메뉴 건너뛰기




Volumn 186, Issue 1, 2011, Pages 341-349

Molecular and functional characterization of cynomolgus monkey IgG subclasses

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; IMMUNOGLOBULIN G; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2; IMMUNOGLOBULIN G3; IMMUNOGLOBULIN G4;

EID: 79251585222     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1001685     Document Type: Article
Times cited : (36)

References (37)
  • 2
    • 34447091994 scopus 로고    scopus 로고
    • Preclinical and clinical safety of monoclonal antibodies
    • Tabrizi, M. A., and L. K. Roskos. 2007. Preclinical and clinical safety of monoclonal antibodies. Drug Discov. Today 12: 540-547.
    • (2007) Drug Discov. Today , vol.12 , pp. 540-547
    • Tabrizi, M.A.1    Roskos, L.K.2
  • 5
    • 0037013743 scopus 로고    scopus 로고
    • Interaction sites on human IgG-Fc for FcγR: Current models
    • Jefferis, R., and J. Lund. 2002. Interaction sites on human IgG-Fc for FcγR: current models. Immunol. Lett. 82: 57-65.
    • (2002) Immunol. Lett. , vol.82 , pp. 57-65
    • Jefferis, R.1    Lund, J.2
  • 6
    • 30444461383 scopus 로고    scopus 로고
    • Fcγ receptors: Old friends and new family members
    • Nimmerjahn, F., and J. V. Ravetch. 2006. Fcγ receptors: old friends and new family members. Immunity 24: 19-28.
    • (2006) Immunity , vol.24 , pp. 19-28
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 7
    • 0025762394 scopus 로고
    • The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region
    • Canfield, S. M., and S. L. Morrison. 1991. The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region. J. Exp. Med. 173: 1483-1491.
    • (1991) J. Exp. Med. , vol.173 , pp. 1483-1491
    • Canfield, S.M.1    Morrison, S.L.2
  • 10
    • 0029816997 scopus 로고    scopus 로고
    • Molecular phylogeny of macaques: Implications of nucleotide sequences from an 896-base pair region of mitochondrial DNA
    • Hayasaka, K., K. Fujii, and S. Horai. 1996. Molecular phylogeny of macaques: implications of nucleotide sequences from an 896-base pair region of mitochondrial DNA. Mol. Biol. Evol. 13: 1044-1053.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 1044-1053
    • Hayasaka, K.1    Fujii, K.2    Horai, S.3
  • 12
    • 0347126490 scopus 로고    scopus 로고
    • Rhesus macaque antibody molecules: Sequences and heterogeneity of α and γ constant regions
    • Scinicariello, F., C. N. Engleman, L. Jayashankar, H. M. McClure, and R. Attanasio. 2004. Rhesus macaque antibody molecules: sequences and heterogeneity of α and γ constant regions. Immunology 111: 66-74.
    • (2004) Immunology , vol.111 , pp. 66-74
    • Scinicariello, F.1    Engleman, C.N.2    Jayashankar, L.3    McClure, H.M.4    Attanasio, R.5
  • 13
    • 0036421663 scopus 로고    scopus 로고
    • Over-expression of protein kinase Bα enhances recombinant protein expression in transient systems
    • Ettehadieh, E., S. Wong-Madden, T. Aldrich, K. Lane, and A. E. Morris. 2002. Over-expression of protein kinase Bα enhances recombinant protein expression in transient systems. Cytotechnology 38: 11-14.
    • (2002) Cytotechnology , vol.38 , pp. 11-14
    • Ettehadieh, E.1    Wong-Madden, S.2    Aldrich, T.3    Lane, K.4    Morris, A.E.5
  • 14
    • 0031913654 scopus 로고    scopus 로고
    • Identification of minimal oriP of Epstein-Barr virus required for DNA replication
    • Shirakata, M., and K. Hirai. 1998. Identification of minimal oriP of Epstein-Barr virus required for DNA replication. J. Biochem. 123: 175-181. (Pubitemid 28068582)
    • (1998) Journal of Biochemistry , vol.123 , Issue.1 , pp. 175-181
    • Shirakata, M.1    Hirai, K.2
  • 15
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR
    • Shields, R. L., A. K. Namenuk, K. Hong, Y. G. Meng, J. Rae, J. Briggs, D. Xie, J. Lai, A. Stadlen, B. Li, et al. 2001. High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR. J. Biol. Chem. 276: 6591-6604.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6    Xie, D.7    Lai, J.8    Stadlen, A.9    Li, B.10
  • 16
    • 0024438061 scopus 로고
    • Studies of aglycosylated chimeric mouse-human IgG: Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region
    • Tao, M. H., and S. L. Morrison. 1989. Studies of aglycosylated chimeric mouse-human IgG: role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J. Immunol. 143: 2595-2601.
    • (1989) J. Immunol. , vol.143 , pp. 2595-2601
    • Tao, M.H.1    Morrison, S.L.2
  • 17
    • 0025943212 scopus 로고
    • Identification of the Fcγ receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies
    • Chappel, M. S., D. E. Isenman, M. Everett, Y. Y. Xu, K. J. Dorrington, and M. H. Klein. 1991. Identification of the Fcγ receptor class I binding site in human IgG through the use of recombinant IgG1/IgG2 hybrid and point-mutated antibodies. Proc. Natl. Acad. Sci. USA 88: 9036-9040.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9036-9040
    • Chappel, M.S.1    Isenman, D.E.2    Everett, M.3    Xu, Y.Y.4    Dorrington, K.J.5    Klein, M.H.6
  • 18
    • 0025666553 scopus 로고
    • Molecular definition of interaction sites on human IgG for Fc receptors (huFcγR)
    • Jefferis, R., J. Lund, and J. Pound. 1990. Molecular definition of interaction sites on human IgG for Fc receptors (huFcγR). Mol. Immunol. 27: 1237-1240.
    • (1990) Mol. Immunol. , vol.27 , pp. 1237-1240
    • Jefferis, R.1    Lund, J.2    Pound, J.3
  • 19
    • 0034905149 scopus 로고    scopus 로고
    • The interheavy chain disulfide bonds of IgG4 are in equilibrium with intra-chain disulfide bonds
    • Schuurman, J., G. J. Perdok, A. D. Gorter, and R. C. Aalberse. 2001. The interheavy chain disulfide bonds of IgG4 are in equilibrium with intra-chain disulfide bonds. Mol. Immunol. 38: 1-8.
    • (2001) Mol. Immunol. , vol.38 , pp. 1-8
    • Schuurman, J.1    Perdok, G.J.2    Gorter, A.D.3    Aalberse, R.C.4
  • 20
    • 0029165029 scopus 로고
    • Advances in human immunoglobulin allotypes
    • Grubb, R. 1995. Advances in human immunoglobulin allotypes. Exp. Clin. Immunogenet. 12: 191-197.
    • (1995) Exp. Clin. Immunogenet. , vol.12 , pp. 191-197
    • Grubb, R.1
  • 21
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses
    • Bruhns, P., B. Iannascoli, P. England, D. A. Mancardi, N. Fernandez, S. Jorieux, and M. Daëron. 2009. Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses. Blood 113: 3716-3725.
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1    Iannascoli, B.2    England, P.3    Mancardi, D.A.4    Fernandez, N.5    Jorieux, S.6    Daëron, M.7
  • 22
    • 33744922424 scopus 로고    scopus 로고
    • TGN1412: Time to change the paradigm for the testing of new pharmaceuticals
    • Bhogal, N., and R. Combes. 2006. TGN1412: time to change the paradigm for the testing of new pharmaceuticals. Altern. Lab. Anim. 34: 225-239.
    • (2006) Altern. Lab. Anim. , vol.34 , pp. 225-239
    • Bhogal, N.1    Combes, R.2
  • 23
    • 33744540096 scopus 로고    scopus 로고
    • Antitumor antibodies in the treatment of cancer: Fc receptors link opsonic antibody with cellular immunity
    • Clynes, R. 2006. Antitumor antibodies in the treatment of cancer: Fc receptors link opsonic antibody with cellular immunity. Hematol. Oncol. Clin. North Am. 20: 585-612.
    • (2006) Hematol. Oncol. Clin. North Am. , vol.20 , pp. 585-612
    • Clynes, R.1
  • 24
    • 0030611643 scopus 로고    scopus 로고
    • FcγRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell FcγRIIIa, independently of the FcγRIIIa-48L/R/H phenotype
    • Koene, H. R., M. Kleijer, J. Algra, D. Roos, A. E. von dem Borne, and M. de Haas. 1997. FcγRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell FcγRIIIa, independently of the FcγRIIIa-48L/ R/H phenotype. Blood 90: 1109-1114.
    • (1997) Blood , vol.90 , pp. 1109-1114
    • Koene, H.R.1    Kleijer, M.2    Algra, J.3    Roos, D.4    Von Dem Borne, A.E.5    De Haas, M.6
  • 25
    • 0024342834 scopus 로고
    • Alternative membrane forms of FcγRIII (CD16) on human natural killer cells and neutrophils: Cell type-specific expression of two genes that differ in single nucleotide substitutions
    • Ravetch, J. V., and B. Perussia. 1989. Alternative membrane forms of FcγRIII (CD16) on human natural killer cells and neutrophils: cell type-specific expression of two genes that differ in single nucleotide substitutions. J. Exp. Med. 170: 481-497.
    • (1989) J. Exp. Med. , vol.170 , pp. 481-497
    • Ravetch, J.V.1    Perussia, B.2
  • 26
    • 0031856505 scopus 로고    scopus 로고
    • IgG receptor polymorphisms: Risk factors for disease
    • DOI 10.1007/s002510050426
    • van der Pol, W., and J. G. van de Winkel. 1998. IgG receptor polymorphisms: risk factors for disease. Immunogenetics 48: 222-232. (Pubitemid 28352188)
    • (1998) Immunogenetics , vol.48 , Issue.3 , pp. 222-232
    • Van Der Pol, W.-L.1    Van De Winkel, J.G.J.2
  • 27
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene
    • Cartron, G., L. Dacheux, G. Salles, P. Solal-Celigny, P. Bardos, P. Colombat, and H. Watier. 2002. Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene. Blood 99: 754-758.
    • (2002) Blood , vol.99 , pp. 754-758
    • Cartron, G.1    Dacheux, L.2    Salles, G.3    Solal-Celigny, P.4    Bardos, P.5    Colombat, P.6    Watier, H.7
  • 29
    • 33748515685 scopus 로고    scopus 로고
    • IgG Fc receptor III homologues in nonhuman primate species: Genetic characterization and ligand interactions
    • Rogers, K. A., F. Scinicariello, and R. Attanasio. 2006. IgG Fc receptor III homologues in nonhuman primate species: genetic characterization and ligand interactions. J. Immunol. 177: 3848-3856.
    • (2006) J. Immunol. , vol.177 , pp. 3848-3856
    • Rogers, K.A.1    Scinicariello, F.2    Attanasio, R.3
  • 30
    • 0026766436 scopus 로고
    • Allelic polymorphisms of human Fcγ receptor IIA and Fcγ receptor IIIB: Independent mechanisms for differences in human phagocyte function
    • Salmon, J. E., J. C. Edberg, N. L. Brogle, and R. P. Kimberly. 1992. Allelic polymorphisms of human Fcγ receptor IIA and Fcγ receptor IIIB: independent mechanisms for differences in human phagocyte function. J. Clin. Invest. 89: 1274-1281.
    • (1992) J. Clin. Invest. , vol.89 , pp. 1274-1281
    • Salmon, J.E.1    Edberg, J.C.2    Brogle, N.L.3    Kimberly, R.P.4
  • 31
    • 0031253752 scopus 로고    scopus 로고
    • Flexibility of human IgG subclasses
    • Roux, K. H., L. Strelets, and T. E. Michaelsen. 1997. Flexibility of human IgG subclasses. J. Immunol. 159: 3372-3382.
    • (1997) J. Immunol. , vol.159 , pp. 3372-3382
    • Roux, K.H.1    Strelets, L.2    Michaelsen, T.E.3
  • 33
    • 0025086946 scopus 로고
    • A protein structural change in aglycosylated IgG3 correlates with loss of huFcγR1 and huFcγR111 binding and/or activation
    • Lund, J., T. Tanaka, N. Takahashi, G. Sarmay, Y. Arata, and R. Jefferis. 1990. A protein structural change in aglycosylated IgG3 correlates with loss of huFcγR1 and huFcγR111 binding and/or activation. Mol. Immunol. 27: 1145-1153.
    • (1990) Mol. Immunol. , vol.27 , pp. 1145-1153
    • Lund, J.1    Tanaka, T.2    Takahashi, N.3    Sarmay, G.4    Arata, Y.5    Jefferis, R.6
  • 36
    • 0023933120 scopus 로고
    • Localization of the binding site for the human high-affinity Fc receptor on IgG
    • Duncan, A. R., J. M. Woof, L. J. Partridge, D. R. Burton, and G. Winter. 1988. Localization of the binding site for the human high-affinity Fc receptor on IgG. Nature 332: 563-564.
    • (1988) Nature , vol.332 , pp. 563-564
    • Duncan, A.R.1    Woof, J.M.2    Partridge, L.J.3    Burton, D.R.4    Winter, G.5
  • 37
    • 0028830782 scopus 로고
    • Oligosaccharide-protein interactions in IgG can modulate recognition by Fcγ receptors
    • Lund, J., N. Takahashi, J. D. Pound, M. Goodall, H. Nakagawa, and R. Jefferis. 1995. Oligosaccharide-protein interactions in IgG can modulate recognition by Fcγ receptors. FASEB J. 9: 115-119.
    • (1995) FASEB J. , vol.9 , pp. 115-119
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Nakagawa, H.5    Jefferis, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.