ChloroquineV1, Main, Exploration, bibRecord, 002A49

Degradation of radioiodinated B cell monoclonal antibodies: inhibition via a FCγ -receptor-II-mediated mechanism and by drugs

Identifieur interne : 002A49 ( Main/Exploration ); précédent : 002A48; suivant : 002A50

Degradation of radioiodinated B cell monoclonal antibodies: inhibition via a FCγ -receptor-II-mediated mechanism and by drugs

Auteurs : Susan F. Vervoordeldonk [Pays-Bas] ; Astrid Y. Balkenende [Pays-Bas] ; H. Van Den Berg ; A. E. G. Kr. Von Dem Borne ; C. E. Van Der Schoot [Pays-Bas] ; E. F. Van Leeuwen ; Ineke C. M. Slaper-Cortenbach [Pays-Bas] ; C. E. Van Der Schoot

Source :

Cancer Immunology, Immunotherapy [ 0340-7004 ] ; 1996-02-01.

RBID : ISTEX:9EE2C7514DF3A01E2997B79FE58A01D7E62B97A5

English descriptors

KwdEn :
- B cell malignancies, Degradation, Fcγ receptor, Key words Monoclonal antibody, Radioimmunotherapy.
Teeft :
- Cancer immunol immunother, Catabolism, Cell malignancies, Cell surface, Chloroquine, Churchill livingstone, Colchicine, Daudi, Daudi cells, Degradation, Degradation products, Degraded, Edinburgh london melbourne, Etoposide, Igg1, Igg2a, Immunol, Internalization, Intracellular, Lymphoma, Malignant, Malignant cells, Monensin, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Murine, Peak plasma concentrations, Radioactivity, Radioiodinated, Radiolabeled, Radiolabeled antibodies, Radiolabelled, Ramos, Ramos cells, Receptor, Simultaneous application, Single agents, Subsequent degradation, Target cell, Taxol, Therapeutic drugs, Therapeutic effect, Trichloroacetic acid, Tumor cells, Various agents, Verapamil, Vinblastine, Vincristine.

Abstract

Abstract: Our aim is to treat patients with B cell malignancies with radioimmunotherapy using monoclonal antibodies (mAb) such as CD19, CD20 and CD22. In this study we investigated the rate of internalization and catabolism of these mAb. After 24 h at 37°C, 20% – 25% of initially cell-bound 125I-CD19 mAb and 125I-CD22 mAb was degraded in B cells, whereas almost no degradation occurred after binding of 125I-CD20 mAb. For B cells expressing Fcγ receptor II (FcγRII), isotype-dependent degradation was noted as the CD19 IgG1 mAb showed an enhanced degradation rate compared to the switch variant IgG2a. The effect of various pharmaceutical agents that delay the internalization or subsequent degradation of mAb was evaluated. The degradation was inhibited most effectively by a combination of etoposide and vinblastine, resulting in accumulation of radioactivity in the target cell. Also the simultaneous application of CD20 or CD22 with 125I-CD19 mAb or of CD20 with 125I-CD22 mAb proved to be a potent inhibitor of the rapid degradation of these mAb, by inhibiting internalization via an FcγRII-mediated mechanism. Both methods of reducing the degradation of radioiodinated mAb are expected to prolong irradiation of malignant B cells and consequently result in an enhanced therapeutic effect in vivo.

Url:

https://api.istex.fr/ark:/67375/1BB-2R8J1Z9V-V/fulltext.pdf

DOI: 10.1007/s002620050247

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Catabolism</term>
<term>Cell malignancies</term>
<term>Cell surface</term>
<term>Chloroquine</term>
<term>Churchill livingstone</term>
<term>Colchicine</term>
<term>Daudi</term>
<term>Daudi cells</term>
<term>Degradation</term>
<term>Degradation products</term>
<term>Degraded</term>
<term>Edinburgh london melbourne</term>
<term>Etoposide</term>
<term>Igg1</term>
<term>Igg2a</term>
<term>Immunol</term>
<term>Internalization</term>
<term>Intracellular</term>
<term>Lymphoma</term>
<term>Malignant</term>
<term>Malignant cells</term>
<term>Monensin</term>
<term>Monoclonal</term>
<term>Monoclonal antibodies</term>
<term>Monoclonal antibody</term>
<term>Murine</term>
<term>Peak plasma concentrations</term>
<term>Radioactivity</term>
<term>Radioiodinated</term>
<term>Radiolabeled</term>
<term>Radiolabeled antibodies</term>
<term>Radiolabelled</term>
<term>Ramos</term>
<term>Ramos cells</term>
<term>Receptor</term>
<term>Simultaneous application</term>
<term>Single agents</term>
<term>Subsequent degradation</term>
<term>Target cell</term>
<term>Taxol</term>
<term>Therapeutic drugs</term>
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<front><div type="abstract" xml:lang="en">Abstract:  Our aim is to treat patients with B cell malignancies with radioimmunotherapy using monoclonal antibodies (mAb) such as CD19, CD20 and CD22. In this study we investigated the rate of internalization and catabolism of these mAb. After 24 h at 37°C, 20% – 25% of initially cell-bound 125I-CD19 mAb and 125I-CD22 mAb was degraded in B cells, whereas almost no degradation occurred after binding of 125I-CD20 mAb. For B cells expressing Fcγ receptor II (FcγRII), isotype-dependent degradation was noted as the CD19 IgG1 mAb showed an enhanced degradation rate compared to the switch variant IgG2a. The effect of various pharmaceutical agents that delay the internalization or subsequent degradation of mAb was evaluated. The degradation was inhibited most effectively by a combination of etoposide and vinblastine, resulting in accumulation of radioactivity in the target cell. Also the simultaneous application of CD20 or CD22 with 125I-CD19 mAb or of CD20 with 125I-CD22 mAb proved to be a potent inhibitor of the rapid degradation of these mAb, by inhibiting internalization via an FcγRII-mediated mechanism. Both methods of reducing the degradation of radioiodinated mAb are expected to prolong irradiation of malignant B cells and consequently result in an enhanced therapeutic effect in vivo.</div>
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Degradation of radioiodinated B cell monoclonal antibodies: inhibition via a FCγ -receptor-II-mediated mechanism and by drugs

Degradation of radioiodinated B cell monoclonal antibodies: inhibition via a FCγ -receptor-II-mediated mechanism and by drugs

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

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