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Volumn 101, Issue 10, 2010, Pages 2227-2233

A defucosylated anti-CD317 antibody exhibited enhanced antibody-dependent cellular cytotoxicity against primary myeloma cells in the presence of effectors from patients

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE LINKED OLIGOSACCHARIDE; FUCOSYLTRANSFERASE; GUANOSINE DIPHOSPHATE FUCOSE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY CD137; UNCLASSIFIED DRUG; BST2 PROTEIN, HUMAN; GLUCOSE TRANSPORTER; GLUCOSYLTRANSFERASE; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; LEUKOCYTE ANTIGEN; MEMBRANE PROTEIN; SLC35C1 PROTEIN, HUMAN;

EID: 77957094316     PISSN: 13479032     EISSN: 13497006     Source Type: Journal    
DOI: 10.1111/j.1349-7006.2010.01663.x     Document Type: Article
Times cited : (21)

References (33)
  • 1
    • 74049142026 scopus 로고    scopus 로고
    • The use of novel agents in the treatment of relapsed and refractory multiple myeloma
    • Laubach JP, Mahindra A, Mitsiades CS. The use of novel agents in the treatment of relapsed and refractory multiple myeloma. Leukemia 2009, 23:2222-32.
    • (2009) Leukemia , vol.23 , pp. 2222-2232
    • Laubach, J.P.1    Mahindra, A.2    Mitsiades, C.S.3
  • 2
    • 66849111894 scopus 로고    scopus 로고
    • Emerging combination treatment strategies containing novel agents in newly diagnosed multiple myeloma
    • Lonial S, Cavenagh J. Emerging combination treatment strategies containing novel agents in newly diagnosed multiple myeloma. Br J Haematol 2009, 145:681-708.
    • (2009) Br J Haematol , vol.145 , pp. 681-708
    • Lonial, S.1    Cavenagh, J.2
  • 3
    • 64749088834 scopus 로고    scopus 로고
    • Emerging treatments for multiple myeloma: beyond immunomodulatory drugs and bortezomib
    • Mitsiades CS, Hideshima T, Chauhan D. Emerging treatments for multiple myeloma: beyond immunomodulatory drugs and bortezomib. Semin Hematol 2009, 46:166-75.
    • (2009) Semin Hematol , vol.46 , pp. 166-175
    • Mitsiades, C.S.1    Hideshima, T.2    Chauhan, D.3
  • 4
    • 62349132009 scopus 로고    scopus 로고
    • Monoclonal antibodies for cancer immunotherapy
    • Weiner LM, Dhodapkar MV, Ferrone S. Monoclonal antibodies for cancer immunotherapy. Lancet 2009, 373:1033-40.
    • (2009) Lancet , vol.373 , pp. 1033-1040
    • Weiner, L.M.1    Dhodapkar, M.V.2    Ferrone, S.3
  • 5
    • 0030847878 scopus 로고    scopus 로고
    • Immunotherapy of multiple myeloma with a monoclonal antibody directed against a plasma cell-specific antigen, HM1.24
    • Ozaki S, Kosaka M, Wakatsuki S, Abe M, Koishihara Y, Matsumoto T. Immunotherapy of multiple myeloma with a monoclonal antibody directed against a plasma cell-specific antigen, HM1.24. Blood 1997, 90:3179-86.
    • (1997) Blood , vol.90 , pp. 3179-3186
    • Ozaki, S.1    Kosaka, M.2    Wakatsuki, S.3    Abe, M.4    Koishihara, Y.5    Matsumoto, T.6
  • 6
    • 0033151528 scopus 로고    scopus 로고
    • Humanized anti-HM1.24 antibody mediates myeloma cell cytotoxicity that is enhanced by cytokine stimulation of effector cells
    • Ozaki S, Kosaka M, Wakahara Y. Humanized anti-HM1.24 antibody mediates myeloma cell cytotoxicity that is enhanced by cytokine stimulation of effector cells. Blood 1999, 93:3922-30.
    • (1999) Blood , vol.93 , pp. 3922-3930
    • Ozaki, S.1    Kosaka, M.2    Wakahara, Y.3
  • 7
    • 0032773386 scopus 로고    scopus 로고
    • The humanized anti-HM1.24 antibody effectively kills multiple myeloma cells by human effector cell-mediated cytotoxicity
    • Ono K, Ohtomo T, Yoshida K. The humanized anti-HM1.24 antibody effectively kills multiple myeloma cells by human effector cell-mediated cytotoxicity. Mol Immunol 1999, 36:387-95.
    • (1999) Mol Immunol , vol.36 , pp. 387-395
    • Ono, K.1    Ohtomo, T.2    Yoshida, K.3
  • 8
    • 33744940509 scopus 로고    scopus 로고
    • Construction of a conventional non-radioisotope method to quantify HM1.24 antigens: correlation of HM1.24 levels and ADCC activity of the humanized antibody against HM1.24
    • Kawai S, Koishihara Y, Iida S. Construction of a conventional non-radioisotope method to quantify HM1.24 antigens: correlation of HM1.24 levels and ADCC activity of the humanized antibody against HM1.24. Leuk Res 2006, 30:949-56.
    • (2006) Leuk Res , vol.30 , pp. 949-956
    • Kawai, S.1    Koishihara, Y.2    Iida, S.3
  • 9
    • 33744496095 scopus 로고    scopus 로고
    • Antitumor activity of humanized monoclonal antibody against HM1.24 antigen in human myeloma xenograft models
    • Kawai S, Yoshimura Y, Iida S. Antitumor activity of humanized monoclonal antibody against HM1.24 antigen in human myeloma xenograft models. Oncol Rep 2006, 15:361-7.
    • (2006) Oncol Rep , vol.15 , pp. 361-367
    • Kawai, S.1    Yoshimura, Y.2    Iida, S.3
  • 10
    • 30344434022 scopus 로고    scopus 로고
    • High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G
    • Preithner S, Elm S, Lippold S. High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G. Mol Immunol 2006, 43:1183-93.
    • (2006) Mol Immunol , vol.43 , pp. 1183-1193
    • Preithner, S.1    Elm, S.2    Lippold, S.3
  • 11
    • 33646740982 scopus 로고    scopus 로고
    • Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa
    • Iida S, Misaka H, Inoue M. Nonfucosylated therapeutic IgG1 antibody can evade the inhibitory effect of serum immunoglobulin G on antibody-dependent cellular cytotoxicity through its high binding to FcgammaRIIIa. Clin Cancer Res 2006, 12:2879-87.
    • (2006) Clin Cancer Res , vol.12 , pp. 2879-2887
    • Iida, S.1    Misaka, H.2    Inoue, M.3
  • 12
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields RL, Lai J, Keck R. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem 2002, 277:26733-40.
    • (2002) J Biol Chem , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3
  • 13
    • 0022477288 scopus 로고
    • Two Chinese hamster ovary glycosylation mutants affected in the conversion of GDP-mannose to GDP-fucose
    • Ripka J, Adamany A, Stanley P. Two Chinese hamster ovary glycosylation mutants affected in the conversion of GDP-mannose to GDP-fucose. Arch Biochem Biophys 1986, 249:533-45.
    • (1986) Arch Biochem Biophys , vol.249 , pp. 533-545
    • Ripka, J.1    Adamany, A.2    Stanley, P.3
  • 14
    • 4644245850 scopus 로고    scopus 로고
    • Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity
    • Yamane-Ohnuki N, Kinoshita S, Inoue-Urakubo M. Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnol Bioeng 2004, 87:614-22.
    • (2004) Biotechnol Bioeng , vol.87 , pp. 614-622
    • Yamane-Ohnuki, N.1    Kinoshita, S.2    Inoue-Urakubo, M.3
  • 15
    • 10844222497 scopus 로고    scopus 로고
    • Engineering Chinese hamster ovary cells to maximize effector function of produced antibodies using FUT8 siRNA
    • Mori K, Kuni-Kamochi R, Yamane-Ohnuki N. Engineering Chinese hamster ovary cells to maximize effector function of produced antibodies using FUT8 siRNA. Biotechnol Bioeng 2004, 88:901-8.
    • (2004) Biotechnol Bioeng , vol.88 , pp. 901-908
    • Mori, K.1    Kuni-Kamochi, R.2    Yamane-Ohnuki, N.3
  • 16
    • 34250369571 scopus 로고    scopus 로고
    • Establishment of a GDP-mannose 4,6-dehydratase (GMD) knockout host cell line: a new strategy for generating completely non-fucosylated recombinant therapeutics
    • Kanda Y, Imai-Nishiya H, Kuni-Kamochi R. Establishment of a GDP-mannose 4,6-dehydratase (GMD) knockout host cell line: a new strategy for generating completely non-fucosylated recombinant therapeutics. J Biotechnol 2007, 130:300-10.
    • (2007) J Biotechnol , vol.130 , pp. 300-310
    • Kanda, Y.1    Imai-Nishiya, H.2    Kuni-Kamochi, R.3
  • 17
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1, 4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II
    • Ferrara C, Brünker P, Suter T, Moser S, Püntener U, Umaña P. Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous beta1, 4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II. Biotechnol Bioeng 2006, 93:851-61.
    • (2006) Biotechnol Bioeng , vol.93 , pp. 851-861
    • Ferrara, C.1    Brünker, P.2    Suter, T.3    Moser, S.4    Püntener, U.5    Umaña, P.6
  • 18
    • 33645218704 scopus 로고    scopus 로고
    • Engineered antibody Fc variants with enhanced effector function
    • Lazar GA, Dang W, Karki S. Engineered antibody Fc variants with enhanced effector function. Proc Natl Acad Sci U S A 2006, 103:4005-10.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4005-4010
    • Lazar, G.A.1    Dang, W.2    Karki, S.3
  • 19
    • 34548770705 scopus 로고    scopus 로고
    • Fc optimization of therapeutic antibodies enhances their ability to kill tumor cells in vitro and controls tumor expansion in vivo via low-affinity activating Fcgamma receptors
    • Stavenhagen JB, Gorlatov S, Tuaillon N. Fc optimization of therapeutic antibodies enhances their ability to kill tumor cells in vitro and controls tumor expansion in vivo via low-affinity activating Fcgamma receptors. Cancer Res 2007, 67:8882-90.
    • (2007) Cancer Res , vol.67 , pp. 8882-8890
    • Stavenhagen, J.B.1    Gorlatov, S.2    Tuaillon, N.3
  • 20
    • 0025672645 scopus 로고
    • Homologous recombination at c-fyn locus of mouse embryonic stem cells with use of diphtheria toxin A-fragment gene in negative selection
    • Yagi T, Ikawa Y, Yoshida K. Homologous recombination at c-fyn locus of mouse embryonic stem cells with use of diphtheria toxin A-fragment gene in negative selection. Proc Natl Acad Sci U S A 1990, 87:9918-22.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 9918-9922
    • Yagi, T.1    Ikawa, Y.2    Yoshida, K.3
  • 22
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge JC, Patel TP, Bruce JA, Goulding PN, Charles SM, Parekh RB. Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal Biochem 1995, 230:229-38.
    • (1995) Anal Biochem , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 23
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene
    • Cartron G, Dacheux L, Salles G. Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene. Blood 2002, 99:754-8.
    • (2002) Blood , vol.99 , pp. 754-758
    • Cartron, G.1    Dacheux, L.2    Salles, G.3
  • 24
    • 0642373290 scopus 로고    scopus 로고
    • Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma
    • Weng WK, Levy R. Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma. J Clin Oncol 2003, 21:3940-7.
    • (2003) J Clin Oncol , vol.21 , pp. 3940-3947
    • Weng, W.K.1    Levy, R.2
  • 25
    • 42949157368 scopus 로고    scopus 로고
    • Immunoglobulin G fragment C receptor polymorphisms and clinical efficacy of trastuzumab-based therapy in patients with HER-2/neu-positive metastatic breast cancer
    • Musolino A, Naldi N, Bortesi B. Immunoglobulin G fragment C receptor polymorphisms and clinical efficacy of trastuzumab-based therapy in patients with HER-2/neu-positive metastatic breast cancer. J Clin Oncol 2008, 26:1789-96.
    • (2008) J Clin Oncol , vol.26 , pp. 1789-1796
    • Musolino, A.1    Naldi, N.2    Bortesi, B.3
  • 26
    • 61449239114 scopus 로고    scopus 로고
    • Impact of Fc{gamma}RIIa-Fc{gamma}RIIIa polymorphisms and KRAS mutations on the clinical outcome of patients with metastatic colorectal cancer treated with cetuximab plus irinotecan
    • Bibeau F, Lopez-Crapez E, Di Fiore F. Impact of Fc{gamma}RIIa-Fc{gamma}RIIIa polymorphisms and KRAS mutations on the clinical outcome of patients with metastatic colorectal cancer treated with cetuximab plus irinotecan. J Clin Oncol 2009, 27:1122-9.
    • (2009) J Clin Oncol , vol.27 , pp. 1122-1129
    • Bibeau, F.1    Lopez-Crapez, E.2    Di Fiore, F.3
  • 27
    • 34548509226 scopus 로고    scopus 로고
    • FCGR2A and FCGR3A polymorphisms associated with clinical outcome of epidermal growth factor receptor expressing metastatic colorectal cancer patients treated with single-agent cetuximab
    • Zhang W, Gordon M, Schultheis AM. FCGR2A and FCGR3A polymorphisms associated with clinical outcome of epidermal growth factor receptor expressing metastatic colorectal cancer patients treated with single-agent cetuximab. J Clin Oncol 2007, 25:3712-8.
    • (2007) J Clin Oncol , vol.25 , pp. 3712-3718
    • Zhang, W.1    Gordon, M.2    Schultheis, A.M.3
  • 28
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
    • Ferrara C, Stuart F, Sondermann P, Brünker P, Umaña P. The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J Biol Chem 2006, 281:5032-6.
    • (2006) J Biol Chem , vol.281 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brünker, P.4    Umaña, P.5
  • 29
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa T, Nakamura K, Yamane N. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J Biol Chem 2003, 278:3466-73.
    • (2003) J Biol Chem , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3
  • 30
    • 49249089100 scopus 로고    scopus 로고
    • Regulation of NK cell responsiveness to achieve self-tolerance and maximal responses to diseased target cells
    • Joncker NT, Raulet DH. Regulation of NK cell responsiveness to achieve self-tolerance and maximal responses to diseased target cells. Immunol Rev 2008, 224:85-97.
    • (2008) Immunol Rev , vol.224 , pp. 85-97
    • Joncker, N.T.1    Raulet, D.H.2
  • 31
    • 33646477295 scopus 로고    scopus 로고
    • Impaired activating receptor expression pattern in natural killer cells from patients with multiple myeloma
    • Fauriat C, Mallet F, Olive D, Costello RT. Impaired activating receptor expression pattern in natural killer cells from patients with multiple myeloma. Leukemia 2006, 20:732-3.
    • (2006) Leukemia , vol.20 , pp. 732-733
    • Fauriat, C.1    Mallet, F.2    Olive, D.3    Costello, R.T.4
  • 32
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006, 313:670-3.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 33
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil SJ, Zang T, Bieniasz PD. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature 2008, 451:425-30.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3


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