메뉴 건너뛰기




Volumn 7, Issue 1, 2009, Pages 33-48

Expression of rat β(1,4)-N-acetylglucosaminyltransferase III in Nicotiana tabacum remodels the plant-specific N-glycosylation

Author keywords

(1,3) fucose; (1,2) xylose; (1,4) N acetylglucosaminyltransferase III; Glycoengineering; Localization; Plant N linked glycosylation

Indexed keywords

BETA 1,4 MANNOSYL GLYCOPROTEIN BETA 1,4 N ACETYLGLUCOSAMINYLTRANSFERASE; BETA-1,4-MANNOSYL-GLYCOPROTEIN BETA-1,4-N-ACETYLGLUCOSAMINYLTRANSFERASE; FUCOSE; MANNOSIDASE; MANNOSYL OLIGOSACCHARIDE 1,3 1,6 ALPHA MANNOSIDASE; MANNOSYL-OLIGOSACCHARIDE 1,3 - 1,6-ALPHA-MANNOSIDASE; N ACETYLGLUCOSAMINYLTRANSFERASE; POLYSACCHARIDE; VEGETABLE PROTEIN; XYLOSE;

EID: 57649129498     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1111/j.1467-7652.2008.00370.x     Document Type: Article
Times cited : (46)

References (43)
  • 2
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes, core alpha (1,3)-fucose and core xylose
    • Bardor, M., Faveeuw, C., Fitchette, A.C., Gilbert, D., Galas, L., Trottein, F., Faye, L. Lerouge, P. (2003) Immunoreactivity in mammals of two typical plant glyco-epitopes, core alpha (1,3)-fucose and core xylose. Glycobiology, 13, 427 434.
    • (2003) Glycobiology , vol.13 , pp. 427-434
    • Bardor, M.1    Faveeuw, C.2    Fitchette, A.C.3    Gilbert, D.4    Galas, L.5    Trottein, F.6    Faye, L.7    Lerouge, P.8
  • 3
    • 20544454097 scopus 로고    scopus 로고
    • Arabidopsis thaliana beta1,2-xylosyltransferase: An unusual glycosyltransferase with the potential to act at multiple stages of the plant N-glycosylation pathway
    • Bencur, P., Steinkellner, H., Svoboda, B., Mucha, J., Strasser, R., Kolarich, D., Hann, S., Kollensperger, G., Glossl, J., Altmann, F. Mach, L. (2005) Arabidopsis thaliana beta1,2-xylosyltransferase: an unusual glycosyltransferase with the potential to act at multiple stages of the plant N-glycosylation pathway. Biochem. J. 388, 515 525.
    • (2005) Biochem. J. , vol.388 , pp. 515-525
    • Bencur, P.1    Steinkellner, H.2    Svoboda, B.3    Mucha, J.4    Strasser, R.5    Kolarich, D.6    Hann, S.7    Kollensperger, G.8    Glossl, J.9    Altmann, F.10    MacH, L.11
  • 4
    • 0036891653 scopus 로고    scopus 로고
    • Analysis of cis-sequence of subgenomic transcript promoter from the Figwort mosaic virus and comparison of promoter activity with the cauliflower mosaic virus promoters in monocot and dicot cells
    • Bhattacharyya, S., Dey, N. Maiti, I.B. (2002) Analysis of cis-sequence of subgenomic transcript promoter from the Figwort mosaic virus and comparison of promoter activity with the cauliflower mosaic virus promoters in monocot and dicot cells. Virus Res. 90, 47 62.
    • (2002) Virus Res. , vol.90 , pp. 47-62
    • Bhattacharyya, S.1    Dey, N.2    Maiti, I.B.3
  • 5
    • 0346038834 scopus 로고    scopus 로고
    • Intron-mediated enhancement of gene expression in transgenic plants using chimeric constructs composed of the Peanut chlorotic streak virus (PClSV) promoter-leader and the antisense orientation of PClSV ORF VII (p7R)
    • Bhattacharyya, S., Pattanaik, S. Maiti, I.B. (2003) Intron-mediated enhancement of gene expression in transgenic plants using chimeric constructs composed of the Peanut chlorotic streak virus (PClSV) promoter-leader and the antisense orientation of PClSV ORF VII (p7R). Planta, 218, 115 124.
    • (2003) Planta , vol.218 , pp. 115-124
    • Bhattacharyya, S.1    Pattanaik, S.2    Maiti, I.B.3
  • 6
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantification of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford, M.M. (1976) Rapid and sensitive method for quantification of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 72, 248 254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0027453187 scopus 로고
    • Affinity purification of antibodies specific for Asn-linked glycans containing alpha 1→3 fucose or beta 1→2 xylose
    • Faye, L., Gomord, V., Fitchette-Laine, A.C. Chrispeels, M.J. (1993) Affinity purification of antibodies specific for Asn-linked glycans containing alpha 1→3 fucose or beta 1→2 xylose. Anal. Biochem. 209, 104 108.
    • (1993) Anal. Biochem. , vol.209 , pp. 104-108
    • Faye, L.1    Gomord, V.2    Fitchette-Laine, A.C.3    Chrispeels, M.J.4
  • 9
    • 14744298421 scopus 로고    scopus 로고
    • Protein modifications in the plant secretory pathway: Current status and practical implications in molecular pharming
    • Faye, L., Boulaflous, A., Benchabane, M., Gomord, V. Michaud, D. (2005) Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming. Vaccine, 23, 1770 1778.
    • (2005) Vaccine , vol.23 , pp. 1770-1778
    • Faye, L.1    Boulaflous, A.2    Benchabane, M.3    Gomord, V.4    Michaud, D.5
  • 10
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co-expression of heterologous beta1,4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II
    • Ferrara, C., Brünker, P., Suter, T., Moser, S., Püntener, U. Umaña, P. (2006) Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1,4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II. Biotechnol. Bioeng. 93, 851 861.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 851-861
    • Ferrara, C.1    Brünker, P.2    Suter, T.3    Moser, S.4    Püntener, U.5    Umaña, P.6
  • 11
    • 10644248642 scopus 로고    scopus 로고
    • Expression of Vitreoscilla haemoglobin in tobacco cell cultures relieves nitrosative stress in vivo and protects from NO in vitro
    • Frey, A.D., Oberle, B.T., Farrés, J. Kallio, P.T. (2004) Expression of Vitreoscilla haemoglobin in tobacco cell cultures relieves nitrosative stress in vivo and protects from NO in vitro. Plant Biotechnol. J. 2, 221 231.
    • (2004) Plant Biotechnol. J. , vol.2 , pp. 221-231
    • Frey, A.D.1    Oberle, B.T.2    Farrés, J.3    Kallio, P.T.4
  • 12
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • Hodoniczky, J., Zheng, Y.Z. James, D.C. (2005) Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro. Biotechnol. Prog. 21, 1644 1652.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1644-1652
    • Hodoniczky, J.1    Zheng, Y.Z.2    James, D.C.3
  • 13
    • 0020574525 scopus 로고
    • A binary plant vector strategy based on separation of vir- and T-region of the Agrobacterium tumefaciens Ti-plasmid
    • Hoekema, A., Hirsch, P.R., Hooykaas, P.J.J. Schilperoort, R.A. (1983) A binary plant vector strategy based on separation of vir- and T-region of the Agrobacterium tumefaciens Ti-plasmid. Nature, 303, 179 180.
    • (1983) Nature , vol.303 , pp. 179-180
    • Hoekema, A.1    Hirsch, P.R.2    Hooykaas, P.J.J.3    Schilperoort, R.A.4
  • 16
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among non-fucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: The high-mannose, hybrid, and complex types
    • Kanda, Y., Yamada, T., Mori, K., Okazaki, A., Inoue, M., Kitajima-Miyama, K., Kuni-Kamochi, R., Nakano, R., Yano, K., Kakita, S., Shitara, K. Satoh, M. (2007) Comparison of biological activity among non-fucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types. Glycobiology, 17, 104 118.
    • (2007) Glycobiology , vol.17 , pp. 104-118
    • Kanda, Y.1    Yamada, T.2    Mori, K.3    Okazaki, A.4    Inoue, M.5    Kitajima-Miyama, K.6    Kuni-Kamochi, R.7    Nakano, R.8    Yano, K.9    Kakita, S.10    Shitara, K.11    Satoh, M.12
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature, 227, 680 &.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 21
    • 0031104851 scopus 로고    scopus 로고
    • Promoter/leader deletion analysis and plant expression vectors with the figwort mosaic virus (FMV) full length transcript (FLt) promoter containing single or double enhancer domains
    • Maiti, I.B., Gowda, S., Kiernan, J., Ghosh, S.K. Shepherd, R.J. (1997) Promoter/leader deletion analysis and plant expression vectors with the figwort mosaic virus (FMV) full length transcript (FLt) promoter containing single or double enhancer domains. Transgenic Res. 6, 143 156.
    • (1997) Transgenic Res. , vol.6 , pp. 143-156
    • Maiti, I.B.1    Gowda, S.2    Kiernan, J.3    Ghosh, S.K.4    Shepherd, R.J.5
  • 22
    • 0020373041 scopus 로고
    • Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide beta-1,4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides
    • Narasimhan, S. (1982) Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide beta-1,4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides. J. Biol. Chem. 257, 10 235 10 242.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10235-10242
    • Narasimhan, S.1
  • 23
    • 0029158550 scopus 로고
    • Strength and tissue-specificity of chimeric promoters derived from the octopine and mannopine synthase genes
    • Ni, M., Cui, D., Einstein, J., Narasimhulu, S., Vergara, C.E. Gelvin, S.B. (1995) Strength and tissue-specificity of chimeric promoters derived from the octopine and mannopine synthase genes. Plant J. 7, 661 676.
    • (1995) Plant J. , vol.7 , pp. 661-676
    • Ni, M.1    Cui, D.2    Einstein, J.3    Narasimhulu, S.4    Vergara, C.E.5    Gelvin, S.B.6
  • 24
    • 0026705382 scopus 로고
    • Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase III from rat kidney
    • Nishikawa, A., Ihara, Y., Hatakeyama, M., Kangawa, K. Taniguchi, N. (1992) Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine: beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase III from rat kidney. J. Biol. Chem. 267, 18 199 18 204.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18199-18204
    • Nishikawa, A.1    Ihara, Y.2    Hatakeyama, M.3    Kangawa, K.4    Taniguchi, N.5
  • 25
    • 0019390652 scopus 로고
    • Grown gall plant tumours of abnormal morphology, induced by Agrobacterium tumefaciens carrying mutated octopine Ti plasmids; Analysis of T-DNA functions
    • Ooms, G., Hooykaas, P.J., Moolenaar, G. Schilperoort, R.A. (1981) Grown gall plant tumours of abnormal morphology, induced by Agrobacterium tumefaciens carrying mutated octopine Ti plasmids; analysis of T-DNA functions. Gene, 14, 33 50.
    • (1981) Gene , vol.14 , pp. 33-50
    • Ooms, G.1    Hooykaas, P.J.2    Moolenaar, G.3    Schilperoort, R.A.4
  • 27
    • 0033551250 scopus 로고    scopus 로고
    • Stable expression of human beta1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns
    • Palacpac, N.Q., Yoshida, S., Sakai, H., Kimura, Y., Fujiyama, K., Yoshida, T. Seki, T. (1999) Stable expression of human beta1,4- galactosyltransferase in plant cells modifies N-linked glycosylation patterns. Proc. Natl. Acad. Sci. USA, 96, 4692 4697.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4692-4697
    • Palacpac, N.Q.1    Yoshida, S.2    Sakai, H.3    Kimura, Y.4    Fujiyama, K.5    Yoshida, T.6    Seki, T.7
  • 30
    • 34250346068 scopus 로고    scopus 로고
    • From planta to pharma with glycosylation in the toolbox
    • Saint-Jore-Dupas, C., Faye, L. Gomord, V. (2007) From planta to pharma with glycosylation in the toolbox. Trends Biotechnol. 25, 317 323.
    • (2007) Trends Biotechnol. , vol.25 , pp. 317-323
    • Saint-Jore-Dupas, C.1    Faye, L.2    Gomord, V.3
  • 31
    • 0032032778 scopus 로고    scopus 로고
    • Synthesis of bisected glycoforms of recombinant IFN-beta by over-expression of beta-1,4-N-acetylglucosaminyltransferase III in Chinese hamster ovary cells
    • Sburlati, A.R., Umaña, P., Prati, E.G. Bailey, J.E. (1998) Synthesis of bisected glycoforms of recombinant IFN-beta by over-expression of beta-1,4-N-acetylglucosaminyltransferase III in Chinese hamster ovary cells. Biotechnol. Prog. 14, 189 192.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 189-192
    • Sburlati, A.R.1    Umaña, P.2    Prati, E.G.3    Bailey, J.E.4
  • 32
    • 0021014033 scopus 로고
    • Control of branching during the biosynthesis of asparagine-linked oligosaccharides
    • Schachter, H., Narasimhan, S., Gleeson, P. Vella, G. (1983) Control of branching during the biosynthesis of asparagine-linked oligosaccharides. Can. J. Biochem. Cell Biol. 61, 1049 1066.
    • (1983) Can. J. Biochem. Cell Biol. , vol.61 , pp. 1049-1066
    • Schachter, H.1    Narasimhan, S.2    Gleeson, P.3    Vella, G.4
  • 33
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., Hanai, N. Shitara, K. (2003) The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 278, 3466 3473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 35
    • 1542358140 scopus 로고    scopus 로고
    • Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose
    • Strasser, R., Altmann, F., Mach, L., Glössl, J. Steinkellner, H. (2004) Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose. FEBS Lett. 561, 132 136.
    • (2004) FEBS Lett. , vol.561 , pp. 132-136
    • Strasser, R.1    Altmann, F.2    MacH, L.3    Glössl, J.4    Steinkellner, H.5
  • 36
    • 33644865777 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Arabidopsis thaliana Golgi alpha-mannosidase II, a key enzyme in the formation of complex N-glycans in plants
    • Strasser, R., Schoberer, J., Jin, C., Glössl, J., Mach, L. Steinkellner, H. (2006) Molecular cloning and characterization of Arabidopsis thaliana Golgi alpha-mannosidase II, a key enzyme in the formation of complex N-glycans in plants. Plant J. 45, 789 803.
    • (2006) Plant J. , vol.45 , pp. 789-803
    • Strasser, R.1    Schoberer, J.2    Jin, C.3    Glössl, J.4    MacH, L.5    Steinkellner, H.6
  • 39
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Umaña, P., Jean-Mairet, J., Moudry, R., Amstutz, H. Bailey, J.E. (1999) Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat. Biotechnol. 17, 176 180.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 176-180
    • Umaña, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5
  • 42
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology, 3, 97 130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 43
    • 0033214207 scopus 로고    scopus 로고
    • Cytokine-release syndrome in patients with B-cell chronic lymphocytic leukaemia and high lymphocyte counts after treatment with an anti-CD20 monoclonal antibody (rituximab, IDEC-C2B8)
    • Winkler, U., Jensen, M., Manzke, O., Schulz, H., Diehl, V. Engert, A. (1999) Cytokine-release syndrome in patients with B-cell chronic lymphocytic leukaemia and high lymphocyte counts after treatment with an anti-CD20 monoclonal antibody (rituximab, IDEC-C2B8). Blood, 94, 2217 2224.
    • (1999) Blood , vol.94 , pp. 2217-2224
    • Winkler, U.1    Jensen, M.2    Manzke, O.3    Schulz, H.4    Diehl, V.5    Engert, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.