Functional properties of FC-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells
FC-2.15 is a murine IgM monoclonal antibody (mAb) that recognizes a cell-surface antigen (Ag2.15) expressed in most tumor-proliferating cells of human breast carcinomas and other neoplasias. In this study the cytotoxic ability of mAb FC-2.15, its cell-surface binding properties and endocytosis in Ag...
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paper:paper_03407004_v41_n1_p15_Ballare2023-06-08T15:34:08Z Functional properties of FC-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells Ballaré, Cecilia J. Barrio, María Marcela Portela, Paula Breast cancer Complement Cytotoxicity Monoclonal antibody (mAb) monoclonal antibody monoclonal antibody fc 2 15 unclassified drug article breast cancer cancer cell culture controlled study cytotoxicity female human human cell priority journal Antibodies, Monoclonal Antibody-Dependent Cell Cytotoxicity Antigen-Antibody Complex Antigens, Neoplasm Breast Neoplasms Complement Complement Activation Cytotoxicity, Immunologic Endocytosis Human In Vitro Support, Non-U.S. Gov't Tumor Cells, Cultured FC-2.15 is a murine IgM monoclonal antibody (mAb) that recognizes a cell-surface antigen (Ag2.15) expressed in most tumor-proliferating cells of human breast carcinomas and other neoplasias. In this study the cytotoxic ability of mAb FC-2.15, its cell-surface binding properties and endocytosis in Ag2.15-expressing (Ag2.15+) cells were investigated. A51Cr-release assay was used to test the FC-2.15-mediated cytotoxicity. When human serum was used as source of complement, FC-2.15 exerted a strong cytotoxic effect against human Ag2.15+ cells such as MCF-7 (breast cancer cell line), primary breast carcinoma cells, polymorphonuclear leukocytes and chronic myeloid leukemia cells. The mAb concentration range was 1-50 μg/ml. Cytotoxicity was completely abolished when complement was inactivated. Only 3.8±2.9% of MCF-7 cells survived the treatment with FC-2.15 in the presence of human serum. A flow-cytometry assay was performed to study the Ag2.15 expression of the surviving cells and they were found to be Ag2.15-. FC-2.15 did not mediate antibody-dependent cell cytotoxicity when different effector cells were used. Scatchard analysis with125I-FC-2.15 on MCF-7 cells demonstrated an affinity constant of 6.9×107 M-1 and 2.8×106 antigenic sites/cell.125I-FC-2.15 was internalized to cytoplasmic vesicles reaching a maximum of 27% after 6 h incubation, followed by the release of labeled degradation products to the supernatant. FC-2.15 appears to exert its cytotoxic effect mainly in the presence of human complement, it reacts with intermediate affinity with a high-density surface antigen, and it is slowly internalized by Ag2.15+ cells. © 1995 Springer-Verlag. Fil:Ballaré, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Barrio, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Portela, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1995 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03407004_v41_n1_p15_Ballare http://hdl.handle.net/20.500.12110/paper_03407004_v41_n1_p15_Ballare |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Breast cancer Complement Cytotoxicity Monoclonal antibody (mAb) monoclonal antibody monoclonal antibody fc 2 15 unclassified drug article breast cancer cancer cell culture controlled study cytotoxicity female human human cell priority journal Antibodies, Monoclonal Antibody-Dependent Cell Cytotoxicity Antigen-Antibody Complex Antigens, Neoplasm Breast Neoplasms Complement Complement Activation Cytotoxicity, Immunologic Endocytosis Human In Vitro Support, Non-U.S. Gov't Tumor Cells, Cultured |
spellingShingle |
Breast cancer Complement Cytotoxicity Monoclonal antibody (mAb) monoclonal antibody monoclonal antibody fc 2 15 unclassified drug article breast cancer cancer cell culture controlled study cytotoxicity female human human cell priority journal Antibodies, Monoclonal Antibody-Dependent Cell Cytotoxicity Antigen-Antibody Complex Antigens, Neoplasm Breast Neoplasms Complement Complement Activation Cytotoxicity, Immunologic Endocytosis Human In Vitro Support, Non-U.S. Gov't Tumor Cells, Cultured Ballaré, Cecilia J. Barrio, María Marcela Portela, Paula Functional properties of FC-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells |
topic_facet |
Breast cancer Complement Cytotoxicity Monoclonal antibody (mAb) monoclonal antibody monoclonal antibody fc 2 15 unclassified drug article breast cancer cancer cell culture controlled study cytotoxicity female human human cell priority journal Antibodies, Monoclonal Antibody-Dependent Cell Cytotoxicity Antigen-Antibody Complex Antigens, Neoplasm Breast Neoplasms Complement Complement Activation Cytotoxicity, Immunologic Endocytosis Human In Vitro Support, Non-U.S. Gov't Tumor Cells, Cultured |
description |
FC-2.15 is a murine IgM monoclonal antibody (mAb) that recognizes a cell-surface antigen (Ag2.15) expressed in most tumor-proliferating cells of human breast carcinomas and other neoplasias. In this study the cytotoxic ability of mAb FC-2.15, its cell-surface binding properties and endocytosis in Ag2.15-expressing (Ag2.15+) cells were investigated. A51Cr-release assay was used to test the FC-2.15-mediated cytotoxicity. When human serum was used as source of complement, FC-2.15 exerted a strong cytotoxic effect against human Ag2.15+ cells such as MCF-7 (breast cancer cell line), primary breast carcinoma cells, polymorphonuclear leukocytes and chronic myeloid leukemia cells. The mAb concentration range was 1-50 μg/ml. Cytotoxicity was completely abolished when complement was inactivated. Only 3.8±2.9% of MCF-7 cells survived the treatment with FC-2.15 in the presence of human serum. A flow-cytometry assay was performed to study the Ag2.15 expression of the surviving cells and they were found to be Ag2.15-. FC-2.15 did not mediate antibody-dependent cell cytotoxicity when different effector cells were used. Scatchard analysis with125I-FC-2.15 on MCF-7 cells demonstrated an affinity constant of 6.9×107 M-1 and 2.8×106 antigenic sites/cell.125I-FC-2.15 was internalized to cytoplasmic vesicles reaching a maximum of 27% after 6 h incubation, followed by the release of labeled degradation products to the supernatant. FC-2.15 appears to exert its cytotoxic effect mainly in the presence of human complement, it reacts with intermediate affinity with a high-density surface antigen, and it is slowly internalized by Ag2.15+ cells. © 1995 Springer-Verlag. |
author |
Ballaré, Cecilia J. Barrio, María Marcela Portela, Paula |
author_facet |
Ballaré, Cecilia J. Barrio, María Marcela Portela, Paula |
author_sort |
Ballaré, Cecilia J. |
title |
Functional properties of FC-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells |
title_short |
Functional properties of FC-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells |
title_full |
Functional properties of FC-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells |
title_fullStr |
Functional properties of FC-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells |
title_full_unstemmed |
Functional properties of FC-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells |
title_sort |
functional properties of fc-2.15, a monoclonal antibody that mediates human complement cytotoxicity against breast cancer cells |
publishDate |
1995 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03407004_v41_n1_p15_Ballare http://hdl.handle.net/20.500.12110/paper_03407004_v41_n1_p15_Ballare |
work_keys_str_mv |
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_version_ |
1768546542308818944 |