메뉴 건너뛰기




Volumn 269, Issue 24, 2002, Pages 6042-6051

ER-resident chaperone interactions with recombinant antibodies in transgenic plants

Author keywords

BiP; Chaperones; IgG; Immunoglobulin assembly; Transgenic plants

Indexed keywords

BINDING PROTEIN; CALRETICULIN; CHAPERONE; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; MESSENGER RNA; RECOMBINANT ANTIBODY;

EID: 18744378812     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03302.x     Document Type: Article
Times cited : (75)

References (54)
  • 1
    • 0026245101 scopus 로고
    • 'Phytoantibodies': A general vector for the expression of immunoglobulin domains in transgenic plants
    • Benvenuto, E., Ordas, R.J., Tavazza, R., Ancora, G., Biocca, S., Cattaneo, A. & Galeffi, P. (1991) 'Phytoantibodies': A general vector for the expression of immunoglobulin domains in transgenic plants. Plant Mol. Biol. 17, 865-874.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 865-874
    • Benvenuto, E.1    Ordas, R.J.2    Tavazza, R.3    Ancora, G.4    Biocca, S.5    Cattaneo, A.6    Galeffi, P.7
  • 3
    • 14744306329 scopus 로고
    • Synthesis of a functional anti-phytochrome single-chain Fv protein in transgenic tobacco
    • Owen, M., Gandecha, A., Cockburn, B. & Whitelam, G. (1992) Synthesis of a functional anti-phytochrome single-chain Fv protein in transgenic tobacco. Biotechnology (NY) 10, 790-794.
    • (1992) Biotechnology (NY) , vol.10 , pp. 790-794
    • Owen, M.1    Gandecha, A.2    Cockburn, B.3    Whitelam, G.4
  • 4
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt, A., Cafferkey, R. & Bowdish, K. (1989) Production of antibodies in transgenic plants. Nature 342, 76-78.
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Cafferkey, R.2    Bowdish, K.3
  • 5
    • 0028031827 scopus 로고
    • Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants
    • Ma, J.K.-C., Lehner, T., Stabila, P., Fux, C.I. & Hiatt, A. (1994) Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants. Eur. J. Immunol. 24, 131-138.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 131-138
    • Ma, J.K.-C.1    Lehner, T.2    Stabila, P.3    Fux, C.I.4    Hiatt, A.5
  • 8
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard, L., Molinari, M. & Helenius, A. (1999) Setting the standards: Quality control in the secretory pathway. Science 286, 1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 9
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • Haas, I.G. & Wabl, M. (1983) Immunoglobulin heavy chain binding protein. Nature 306, 387-389.
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 10
    • 0024121547 scopus 로고
    • cDNA cloning of the immunoglobulin heavy chain binding protein
    • Haas, I.G. & Meo, T. (1988) cDNA cloning of the immunoglobulin heavy chain binding protein. Proc. Natl. Acad. Sci. USA 85, 2250-2254.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2250-2254
    • Haas, I.G.1    Meo, T.2
  • 11
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S. & Pelham, H.R.B. (1986) An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46, 291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 12
    • 0023253949 scopus 로고
    • The nucleotide sequence encoding the hamster 78-kDa glucose-regulated protein (GRP78) and its conservation between hamster and rat
    • Ting, J., Wooden, S.K., Kriz, R., Kelleher, K., Kaufman, R.J. & Lee, A.S. (1987) The nucleotide sequence encoding the hamster 78-kDa glucose-regulated protein (GRP78) and its conservation between hamster and rat. Gene 55, 147-152.
    • (1987) Gene , vol.55 , pp. 147-152
    • Ting, J.1    Wooden, S.K.2    Kriz, R.3    Kelleher, K.4    Kaufman, R.J.5    Lee, A.S.6
  • 13
    • 0023809215 scopus 로고
    • The organization of the rat GRP78 gene and A23187-induced expression of fusion gene products targeted intracellularly
    • Wooden, S.K., Kapur, R.P. & Lee, A.S. (1988) The organization of the rat GRP78 gene and A23187-induced expression of fusion gene products targeted intracellularly. Exp. Cell Res. 178, 84-92.
    • (1988) Exp. Cell Res. , vol.178 , pp. 84-92
    • Wooden, S.K.1    Kapur, R.P.2    Lee, A.S.3
  • 14
    • 0024395160 scopus 로고
    • S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington, K., Kohno, K., Kozutsumi, Y., Gething, M.-J. & Sambrook, J. (1989) S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57, 1223-1236.
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.-J.4    Sambrook, J.5
  • 15
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
    • Rose, M.D., Misra, L.M. & Vogel, J.P. (1989) KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 17
  • 18
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething, M.-J. (1999) Role and regulation of the ER chaperone BiP. Sem. Cell Dev. Biol. 10, 465-472.
    • (1999) Sem. Cell Dev. Biol. , vol.10 , pp. 465-472
    • Gething, M.-J.1
  • 19
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • Nishikawa, S., Fewell, S.W., Kato, Y., Brodsky, J.L. & Endo, T. (2001) Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J. Cell Biol. 153, 1061-1069.
    • (2001) J. Cell Biol. , vol.153 , pp. 1061-1069
    • Nishikawa, S.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 20
    • 0029167492 scopus 로고
    • The binding protein associates with monomeric phaseolin
    • Vitale, A., Bielli, A. & Ceriotti, A. (1995) The binding protein associates with monomeric phaseolin. Plant Physiol. 107, 1411-1418.
    • (1995) Plant Physiol. , vol.107 , pp. 1411-1418
    • Vitale, A.1    Bielli, A.2    Ceriotti, A.3
  • 25
    • 0031774263 scopus 로고    scopus 로고
    • BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress
    • Crofts, A.J., Leborgne-Castel, N., Pesca, M., Vitale, A. & Denecke, J. (1998) BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress. Plant Cell 10, 813-823.
    • (1998) Plant Cell , vol.10 , pp. 813-823
    • Crofts, A.J.1    Leborgne-Castel, N.2    Pesca, M.3    Vitale, A.4    Denecke, J.5
  • 27
    • 0031680678 scopus 로고    scopus 로고
    • Calreticulin and calnexin in plants
    • Crofts, A.J. & Denecke, J. (1998) Calreticulin and calnexin in plants. Trends Plant Sci. 3, 396-399.
    • (1998) Trends Plant Sci. , vol.3 , pp. 396-399
    • Crofts, A.J.1    Denecke, J.2
  • 28
    • 0026511275 scopus 로고
    • Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly
    • Hochstenbach, F., David, V., Watkins, S. & Brenner, M.B. (1992) Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc. Natl. Acad. Sci. USA 89, 4734-4738.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4734-4738
    • Hochstenbach, F.1    David, V.2    Watkins, S.3    Brenner, M.B.4
  • 29
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • Sadasivan, B., Lehner, P.J., Ortmann, B., Spies, T. & Cresswell, P. (1996) Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5, 103-114.
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 30
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • Otteken, A. & Moss, B. (1996) Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem. 271, 97-103.
    • (1996) J. Biol. Chem. , vol.271 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 31
    • 0026569212 scopus 로고
    • Interaction of BiP with newly synthesized immunoglobulin light chain molecules: Cycles of sequential binding and release
    • Knittler, M.R. & Haas, I.G. (1992) Interaction of BiP with newly synthesized immunoglobulin light chain molecules: Cycles of sequential binding and release. EMBO J. 11, 1573-1581.
    • (1992) EMBO J. , vol.11 , pp. 1573-1581
    • Knittler, M.R.1    Haas, I.G.2
  • 32
    • 0034896499 scopus 로고    scopus 로고
    • Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release
    • Vanhove, M., Usherwood, Y.K. & Hendershot, L.M. (2001) Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release. Immunity 15, 105-114.
    • (2001) Immunity , vol.15 , pp. 105-114
    • Vanhove, M.1    Usherwood, Y.K.2    Hendershot, L.M.3
  • 33
    • 0028923597 scopus 로고
    • Molecular chaperones and the biosynthesis of antigen receptors
    • Melnick, J. & Argon, Y. (1995) Molecular chaperones and the biosynthesis of antigen receptors. Immunol. Today 16, 243-250.
    • (1995) Immunol. Today , vol.16 , pp. 243-250
    • Melnick, J.1    Argon, Y.2
  • 34
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., Dul, J.L. & Argon, Y. (1994) Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370, 373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 35
    • 0023653141 scopus 로고
    • In vivo cross-linking of protein disulfide isomerase to immunoglobulins
    • Roth, R.A. & Pierce, S.B. (1987) In vivo cross-linking of protein disulfide isomerase to immunoglobulins. Biochemistry 26, 4179-4182.
    • (1987) Biochemistry , vol.26 , pp. 4179-4182
    • Roth, R.A.1    Pierce, S.B.2
  • 37
    • 0023654956 scopus 로고
    • Improved method for the isolation of RNA from plant tissues
    • Logemann, J., Schell, J. & Willmitzer, L. (1987) Improved method for the isolation of RNA from plant tissues. Anal. Biochem. 163, 16-20.
    • (1987) Anal. Biochem. , vol.163 , pp. 16-20
    • Logemann, J.1    Schell, J.2    Willmitzer, L.3
  • 38
    • 0031214672 scopus 로고    scopus 로고
    • Cloning and characterization of the calreticulin gene from Ricinus communis L.
    • Coughlan, S.J., Hastings, C. & Winfrey, R.J. (1997) Cloning and characterization of the calreticulin gene from Ricinus communis L. Plant Mol. Biol. 34, 897-911.
    • (1997) Plant Mol. Biol. , vol.34 , pp. 897-911
    • Coughlan, S.J.1    Hastings, C.2    Winfrey, R.J.3
  • 39
    • 0015373107 scopus 로고
    • Ultrastructure of infection of tobacco mesophyll protoplasts by tobacco mosaic virus
    • Otsuki, Y., Takebe, I., Honda, Y. & Matsui, C. (1972) Ultrastructure of infection of tobacco mesophyll protoplasts by tobacco mosaic virus. Virology 49, 188-194.
    • (1972) Virology , vol.49 , pp. 188-194
    • Otsuki, Y.1    Takebe, I.2    Honda, Y.3    Matsui, C.4
  • 40
    • 0034699356 scopus 로고    scopus 로고
    • Glycoprotein degradation: Do sugars hold the key?
    • Frigerio, L. & Lord, J.M. (2000) Glycoprotein degradation: Do sugars hold the key? Curr. Biol. 10, R674-R677.
    • (2000) Curr. Biol. , vol.10
    • Frigerio, L.1    Lord, J.M.2
  • 42
    • 0025340630 scopus 로고
    • High-level production of a functional immunoglobulin heterodimer in a baculovirus expression system
    • Hasemann, C.A. & Capra, J.D. (1990) High-level production of a functional immunoglobulin heterodimer in a baculovirus expression system. Proc. Natl. Acad. Sci. USA 87, 3942-3946.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3942-3946
    • Hasemann, C.A.1    Capra, J.D.2
  • 44
    • 0025977749 scopus 로고
    • BiP - A heat shock protein involved in immunoglobulin chain assembly
    • Haas, I.G. (1991) BiP - A heat shock protein involved in immunoglobulin chain assembly. Curr. Top Microbiol. Immunol. 167, 71-82.
    • (1991) Curr. Top Microbiol. Immunol. , vol.167 , pp. 71-82
    • Haas, I.G.1
  • 46
    • 0025339295 scopus 로고
    • Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
    • Vogel, J.P., Misra, L.M. & Rose, M.D. (1990) Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110, 1885-1895.
    • (1990) J. Cell Biol. , vol.110 , pp. 1885-1895
    • Vogel, J.P.1    Misra, L.M.2    Rose, M.D.3
  • 47
    • 0025305021 scopus 로고
    • Role of glycosylation in the transport of recombinant glycoproteins through the secretory pathway of lepidopteran insect cells
    • Jarvis, D.L., Oker-Blom, C. & Summers, M.D. (1990) Role of glycosylation in the transport of recombinant glycoproteins through the secretory pathway of lepidopteran insect cells. J. Cell Biochem. 42, 181-191.
    • (1990) J. Cell Biochem. , vol.42 , pp. 181-191
    • Jarvis, D.L.1    Oker-Blom, C.2    Summers, M.D.3
  • 48
    • 0028675536 scopus 로고
    • Effects of co-expressing chaperone BiP on functional antibody production in the baculovirus system
    • Hsu, T.A., Eiden, J.J., Bourgarel, P., Meo, T. & Betenbaugh, M.J. (1994) Effects of co-expressing chaperone BiP on functional antibody production in the baculovirus system. Protein Expr. Purif. 5, 595-603.
    • (1994) Protein Expr. Purif. , vol.5 , pp. 595-603
    • Hsu, T.A.1    Eiden, J.J.2    Bourgarel, P.3    Meo, T.4    Betenbaugh, M.J.5
  • 49
    • 0028928021 scopus 로고    scopus 로고
    • Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
    • Knittler, M.R., Dirks, S. & Haas, I.G. (1996) Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92, 1764-1768.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1764-1768
    • Knittler, M.R.1    Dirks, S.2    Haas, I.G.3
  • 50
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta, E.V., Raines, R.T., Plückthun, A. & Wittrup, K.D. (1998) Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nat. Biotechnol. 16, 773-777.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Plückthun, A.3    Wittrup, K.D.4
  • 52
    • 0035146430 scopus 로고    scopus 로고
    • The endomembrane system and the problem of protein sorting
    • Vitale, A. & Galili, G. (2001) The endomembrane system and the problem of protein sorting. Plant Physiol. 125, 115-118.
    • (2001) Plant Physiol. , vol.125 , pp. 115-118
    • Vitale, A.1    Galili, G.2
  • 53
    • 0025840492 scopus 로고
    • Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C
    • Shorrosh, B.S. & Dixon, R.A. (1991) Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C. Proc. Natl. Acad. Sci. USA 88, 10941-10945.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10941-10945
    • Shorrosh, B.S.1    Dixon, R.A.2
  • 54
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • Molinari, M. & Helenius, A. (2000) Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 288, 331-333.
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.