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http://purl.uniprot.org/citations/23634281http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23634281http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23634281http://www.w3.org/2000/01/rdf-schema#comment"Cellular activity of BM-ca, a novel humanized anti-CD20 antibody, was quantitatively compared with that of two other anti-CD20 antibodies used for clinical practice, rituximab and ofatumumab. The results of a complement-dependent cytotoxicity (CDC) assay revealed that the strongest antibody was ofatumumab, followed by BM-ca, with rituximab being the weakest. Ofatumumab and BM-ca were effective not only against rituximab-sensitive SU-DHL-4 cells but also against rituximab-resistant RC-K8 cells. In an antibody-dependent cell-mediated cytotoxicity (ADCC) assay, although the effective concentrations against SU-DHL-4 cells were almost the same among these three antibodies, the maximum cytotoxic level was the highest for BM-ca. In an anti-cell proliferation assay using SU-DHL-4 cells, BM-ca was the most effective and ofatumumab, the weakest. Against RC-K8 cells, only BM-ca was effective. When combined with each of four cancer chemotherapeutics (prednisolone, vincristine, hydroxydaunorubicin, and cisplatin), BM-ca exerted the most effective combinatorial anti-cell proliferation activity. To assess the in vivo effect of BM-ca, we intravenously administered BM-ca into cynomolgus monkeys and found that the peripheral B-cell levels did not decrease in half of the animals. Sequencing of cDNA encoding CD20 of cynomolgus monkeys revealed that the responders and nonresponders had Leu/Pro (hetero) and Leu/Leu (homo) at amino acid (a.a.) position 160, respectively, suggesting that the epitope recognized by BM-ca was around this a.a. By analyzing reactivity to synthetic peptides, the epitope recognized by BM-ca was estimated to be a.a.'s 156-166, not shared with rituximab and ofatumumab. These results suggest BM-ca to be a promising anti-CD20 antibody having superior properties and recognizing a unique epitope."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.org/dc/terms/identifier"doi:10.1002/cam4.60"xsd:string
http://purl.uniprot.org/citations/23634281http://purl.org/dc/terms/identifier"doi:10.1002/cam4.60"xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Kobayashi H."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Kobayashi H."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Uchiyama Y."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Uchiyama Y."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Komatsu Y."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Komatsu Y."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Matsunaga Y."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Matsunaga Y."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Nagura K."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/author"Nagura K."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/name"Cancer Med."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/name"Cancer Med"xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/pages"130-143"xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/pages"130-143"xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/title"Novel humanized anti-CD20 antibody BM-ca binds to a unique epitope and exerts stronger cellular activity than others."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/title"Novel humanized anti-CD20 antibody BM-ca binds to a unique epitope and exerts stronger cellular activity than others."xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/volume"2"xsd:string
http://purl.uniprot.org/citations/23634281http://purl.uniprot.org/core/volume"2"xsd:string
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