Binding Affinity, Specificity and Comparative Biodistribution of the Parental Murine Monoclonal Antibody MX35 (Anti-NaPi2b) and Its Humanized Version Rebmab200

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Citações na Scopus
13
Tipo de produção
article
Data de publicação
2015
Título da Revista
ISSN da Revista
Título do Volume
Editora
PUBLIC LIBRARY SCIENCE
Autores
LINDEGREN, Sture
BACK, Tom
HORTA, Bruno Brasil
MORO, Ana Maria
OKAMOTO, Oswaldo Keith
JACOBSSON, Lars
CEDERKRANTZ, Elin
Citação
PLOS ONE, v.10, n.5, article ID e0126298, 16p, 2015
Projetos de Pesquisa
Unidades Organizacionais
Fascículo
Resumo
The aim of this preclinical study was to evaluate the characteristics of the monoclonal antibody Rebmab200, which is a humanized version of the ovarian-specific murine antibody MX35. This investigation contributes to the foundation for future clinical alpha-radioimmunotherapy of minimal residual ovarian cancer with At-211-Rebmab200. Here, the biodistribution of 211At-Rebmab200 was evaluated, as was the utility of Tc-99m-Rebmab200 for bioimaging. Rebmab200 was directly compared with its murine counterpart MX35 in terms of its in-vitro capacity for binding the immobilized NaPi2B epitope and live cells; we also assessed its biodistribution in nude mice carrying subcutaneous OVCAR-3 tumors. Tumor antigen and cell binding were similar between Rebmab200 and murine MX35, as was biodistribution, including normal tissue uptake and in-vivo tumor binding. We also demonstrated that Tc-99m-Rebmab200 can be used for single-photon emission computed tomography of subcutaneous ovarian carcinomas in tumor-bearing mice. Taken together, our data support the further development of Rebmab200 for radioimmunotherapy and diagnostics.
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Referências
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