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Volumn 170, Issue 4, 2003, Pages 1903-1909

Restoration of ig secretion: Mutation of germline-encoded residues in T15L chains leads to secretion of free light chains and assembled antibody complexes bearing secretion-impaired heavy chains

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN KAPPA CHAIN; IMMUNOGLOBULIN LIGHT CHAIN;

EID: 0037442011     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.170.4.1903     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0026782875 scopus 로고
    • Generation and analysis of random point mutations in an antibody CDR2 sequence: Many mutated antibodies lose their ability to bind antigen
    • Chen, C., V. A. Roberts, and M. B. Rittenberg. 1992. Generation and analysis of random point mutations in an antibody CDR2 sequence: many mutated antibodies lose their ability to bind antigen. J. Exp. Med. 176:855.
    • (1992) J. Exp. Med. , vol.176 , pp. 855
    • Chen, C.1    Roberts, V.A.2    Rittenberg, M.B.3
  • 2
    • 0031204378 scopus 로고    scopus 로고
    • H complementarity-determining region 2 and framework region 2: Differential effects of antigen binding and Ig secretion
    • H complementarity-determining region 2 and framework region 2: differential effects of antigen binding and Ig secretion. J. Immunol. 159:1293.
    • (1997) J. Immunol. , vol.159 , pp. 1293
    • Wiens, G.D.1    Heldwein, K.A.2    Stenzel-Poore, M.P.3    Rittenberg, M.B.4
  • 3
    • 0028111743 scopus 로고
    • Sequence statistics reliably predict stabilizing mutations in a protein domain
    • Steipe, B., B. Schiller, A. Pluckthun, and S. Steinbacher. 1994. Sequence statistics reliably predict stabilizing mutations in a protein domain. J. Mol. Biol. 240:188.
    • (1994) J. Mol. Biol , vol.240 , pp. 188
    • Steipe, B.1    Schiller, B.2    Pluckthun, A.3    Steinbacher, S.4
  • 5
    • 0018182699 scopus 로고
    • A better cell line for making hybridomas secreting specific antibodies
    • Shulman, M., C. D. Wilde, and G. Kohler. 1978. A better cell line for making hybridomas secreting specific antibodies. Nature 276:269.
    • (1978) Nature , vol.276 , pp. 269
    • Shulman, M.1    Wilde, C.D.2    Kohler, G.3
  • 6
    • 0033168160 scopus 로고    scopus 로고
    • Proteasome involvement in the degradation of unassembled immunoglobulin light chains
    • O'Hare, T., G. D. Wiens, E. A. Whitcomb, C. A. Enns, and M. B. Rittenberg. 1999. Proteasome involvement in the degradation of unassembled immunoglobulin light chains. J. Immunol. 163:11.
    • (1999) J. Immunol. , vol.163 , pp. 11
    • O'Hare, T.1    Wiens, G.D.2    Whitcomb, E.A.3    Enns, C.A.4    Rittenberg, M.B.5
  • 7
    • 0028357638 scopus 로고
    • Defective secretion of an immunoglobulin caused by mutations in the heavy chain complementarity determining region 2
    • Chen, C., T. M. Martin, S. Stevens, and M. B. Rittenberg. 1994. Defective secretion of an immunoglobulin caused by mutations in the heavy chain complementarity determining region 2. J. Exp. Med. 180:577.
    • (1994) J. Exp. Med. , vol.180 , pp. 577
    • Chen, C.1    Martin, T.M.2    Stevens, S.3    Rittenberg, M.B.4
  • 9
    • 0030009781 scopus 로고    scopus 로고
    • H regions: A means of minimizing B cell wastage from somatic hypermutation?
    • H regions: a means of minimizing B cell wastage from somatic hypermutation? J. Immunol. 156:3285.
    • (1996) J. Immunol. , vol.156 , pp. 3285
    • Brown, M.1    Rittenberg, M.B.2    Roberts, V.A.3
  • 11
    • 0020641571 scopus 로고
    • Secretion of a λ2 immunoglobulin chain is prevented by a single amino acid substitution in its variable region
    • Wu, G. E., N. Hozumi, and H. Murialdo. 1983. Secretion of a λ2 immunoglobulin chain is prevented by a single amino acid substitution in its variable region. Cell 33:77.
    • (1983) Cell , vol.33 , pp. 77
    • Wu, G.E.1    Hozumi, N.2    Murialdo, H.3
  • 12
    • 0025134871 scopus 로고
    • A single amino acid substitution in the variable region of the light chain specifically blocks immunoglobulin secretion
    • Dul, J. L., and Y. Argon. 1990. A single amino acid substitution in the variable region of the light chain specifically blocks immunoglobulin secretion. Proc. Natl. Acad. Sci. USA 87:8135.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8135
    • Dul, J.L.1    Argon, Y.2
  • 13
    • 0026768470 scopus 로고
    • A conditional secretory mutant in an Ig L chain is caused by replacement of a tyrosine/phenylalanine 87 with histidine
    • Dul, J. L., O. R. Burrone, and Y. Argon. 1992. A conditional secretory mutant in an Ig L chain is caused by replacement of a tyrosine/phenylalanine 87 with histidine. J. Immunol. 149:1927.
    • (1992) J. Immunol. , vol.149 , pp. 1927
    • Dul, J.L.1    Burrone, O.R.2    Argon, Y.3
  • 14
    • 0028168756 scopus 로고
    • Chimeric immunoglobulin light chains are secreted at different levels: Influence of framework-1 amino acids
    • Horwitz, A. H., R. Nadell, F. Preugschat, and M. Better. 1994. Chimeric immunoglobulin light chains are secreted at different levels: influence of framework-1 amino acids. Mol. Immunol. 31:683.
    • (1994) Mol. Immunol. , vol.31 , pp. 683
    • Horwitz, A.H.1    Nadell, R.2    Preugschat, F.3    Better, M.4
  • 16
    • 0026569212 scopus 로고
    • Interaction of BiP with newly synthesized immunoglobulin light chain molecules: Cycles of sequential binding and release
    • Knittler, M. R., and I. G. Haas. 1992. Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release. EMBO J. 11:1573.
    • (1992) EMBO J. , vol.11 , pp. 1573
    • Knittler, M.R.1    Haas, I.G.2
  • 17
    • 0033215279 scopus 로고    scopus 로고
    • Pathogenic light chains and the B-cell repertoire
    • Stevens, F. J., and Y. Argon. 1999. Pathogenic light chains and the B-cell repertoire. Immunol. Today 20:451.
    • (1999) Immunol. Today , vol.20 , pp. 451
    • Stevens, F.J.1    Argon, Y.2
  • 18
    • 0032080047 scopus 로고    scopus 로고
    • Structural determinants in the sequences of immunoglobulin variable domain
    • Chothia, C., I. Gelfand, and A. Kister. 1998. Structural determinants in the sequences of immunoglobulin variable domain. J. Mol. Biol. 278:457.
    • (1998) J. Mol. Biol. , vol.278 , pp. 457
    • Chothia, C.1    Gelfand, I.2    Kister, A.3
  • 20
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle, M. R., L. R. Helms, L. Li, and R. Wetzel. 1994. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc. Natl. Acad. Sci. USA 91:5446.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5446
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Wetzel, R.4
  • 21
  • 23
    • 0344549167 scopus 로고    scopus 로고
    • The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli
    • Wall, J. G., and A. Pluckthun. 1999. The hierarchy of mutations influencing the folding of antibody domains in Escherichia coli. Protein Eng. 12:605.
    • (1999) Protein Eng. , vol.12 , pp. 605
    • Wall, J.G.1    Pluckthun, A.2
  • 24
    • 0033178126 scopus 로고    scopus 로고
    • A single backmutation in the human kIV framework of a previously unsuccessfully humanized antibody restores the binding activity and increases the secretion in COS cells
    • Saldanha, J. W., A. C. R. Martin, and O. J. P. Leger. 1999. A single backmutation in the human kIV framework of a previously unsuccessfully humanized antibody restores the binding activity and increases the secretion in COS cells. Mol. Immunol. 36:709.
    • (1999) Mol. Immunol. , vol.36 , pp. 709
    • Saldanha, J.W.1    Martin, A.C.R.2    Leger, O.J.P.3
  • 25
    • 0016215235 scopus 로고
    • Equilibrium and kinetic aspects of subunit association in immunoglobulin G
    • Bigelow, C. C., B. R. Smith, and K. J. Dorrington. 1974. Equilibrium and kinetic aspects of subunit association in immunoglobulin G. Biochemistry 13:4602.
    • (1974) Biochemistry , vol.13 , pp. 4602
    • Bigelow, C.C.1    Smith, B.R.2    Dorrington, K.J.3
  • 26
    • 0019196543 scopus 로고
    • Non-covalent association of heavy and light chains of human immunoglobulin G: Studies using light chain labelled with a fluorescent probe
    • Alexandru, I., D. I. C. Kells, K. J. Dorrington, and M. Klein. 1980. Non-covalent association of heavy and light chains of human immunoglobulin G: studies using light chain labelled with a fluorescent probe. Mol. Immunol. 17:1351.
    • (1980) Mol. Immunol. , vol.17 , pp. 1351
    • Alexandru, I.1    Kells, D.I.C.2    Dorrington, K.J.3    Klein, M.4
  • 27
    • 0029022591 scopus 로고
    • Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG
    • Kaloff, C. R., and I. G. Haas. 1995. Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG. Immunity 2:629.
    • (1995) Immunity , vol.2 , pp. 629
    • Kaloff, C.R.1    Haas, I.G.2
  • 28
    • 0032838622 scopus 로고    scopus 로고
    • BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly
    • Lee, Y. K., J. W. Brewer, R. Hellman, and L. M. Hendershot. 1999. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly. Mol. Biol. Cell 10:2209.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2209
    • Lee, Y.K.1    Brewer, J.W.2    Hellman, R.3    Hendershot, L.M.4
  • 29
    • 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., Y.-K. Usherwood, and L. M. Herdershot. 2001. Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release. Immunity 15:105.
    • (2001) Immunity , vol.15 , pp. 105
    • Vanhove, M.1    Usherwood, Y.-K.2    Herdershot, L.M.3
  • 30
    • 0032558362 scopus 로고    scopus 로고
    • H in single-chain antibody fragments, investigated with mutants engineered for stability
    • H in single-chain antibody fragments, investigated with mutants engineered for stability. Biochemistry 37:13120.
    • (1998) Biochemistry , vol.37 , pp. 13120
    • Worn, A.1    Pluckthun, A.2
  • 31
    • 0028928021 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., S. Dirks, and I. G. Haas. 1995. 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.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1764
    • Knittler, M.R.1    Dirks, S.2    Haas, I.G.3
  • 32
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., J. L. Dul, and Y. Argon. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370:373.
    • (1994) Nature , vol.370 , pp. 373
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 33
    • 0029890917 scopus 로고    scopus 로고
    • Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants
    • Hendershot, L., J. Wei, J. Gaut, J. Melnick, S. Aviel, and Y. Argon. 1996. Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants. Proc. Natl. Acad. Sci. USA 93:5269.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5269
    • Hendershot, L.1    Wei, J.2    Gaut, J.3    Melnick, J.4    Aviel, S.5    Argon, Y.6
  • 34
    • 0030320813 scopus 로고    scopus 로고
    • Contribution of the intramolecular disulfide bridge to the folding and stability of REIv, the variable domain of a human immunoglobulin κ light chain
    • Frisch, C., H. Komar, A. Schmidt, G. Kleeman, A. Reinhardt, E. Pohl, I. Uson, T. R. Schneider, and H.-J. Fritz. 1996. Contribution of the intramolecular disulfide bridge to the folding and stability of REIv, the variable domain of a human immunoglobulin κ light chain. Folding and Design 1:431.
    • (1996) Folding and Design , vol.1 , pp. 431
    • Frisch, C.1    Komar, H.2    Schmidt, A.3    Kleeman, G.4    Reinhardt, A.5    Pohl, E.6    Uson, I.7    Schneider, T.R.8    Fritz, H.-J.9
  • 35
    • 0028784428 scopus 로고
    • Identification of residues that stabilize the single-chain Fv of monoclonal antibodies B3
    • Benhar, I., and I. Pastan. 1995. Identification of residues that stabilize the single-chain Fv of monoclonal antibodies B3. J. Biol. Chem. 270:23373.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23373
    • Benhar, I.1    Pastan, I.2


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