Characterization of the ETSA-21 antigen, a glycosylphosphatidyl-inositol anchor glycoprotein identified in breast cancer cells using monoclonal antibody B21

Mab B21 is a monoclonal antibody (Mab) that recognizes an epithelial tumor surface antigen (ETSA-B21) from diverse human tumor cell lines including breast, ovary, uterus, and their cognate carcinoma tissues. A lower reactivity has been observed in normal breast tissue and benign hyperplesia. In this...

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Autor principal: Annibali, N.V
Otros Autores: Baldi, A.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Mary Ann Liebert Inc. 1997
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Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-0030906024 
024 7 |2 cas  |a phospholipase C, 9001-86-9; sialidase, 9001-67-6; tunicamycin, 11089-65-9 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a HYBRD 
100 1 |a Annibali, N.V. 
245 1 0 |a Characterization of the ETSA-21 antigen, a glycosylphosphatidyl-inositol anchor glycoprotein identified in breast cancer cells using monoclonal antibody B21 
260 |b Mary Ann Liebert Inc.  |c 1997 
270 1 0 |m Baldi, A.; Inst. of Biol./Experimental Medicine, Obligado 2490, 1428 Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
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520 3 |a Mab B21 is a monoclonal antibody (Mab) that recognizes an epithelial tumor surface antigen (ETSA-B21) from diverse human tumor cell lines including breast, ovary, uterus, and their cognate carcinoma tissues. A lower reactivity has been observed in normal breast tissue and benign hyperplesia. In this study, the characteristics of the ETSA-B21 antigen have been examined in greater detail in the MCF-7, SK-BR-3, and MDA-MB-453 breast cancer cell lines. Treatment with phosphatidylinositol-phospholipase C, but no neuraminidase were found to partially remove the ETSA-B21 signal from the cell surface as revealed by immunofluorescence microscopy. Inhibition of the N-glycosylation pathway by tunicamycin resulted in a decreased ETSA-B21 signal on the cell membrane. In addition, the antigen-antibody complex was internalized in breast cancer cells as demonstrated by an acidic wash internalization assay evaluated using immunofluorescence. In conclusion, this study suggests that ETSA-B21 is a GPI anchor N-glycosylated protein promoting specific antibody internalization in breast cancer cells.  |l eng 
593 |a Institute of Biology and Experimental Medicine, National Research Council of Argentina, Obligado 2490, 1428 Buenos Aires, Argentina 
593 |a Institute of Biology and Experimental Medicine, Obligado 2490, 1428 Buenos Aires, Argentina 
690 1 0 |a GLYCOPROTEIN 
690 1 0 |a GLYCOSYLPHOSPHATIDYLINOSITOL 
690 1 0 |a MEMBRANE ANTIGEN 
690 1 0 |a MONOCLONAL ANTIBODY 
690 1 0 |a PHOSPHATIDYLINOSITOL 
690 1 0 |a PHOSPHOLIPASE C 
690 1 0 |a SIALIDASE 
690 1 0 |a TUMOR ANTIGEN 
690 1 0 |a TUNICAMYCIN 
690 1 0 |a ANTIGEN ANTIBODY COMPLEX 
690 1 0 |a ANTIGEN DETECTION 
690 1 0 |a ANTIGEN EXPRESSION 
690 1 0 |a ARTICLE 
690 1 0 |a BREAST CANCER 
690 1 0 |a CANCER CELL CULTURE 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a HUMAN 
690 1 0 |a HUMAN CELL 
690 1 0 |a IMMUNOFLUORESCENCE MICROSCOPY 
690 1 0 |a INTERNALIZATION 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN GLYCOSYLATION 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a MINK CELL FOCUS-FORMING VIRUS 
651 4 |a BREAST HYPERPLASIA 
700 1 |a Baldi, A. 
773 0 |d Mary Ann Liebert Inc., 1997  |g v. 16  |h pp. 139-145  |k n. 2  |p HYBRIDOMA  |x 0272457X  |t Hybridoma 
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