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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Mary Ann Liebert Inc.
1997
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 10697caa a22010337a 4500 | ||
|---|---|---|---|
| 001 | PAPER-20127 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518205131.0 | ||
| 008 | 190411s1997 xx ||||fo|||| 00| 0 eng|d | ||
| 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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| 856 | 4 | 0 | |u https://doi.org/10.1089/hyb.1997.16.139 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_0272457X_v16_n2_p139_Annibali |y Handle |
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