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Volumn 1844, Issue 11, 2014, Pages 1943-1950

PH-dependent antigen-binding antibodies as a novel therapeutic modality

Author keywords

Antibody engineering; Monoclonal antibody; pH dependent

Indexed keywords

ECULIZUMAB; FC RECEPTOR; HISTIDINE; MEMBRANE ANTIGEN; MONOCLONAL ANTIBODY; TOCILIZUMAB;

EID: 85027938012     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.08.003     Document Type: Review
Times cited : (51)

References (45)
  • 1
    • 84871622500 scopus 로고    scopus 로고
    • Therapeutic antibodies: Market considerations, disease targets and bioprocessing
    • J.G. Elvin, R.G. Couston, and C.F. van der Walle Therapeutic antibodies: market considerations, disease targets and bioprocessing Int. J. Pharm. 440 2013 83 98
    • (2013) Int. J. Pharm. , vol.440 , pp. 83-98
    • Elvin, J.G.1    Couston, R.G.2    Van Der Walle, C.F.3
  • 2
    • 84872858296 scopus 로고    scopus 로고
    • Which are the antibodies to watch in 2013?
    • J.M. Reichert Which are the antibodies to watch in 2013? mAbs 5 2013 1 4
    • (2013) MAbs , vol.5 , pp. 1-4
    • Reichert, J.M.1
  • 3
    • 79952399087 scopus 로고    scopus 로고
    • Beyond natural antibodies: The power of in vitro display technologies
    • A.R. Bradbury, S. Sidhu, S. Dubel, and J. McCafferty Beyond natural antibodies: the power of in vitro display technologies Nat. Biotechnol. 29 2011 245 254
    • (2011) Nat. Biotechnol. , vol.29 , pp. 245-254
    • Bradbury, A.R.1    Sidhu, S.2    Dubel, S.3    McCafferty, J.4
  • 4
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibody-affinity improvement beyond in vivo maturation
    • S.M. Lippow, K.D. Wittrup, and B. Tidor Computational design of antibody-affinity improvement beyond in vivo maturation Nat. Biotechnol. 25 2007 1171 1176
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 6
    • 33747631571 scopus 로고    scopus 로고
    • Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn)
    • W.F. Dall'Acqua, P.A. Kiener, and H. Wu Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn) J. Biol. Chem. 281 2006 23514 23524
    • (2006) J. Biol. Chem. , vol.281 , pp. 23514-23524
    • Dall'Acqua, W.F.1    Kiener, P.A.2    Wu, H.3
  • 7
    • 79955646410 scopus 로고    scopus 로고
    • Modulation of antibody effector function
    • J.R. Desjarlais, and G.A. Lazar Modulation of antibody effector function Exp. Cell Res. 317 2011 1278 1285
    • (2011) Exp. Cell Res. , vol.317 , pp. 1278-1285
    • Desjarlais, J.R.1    Lazar, G.A.2
  • 9
    • 84875955851 scopus 로고    scopus 로고
    • Redirection of T-cell effector functions for cancer therapy: Bispecific antibodies and chimeric antigen receptors
    • A. Satta, D. Mezzanzanica, F. Turatti, S. Canevari, and M. Figini Redirection of T-cell effector functions for cancer therapy: bispecific antibodies and chimeric antigen receptors Future Oncol. 9 2013 527 539
    • (2013) Future Oncol. , vol.9 , pp. 527-539
    • Satta, A.1    Mezzanzanica, D.2    Turatti, F.3    Canevari, S.4    Figini, M.5
  • 11
    • 43649104094 scopus 로고    scopus 로고
    • The recombinant humanized anti-IL-6 receptor antibody tocilizumab, an innovative drug for the treatment of rheumatoid arthritis
    • Y. Ohsugi, and T. Kishimoto The recombinant humanized anti-IL-6 receptor antibody tocilizumab, an innovative drug for the treatment of rheumatoid arthritis Expert. Opin. Biol. Ther. 8 2008 669 681
    • (2008) Expert. Opin. Biol. Ther. , vol.8 , pp. 669-681
    • Ohsugi, Y.1    Kishimoto, T.2
  • 12
    • 32444438731 scopus 로고    scopus 로고
    • Elimination mechanisms of therapeutic monoclonal antibodies
    • M.A. Tabrizi, C.M. Tseng, and L.K. Roskos Elimination mechanisms of therapeutic monoclonal antibodies Drug Discov. Today 11 2006 81 88
    • (2006) Drug Discov. Today , vol.11 , pp. 81-88
    • Tabrizi, M.A.1    Tseng, C.M.2    Roskos, L.K.3
  • 13
    • 77449119116 scopus 로고    scopus 로고
    • Biodistribution mechanisms of therapeutic monoclonal antibodies in health and disease
    • M. Tabrizi, G.G. Bornstein, and H. Suria Biodistribution mechanisms of therapeutic monoclonal antibodies in health and disease AAPS J. 12 2010 33 43
    • (2010) AAPS J. , vol.12 , pp. 33-43
    • Tabrizi, M.1    Bornstein, G.G.2    Suria, H.3
  • 14
  • 15
    • 34247344172 scopus 로고    scopus 로고
    • A mechanism-based binding model for the population pharmacokinetics and pharmacodynamics of omalizumab
    • N. Hayashi, Y. Tsukamoto, W.M. Sallas, and P.J. Lowe A mechanism-based binding model for the population pharmacokinetics and pharmacodynamics of omalizumab Br. J. Clin. Pharmacol. 63 2007 548 561
    • (2007) Br. J. Clin. Pharmacol. , vol.63 , pp. 548-561
    • Hayashi, N.1    Tsukamoto, Y.2    Sallas, W.M.3    Lowe, P.J.4
  • 16
    • 34948880782 scopus 로고    scopus 로고
    • Eculizumab: A novel therapy for paroxysmal nocturnal hemoglobinuria
    • K.M. Zareba Eculizumab: a novel therapy for paroxysmal nocturnal hemoglobinuria Drugs Today (Barc) 43 2007 539 546
    • (2007) Drugs Today (Barc) , vol.43 , pp. 539-546
    • Zareba, K.M.1
  • 18
    • 0027239843 scopus 로고
    • Anti-cytokine antibodies as carrier proteins. Prolongation of in vivo effects of exogenous cytokines by injection of cytokine-anti-cytokine antibody complexes
    • F.D. Finkelman, K.B. Madden, S.C. Morris, J.M. Holmes, N. Boiani, I.M. Katona, and C.R. Maliszewski Anti-cytokine antibodies as carrier proteins. Prolongation of in vivo effects of exogenous cytokines by injection of cytokine-anti-cytokine antibody complexes J. Immunol. 151 1993 1235 1244
    • (1993) J. Immunol. , vol.151 , pp. 1235-1244
    • Finkelman, F.D.1    Madden, K.B.2    Morris, S.C.3    Holmes, J.M.4    Boiani, N.5    Katona, I.M.6    Maliszewski, C.R.7
  • 19
    • 0032851674 scopus 로고    scopus 로고
    • Accumulation of antibody-target complexes and the pharmacodynamics of clotting after single intravenous administration of humanized anti-factor IX monoclonal antibody to rats
    • Charles B. Davis, Leeann P. Tobia, Deborah C. Kwok, Christine M. Oishi, Neil Kheterpal, Timothy W. Hepburn, Lisa J. Benincosa, Fung-Sing Chow, and William J. Jusko Accumulation of antibody-target complexes and the pharmacodynamics of clotting after single intravenous administration of humanized anti-factor IX monoclonal antibody to rats Drug Deliv. 6 1999 171 179
    • (1999) Drug Deliv. , vol.6 , pp. 171-179
    • Davis, C.B.1    Tobia, L.P.2    Kwok, D.C.3    Oishi, C.M.4    Kheterpal, N.5    Hepburn, T.W.6    Benincosa, L.J.7    Chow, F.-S.8    Jusko, W.J.9
  • 24
    • 77958583035 scopus 로고    scopus 로고
    • Properties of a general PK/PD model of antibody-ligand interactions for therapeutic antibodies that bind to soluble endogenous targets
    • J.P. Davda, and R.J. Hansen Properties of a general PK/PD model of antibody-ligand interactions for therapeutic antibodies that bind to soluble endogenous targets mAbs 2 2010 576 588
    • (2010) MAbs , vol.2 , pp. 576-588
    • Davda, J.P.1    Hansen, R.J.2
  • 26
    • 29044445019 scopus 로고    scopus 로고
    • Reviews preclinical safety and immune-modulating effects of therapeutic monoclonal antibodies to interleukin-6 and tumor necrosis factor-alpha in cynomolgus macaques
    • P.L. Martin, J. Cornacoff, U. Prabhakar, T. Lohr, G. Treacy, J.E. Sutherland, S. Hersey, and E. Martin Reviews preclinical safety and immune-modulating effects of therapeutic monoclonal antibodies to interleukin-6 and tumor necrosis factor-alpha in cynomolgus macaques J. Immunotoxicol. 1 2005 131 139
    • (2005) J. Immunotoxicol. , vol.1 , pp. 131-139
    • Martin, P.L.1    Cornacoff, J.2    Prabhakar, U.3    Lohr, T.4    Treacy, G.5    Sutherland, J.E.6    Hersey, S.7    Martin, E.8
  • 29
    • 84867796429 scopus 로고    scopus 로고
    • Fc engineering: Serum half-life modulation through FcRn binding
    • T. Olafsen Fc engineering: serum half-life modulation through FcRn binding Methods Mol. Biol. 907 2012 537 556
    • (2012) Methods Mol. Biol. , vol.907 , pp. 537-556
    • Olafsen, T.1
  • 30
    • 27144465484 scopus 로고    scopus 로고
    • Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels
    • C. Vaccaro, J. Zhou, R.J. Ober, and E.S. Ward Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels Nat. Biotechnol. 23 2005 1283 1288
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1283-1288
    • Vaccaro, C.1    Zhou, J.2    Ober, R.J.3    Ward, E.S.4
  • 31
    • 0021243024 scopus 로고
    • The blockade of Fc receptor-mediated clearance of immune complexes in vivo by a monoclonal antibody (2.4G2) directed against Fc receptors on murine leukocytes
    • R.J. Kurlander, D.M. Ellison, and J. Hall The blockade of Fc receptor-mediated clearance of immune complexes in vivo by a monoclonal antibody (2.4G2) directed against Fc receptors on murine leukocytes J. Immunol. 133 1984 855 862
    • (1984) J. Immunol. , vol.133 , pp. 855-862
    • Kurlander, R.J.1    Ellison, D.M.2    Hall, J.3
  • 33
    • 77958577389 scopus 로고    scopus 로고
    • Divergent intracellular sorting of Fc{gamma}RIIA and Fc{gamma}RIIB2
    • C.Y. Zhang, and J.W. Booth Divergent intracellular sorting of Fc{gamma}RIIA and Fc{gamma}RIIB2 J. Biol. Chem. 285 2010 34250 34258
    • (2010) J. Biol. Chem. , vol.285 , pp. 34250-34258
    • Zhang, C.Y.1    Booth, J.W.2
  • 34
    • 0032779054 scopus 로고    scopus 로고
    • Variant genotypes of the low-affinity Fcgamma receptors in two control populations and a review of low-affinity Fcgamma receptor polymorphisms in control and disease populations
    • T. Lehrnbecher, C.B. Foster, S. Zhu, S.F. Leitman, L.R. Goldin, K. Huppi, and S.J. Chanock Variant genotypes of the low-affinity Fcgamma receptors in two control populations and a review of low-affinity Fcgamma receptor polymorphisms in control and disease populations Blood 94 1999 4220 4232
    • (1999) Blood , vol.94 , pp. 4220-4232
    • Lehrnbecher, T.1    Foster, C.B.2    Zhu, S.3    Leitman, S.F.4    Goldin, L.R.5    Huppi, K.6    Chanock, S.J.7
  • 37
    • 0032518373 scopus 로고    scopus 로고
    • Structural basis of pH-dependent antibody binding by the neonatal Fc receptor
    • D.E. Vaughn, and P.J. Bjorkman Structural basis of pH-dependent antibody binding by the neonatal Fc receptor Structure 6 1998 63 73
    • (1998) Structure , vol.6 , pp. 63-73
    • Vaughn, D.E.1    Bjorkman, P.J.2
  • 39
    • 84860388904 scopus 로고    scopus 로고
    • A combinatorial histidine scanning library approach to engineer highly pH-dependent protein switches
    • M.L. Murtaugh, S.W. Fanning, T.M. Sharma, A.M. Terry, and J.R. Horn A combinatorial histidine scanning library approach to engineer highly pH-dependent protein switches Protein Sci. 20 2011 1619 1631
    • (2011) Protein Sci. , vol.20 , pp. 1619-1631
    • Murtaugh, M.L.1    Fanning, S.W.2    Sharma, T.M.3    Terry, A.M.4    Horn, J.R.5
  • 40
    • 0032481105 scopus 로고    scopus 로고
    • Calcium uptake via endocytosis with rapid release from acidifying endosomes
    • J.V. Gerasimenko, A.V. Tepikin, O.H. Petersen, and O.V. Gerasimenko Calcium uptake via endocytosis with rapid release from acidifying endosomes Curr. Biol. 8 1998 1335 1338
    • (1998) Curr. Biol. , vol.8 , pp. 1335-1338
    • Gerasimenko, J.V.1    Tepikin, A.V.2    Petersen, O.H.3    Gerasimenko, O.V.4
  • 42
    • 0036713917 scopus 로고    scopus 로고
    • Rational cytokine design for increased lifetime and enhanced potency using pH-activated "histidine switching"
    • C.A. Sarkar, K. Lowenhaupt, T. Horan, T.C. Boone, B. Tidor, and D.A. Lauffenburger Rational cytokine design for increased lifetime and enhanced potency using pH-activated "histidine switching" Nat. Biotechnol. 20 2002 908 913
    • (2002) Nat. Biotechnol. , vol.20 , pp. 908-913
    • Sarkar, C.A.1    Lowenhaupt, K.2    Horan, T.3    Boone, T.C.4    Tidor, B.5    Lauffenburger, D.A.6
  • 43
    • 0014240071 scopus 로고
    • The glomerular permeability determined by dextran clearance using Sephadex gel filtration
    • C.E. Mogensen The glomerular permeability determined by dextran clearance using Sephadex gel filtration Scand. J. Clin. Lab. Invest. 21 1968 77 82
    • (1968) Scand. J. Clin. Lab. Invest. , vol.21 , pp. 77-82
    • Mogensen, C.E.1
  • 44
    • 0034634584 scopus 로고    scopus 로고
    • Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor
    • H. Feinberg, D. Torgersen, K. Drickamer, and W.I. Weis Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor J. Biol. Chem. 275 2000 35176 35184
    • (2000) J. Biol. Chem. , vol.275 , pp. 35176-35184
    • Feinberg, H.1    Torgersen, D.2    Drickamer, K.3    Weis, W.I.4
  • 45
    • 55249114139 scopus 로고    scopus 로고
    • Molecular studies of pH-dependent ligand interactions with the low-density lipoprotein receptor
    • T. Yamamoto, H.C. Chen, E. Guigard, C.M. Kay, and R.O. Ryan Molecular studies of pH-dependent ligand interactions with the low-density lipoprotein receptor Biochemistry 47 2008 11647 11652
    • (2008) Biochemistry , vol.47 , pp. 11647-11652
    • Yamamoto, T.1    Chen, H.C.2    Guigard, E.3    Kay, C.M.4    Ryan, R.O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.