp. 9-10
    • Werber, Y.1
  • 50
    • 0030954670 scopus 로고    scopus 로고
    • Carbohydrate structures of recombinant human α
    • l-iduronidase secreted by Chinese hamster ovary cells
    • Zhao K.W. Faull K.F. Kakkis E.D. Neufeld E.F. 1997 Carbohydrate structures of recombinant human α- l -iduronidase secreted by Chinese hamster ovary cells JBiolChem 272 22758 22765
    • (1997) JBiolChem , vol.272 , pp. 22758-22765
    • Zhao, K.W.1    Faull, K.F.2    Kakkis, E.D.3    Neufeld, E.F.4


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