메뉴 건너뛰기




Volumn 13, Issue 1, 1997, Pages 96-104

Coexpression of molecular chaperone BiP improves immunoglobulin solubility and IgG secretion from trichoplusia ni insect cells

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN; IMMUNOGLOBULIN G; MOLECULAR CHAPERONE GRP78; TUNICAMYCIN;

EID: 0031055289     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp960088d     Document Type: Article
Times cited : (69)

References (39)
  • 1
    • 0021797741 scopus 로고
    • Mott Cells are Plasma Cells Defective in Immunoglobulin Secretion
    • Alanen, A.; Pira, U.; Lassilla, O., Roth, J.; Franklin, R. M. Mott Cells Are Plasma Cells Defective in Immunoglobulin Secretion. Eur. J. Immunol. 1985, 15, 235-242.
    • (1985) Eur. J. Immunol. , vol.15 , pp. 235-242
    • Alanen, A.1    Pira, U.2    Lassilla, O.3    Roth, J.4    Franklin, R.M.5
  • 3
    • 0022536233 scopus 로고
    • Post-translational Association of Immunoglobulin Heavy Chain Binding Protein with Nascent Heavy Chains in Nonsecreting and Secreting Hybridomas
    • Bole, D. G.; L. M. Hendershot.; J. F. Kearney. Post-translational Association of Immunoglobulin Heavy Chain Binding Protein with Nascent Heavy Chains in Nonsecreting and Secreting Hybridomas. J. Cell Biol. 1986, 102, 1558-1566.
    • (1986) J. Cell Biol. , vol.102 , pp. 1558-1566
    • Bole, D.G.1    Hendershot, L.M.2    Kearney, J.F.3
  • 5
    • 0023708177 scopus 로고
    • Reduction of Endogenous GRP78 Levels Improves Secretion of a Heterologous Protein in CHO cells
    • Dorner, A. J.; Krane, M. G.; Kaufman, R. J. Reduction of Endogenous GRP78 Levels Improves Secretion of a Heterologous Protein in CHO cells. Mol. Cell. Biol. 1988, 8, 4063-4070.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4063-4070
    • Dorner, A.J.1    Krane, M.G.2    Kaufman, R.J.3
  • 6
    • 0026511824 scopus 로고
    • Overexpression of GRP78 Mitigates Stress Induction of Glucose Regulated Protein and Blocks Secretion of Selective Proteins in Chinese Hamster Ovary Cells
    • Dorner, A. J.; Wasley, L. C.; Kaufman, R. J. Overexpression of GRP78 Mitigates Stress Induction of Glucose Regulated Protein and Blocks Secretion of Selective Proteins in Chinese Hamster Ovary Cells. EMBO J. 1992, 11, 1563-1572.
    • (1992) EMBO J. , vol.11 , pp. 1563-1572
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 7
    • 0026440051 scopus 로고
    • Heat-Induced Aggregation of Recombinant Erythropoietin in the Intact and Deglycosylated States as Monitored by Gel Permeation Chromatography Combined with a Low-Angle Laser light Scattering Technique
    • Endo, Y.; Nagai, H.; Watanabe, Y.; Ochi, K.; Takagi, T. Heat-Induced Aggregation of Recombinant Erythropoietin in the Intact and Deglycosylated States as Monitored by Gel Permeation Chromatography Combined with a Low-Angle Laser light Scattering Technique. J. Biochem. 1992, 112, 700-706.
    • (1992) J. Biochem. , vol.112 , pp. 700-706
    • Endo, Y.1    Nagai, H.2    Watanabe, Y.3    Ochi, K.4    Takagi, T.5
  • 8
    • 0026059137 scopus 로고
    • Peptide-Binding Specificity of the Molecular Chaperone BiP
    • Flynn, G. C.; Pohl, J.; Flocco, M. T.; Rothman, J. E. Peptide-Binding Specificity of the Molecular Chaperone BiP. Nature 1991, 353, 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 9
    • 0026584271 scopus 로고
    • Protein Folding in the Cell
    • Gething, M. J.; Sambrook, J. Protein Folding in the Cell. Nature 1992, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 11
    • 0021076098 scopus 로고
    • Immunoglobulin Heavy Chain Binding Protein
    • Haas, I. G.; Wabl, M. Immunoglobulin Heavy Chain Binding Protein. Nature 1983, 306, 387-389.
    • (1983) Nature , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 12
    • 0025340630 scopus 로고
    • High-level Production of a Functional Immunoglobulin Heterodimer in a Baculovirus Expression System
    • Haseman, C. A.; Capra, J. D. High-level Production of a Functional Immunoglobulin Heterodimer in a Baculovirus Expression System. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 3942-3946.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3942-3946
    • Haseman, C.A.1    Capra, J.D.2
  • 13
    • 0025007007 scopus 로고
    • Immunoglobulin Heavy Chain and Binding Protein Complexes are Dissociated in Vitro by Light Chain Addition
    • Hendershot, L. M. Immunoglobulin Heavy Chain and Binding Protein Complexes Are Dissociated in Vitro by Light Chain Addition. J. Cell Biol. 1990, 111, 829-837.
    • (1990) J. Cell Biol. , vol.111 , pp. 829-837
    • Hendershot, L.M.1
  • 14
    • 0023096246 scopus 로고
    • Assembly and Secretion of Heavy Chains That Do Not Associate Post-Translationally with Immunoglobulin Heavy Chain Binding Protein
    • Hendershot, L.; Bole, D. G.; Kohler, G.; Kearney, J. F. Assembly and Secretion of Heavy Chains That Do Not Associate Post-Translationally with Immunoglobulin Heavy Chain Binding Protein. J. Cell Biol. 1987, 104, 761-767.
    • (1987) J. Cell Biol. , vol.104 , pp. 761-767
    • Hendershot, L.1    Bole, D.G.2    Kohler, G.3    Kearney, J.F.4
  • 15
    • 0027184721 scopus 로고
    • Molecular Chaperone Functions of Heat-Shock Proteins
    • Hendrick, J. P.; Hartl, F. U. Molecular Chaperone Functions of Heat-Shock Proteins. Annu. Rev. Biochem. 1993, 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 16
    • 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. Effects of Co-Expressing Chaperone BiP on Functional Antibody Production in the Baculovirus System. Protein. Expression Purif. 1994, 5, 595-603.
    • (1994) Protein. Expression Purif. , vol.5 , pp. 595-603
    • Hsu, T.-A.1    Eiden, J.J.2    Bourgarel, P.3    Meo, T.4    Betenbaugh, M.J.5
  • 17
    • 0030151987 scopus 로고    scopus 로고
    • Rescue of Immunoglobulins from Insolubility is Facilitated by PDI in the Baculovirus Expression System
    • Hsu, T.-A.; Watson, S.; Eiden, J. J.; Betenbaugh, M. J. Rescue of Immunoglobulins from Insolubility is Facilitated by PDI in the Baculovirus Expression System. Protein Expression Purif. 1996, 7, 281-288.
    • (1996) Protein Expression Purif. , vol.7 , pp. 281-288
    • Hsu, T.-A.1    Watson, S.2    Eiden, J.J.3    Betenbaugh, M.J.4
  • 18
    • 0024574726 scopus 로고
    • Glycosylation and Secretion of Human Tissue Plasminogen Activator in Recombinant Baculovirus-Infected Insect Cells
    • Jarvis, D. L.; Summers, M. D. Glycosylation and Secretion of Human Tissue Plasminogen Activator in Recombinant Baculovirus-Infected Insect Cells. Mol. Cell. Biol. 1989, 9, 214-223.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 214-223
    • Jarvis, D.L.1    Summers, M.D.2
  • 20
    • 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. Interaction of BiP with Newly Synthesized Immunoglobulin Light Chain Molecules - Cycles of Sequential Binding and Release. EMBO J. 1992, 11, 1573-1581.
    • (1992) EMBO J. , vol.11 , pp. 1573-1581
    • Knittler, M.R.1    Haas, I.G.2
  • 21
    • 0023133224 scopus 로고
    • Coordinated Regulation of a Set of Genes by Glucose and Calcium Ionophores in Mammalian Cells
    • Lee, A. S. Coordinated Regulation of a Set of Genes by Glucose and Calcium Ionophores in Mammalian Cells. Trends Biol. Sci. 1987, 12, 20-23.
    • (1987) Trends Biol. Sci. , vol.12 , pp. 20-23
    • Lee, A.S.1
  • 22
    • 0026843954 scopus 로고
    • Mammalian Stress Response: Induction of the Glucose-Regulated Protein Family
    • Lee, A. S. Mammalian Stress Response: Induction of the Glucose-Regulated Protein Family. Curr. Opin. Cell Biol. 1992, 4, 267-73.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 267-273
    • Lee, A.S.1
  • 23
    • 0027216162 scopus 로고
    • Baculovirus Expression of Gene 6 of the IDIR Strain of Group B rotavirus (GBR): Coding Assignment of the Major Inner Capsid Protein
    • Lindsay, D. A.; Vonderfecht, S. L.; Betenbaugh, M. J.; Eiden, J. J. Baculovirus Expression of Gene 6 of the IDIR Strain of Group B rotavirus (GBR): Coding Assignment of the Major Inner Capsid Protein. Virology 1993, 193, 367-375.
    • (1993) Virology , vol.193 , pp. 367-375
    • Lindsay, D.A.1    Vonderfecht, S.L.2    Betenbaugh, M.J.3    Eiden, J.J.4
  • 24
    • 0028927489 scopus 로고
    • Generation of a Mammalian-Cell Line Deficient in Glucose Regulated Protein Stress Inducible Promoter
    • Little, E.; Lee A. S. Generation of a Mammalian-Cell Line Deficient in Glucose Regulated Protein Stress Inducible Promoter. J. Biol. Chem. 1995, 270, 9526-9534.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9526-9534
    • Little, E.1    Lee, A.S.2
  • 25
    • 0021280849 scopus 로고
    • Glucose Removal from N-linked Oligosaccharides is Required for Efficient Maturation of Certain Secretory Glycoproteins from the Rough Endoplasmic Reticulum to the Golgi Complex
    • Lodish, H. F.; Kong, N. Glucose Removal from N-linked Oligosaccharides Is Required for Efficient Maturation of Certain Secretory Glycoproteins from the Rough Endoplasmic Reticulum to the Golgi Complex. J. Cell Biol. 1984, 98, 1720-1729.
    • (1984) J. Cell Biol. , vol.98 , pp. 1720-1729
    • Lodish, H.F.1    Kong, N.2
  • 26
    • 0002554146 scopus 로고
    • Shuler, M. L., Wood, H. A., Granados, R. R., Hammer, D. A., Eds.; John Wiley & Sons, Inc.: New York
    • Luckow, V. A. In Baculovirus Expression Systems and Biopesticides. Shuler, M. L., Wood, H. A., Granados, R. R., Hammer, D. A., Eds.; John Wiley & Sons, Inc.: New York, 1995; pp 51-90.
    • (1995) Baculovirus Expression Systems and Biopesticides , pp. 51-90
    • Luckow, V.A.1
  • 27
    • 0013919647 scopus 로고
    • Cytoplasmic and Intra-Nuclear Electron-Dense Bodies in the Myeloma Cells
    • Maldonado, J. E.; Brown, J. A. L.; Boyd, E. D.; Pearse. G. L. Cytoplasmic and Intra-Nuclear Electron-Dense Bodies in the Myeloma Cells. Arch. Pathol. 1966, 81, 484-500.
    • (1966) Arch. Pathol. , vol.81 , pp. 484-500
    • Maldonado, J.E.1    Brown, J.A.L.2    Boyd, E.D.3    Pearse, G.L.4
  • 28
    • 0022969885 scopus 로고
    • Speculations on the Functions of the Major Heat Shock and Glucose Regulated Proteins
    • Pelham, H. R. B. Speculations on the Functions of the Major Heat Shock and Glucose Regulated Proteins. Cell 1986, 46, 959-961.
    • (1986) Cell , vol.46 , pp. 959-961
    • Pelham, H.R.B.1
  • 29
    • 0024427039 scopus 로고
    • Control of Protein Exit from the Endoplasmic Reticulum
    • Pelham, H. R. B. Control of Protein Exit from the Endoplasmic Reticulum. Annu. Rev. Cell Biol. 1989, 5, 1-23
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 1-23
    • Pelham, H.R.B.1
  • 30
    • 0029257263 scopus 로고
    • Constitutive Overexpression of Secreted Heterologous Proteins Decreases Extractable BiP and Protein Disulfide Isomerase Levels in Saccharomyces cerevisiae
    • Robinson, A. S.; Wittrup, K. D. Constitutive Overexpression of Secreted Heterologous Proteins Decreases Extractable BiP and Protein Disulfide Isomerase Levels in Saccharomyces cerevisiae. Biotechnol. Prog. 1995, 11, 171-177.
    • (1995) Biotechnol. Prog. , vol.11 , pp. 171-177
    • Robinson, A.S.1    Wittrup, K.D.2
  • 31
    • 0029944822 scopus 로고    scopus 로고
    • Reduction of BiP Levels Decreases Heterologous Protein Secretion in Saccharomyces cerevisiae
    • Robinson, A. S.; Bockhaus, J. A.; Voegler, A. C.; Wittrup, K. D. Reduction of BiP Levels Decreases Heterologous Protein Secretion in Saccharomyces cerevisiae. J. Biol. Chem. 1996, 271, 10017-10022.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10017-10022
    • Robinson, A.S.1    Bockhaus, J.A.2    Voegler, A.C.3    Wittrup, K.D.4
  • 32
    • 0027176067 scopus 로고
    • Genomic Structure and Sequence Analysis of Drosophila Melanogaster HSC70 Genes
    • Rubin, D. M.; Mehta, A. D.; Zhu, J.; Shoham, S.; Chen, X.; Wells, Q. R.; Palter, K. B. Genomic Structure and Sequence Analysis of Drosophila Melanogaster HSC70 Genes. Gene 1993, 128, 155-163.
    • (1993) Gene , vol.128 , pp. 155-163
    • Rubin, D.M.1    Mehta, A.D.2    Zhu, J.3    Shoham, S.4    Chen, X.5    Wells, Q.R.6    Palter, K.B.7
  • 33
    • 0001720417 scopus 로고
    • Address on a Characteristic Organism of Cancer
    • Russel, W. Address on a Characteristic Organism of Cancer. Brit. Med. J. 1890, 2, 1356-1360.
    • (1890) Brit. Med. J. , vol.2 , pp. 1356-1360
    • Russel, W.1
  • 34
    • 0029042422 scopus 로고
    • BiP/Kar2p Serves as a Molecular Chaperone during Carboxypeptidase Y Folding in Yeast
    • Simons, J. F.; Novick, S. F.; Rose, M. D.; Helenius, A. BiP/Kar2p Serves as a Molecular Chaperone during Carboxypeptidase Y Folding in Yeast. J. Cell. Biol. 1995, 130, 41-49.
    • (1995) J. Cell. Biol. , vol.130 , pp. 41-49
    • Simons, J.F.1    Novick, S.F.2    Rose, M.D.3    Helenius, A.4
  • 35
    • 0026571278 scopus 로고
    • The Human Class II MHC Protein HLA_DR1 Assembles as Empty αβ Heterodimers in the Absence of Antigenic Peptide
    • Stern, L. J.; Wiley, D. C. The Human Class II MHC Protein HLA_DR1 Assembles as Empty αβ Heterodimers in the Absence of Antigenic Peptide. Cell 1992, 68, 465-477.
    • (1992) Cell , vol.68 , pp. 465-477
    • Stern, L.J.1    Wiley, D.C.2
  • 37
    • 0026347810 scopus 로고
    • Russell Bodies: A General Response of Secretory Cells to Synthesis of a Mutant Immunoglobulin which can Neither Exit from, nor Be Degraded in, the Endoplasmic Reticulum
    • Valetti, C.; Grossi, C. E.; Milstein, C.; Sitia, R. Russell Bodies: A General Response of Secretory Cells to Synthesis of a Mutant Immunoglobulin which can Neither Exit from, nor Be Degraded in, the Endoplasmic Reticulum. J. Cell Biol. 1991, 115, 983-994.
    • (1991) J. Cell Biol. , vol.115 , pp. 983-994
    • Valetti, C.1    Grossi, C.E.2    Milstein, C.3    Sitia, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.