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Abstract:

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.

Registro:

Documento: Artículo
Título:Characterization of the ETSA-21 antigen, a glycosylphosphatidyl-inositol anchor glycoprotein identified in breast cancer cells using monoclonal antibody B21
Autor:Annibali, N.V.; Baldi, A.
Filiación:Institute of Biology and Experimental Medicine, National Research Council of Argentina, Obligado 2490, 1428 Buenos Aires, Argentina
Institute of Biology and Experimental Medicine, Obligado 2490, 1428 Buenos Aires, Argentina
Palabras clave:glycoprotein; glycosylphosphatidylinositol; membrane antigen; monoclonal antibody; phosphatidylinositol; phospholipase C; sialidase; tumor antigen; tunicamycin; antigen antibody complex; antigen detection; antigen expression; article; breast cancer; breast hyperplasia; cancer cell culture; controlled study; human; human cell; immunofluorescence microscopy; internalization; priority journal; protein glycosylation; signal transduction; Mink cell focus-forming virus
Año:1997
Volumen:16
Número:2
Página de inicio:139
Página de fin:145
DOI: http://dx.doi.org/10.1089/hyb.1997.16.139
Título revista:Hybridoma
Título revista abreviado:HYBRIDOMA
ISSN:0272457X
CODEN:HYBRD
CAS:phospholipase C, 9001-86-9; sialidase, 9001-67-6; tunicamycin, 11089-65-9
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0272457X_v16_n2_p139_Annibali

Referencias:

  • Annibali, N.V., San Martino, J.A., Baldi, A., Monoclonal antibodies against human breast tumor-associated antigens: Characterization of B21 antigen (1994) J Natl Cancer Inst, 86, pp. 215-221
  • Low, M.G., Saltiel, A.R., Structural and functional roles of glycosylphosphatidylinositol in membranes (1988) Science, 239, pp. 268-275
  • Fenton, R.G., Longo, D.L., Genetic instability and tumor cell vari-ation: Implications for immunolherapy (1995) J Natl Cancer Inst, 87, pp. 241-243
  • Steplewski, Z., Advocates and outlooks for immunotherapy of cancer (1993) Hybridoma, 12, pp. 493-497
  • Sullivan, C.O., Price, M.R., Baldwin, R.W., Polymorphic epithelial mucin from the sera of advanced breast cancer patients - Isolation and parcial characterisation (1990) Br J Cancer, 61, pp. 801-808
  • Chang, K., Pai, L.H., Batra, J.K., Pastan, I., Willingham, M.C., Characterization of the antigen (CAK1) recognized by monoclonal antibody K1 present on ovarian cancer and normal mesothelium (1992) Cancer Res, 52, pp. 181-186
  • Denine, P.L., Clark, B.A., Birrell, G.W., Layton, G.T., Ward, B.G., Alewood, P.F., McKenzie, I.F.C., The breast tumor-associated epitope defined by monoclonal antibody 3E1.2 Ia an O-linked mucin carbohydrate containing N-glycolylneuraminic acid (1991) Cancer Res, 51, pp. 5826-5836
  • Singh, N., Tartakoff, A.M., Two different mutants in synthesis of dolichol-phosphoryl-mannose do not add glycophospholipid anchors to membrane proteins: Quantitative correction of the phenotype of a CHO cell mutant with tunicamycin (1991) Mol Cell Biol, 11, pp. 391-1100
  • Bharathan, S., Moriarty, J., Moody, C.E., Sherblom, A.P., Effect of tunicamycin on sialomucin and natural killer susceptibility of rat mammary tumor ascites cells (1990) Cancer Res, 50, pp. 5250-5256
  • Brunk, C.F., Jones, C.J., James, W.T., Assay for nanogram quantitaties of DNA in cellular homogenates (1979) Anal Biochem, 92, pp. 497-500
  • Fernstein, P.D., Primus, F.J., Greiner, J.W., Simpson, J.F., Schlom, J., Characterization of the colorectal carcinoma-associated antigen defined by monoclonal antibody D612 (1991) Cancer Res, 51, pp. 926-934
  • Aboud-Pirak, E., Sergent, T., Slachmuylder, C., Binding and endocytosis of a monoclonal antibody to a high molecular weight human milk fat globule membrane-associated antigen by cultured MCF-7 breast carcinoma cells (1988) Cancer Res, 48, pp. 3188-3193
  • Della Torre, G., Colnaghi, M.I., Internalization of a monoclonal antibody against human breast cancer by immunoelectron microscopy (1987) Br J Cancer, 55, pp. 357-360
  • Elbein, A.D., Inhibitors of the biosynthesis and processing of N-linked oligosaccharide chains (1987) Annu Rev Biochem, 56, pp. 497-534
  • Hilkens, J., Ligtenberg, M.J.L., Vos, H.L., Litvinov, S.V., Cell membrane-associated mucins and their adhesion-modulating property (1992) Trends Biochem Sci, 17, pp. 359-363
  • Alemany, R., Vilá, M.R., Franci, C., Egea, G., Real, F.X., Glycosyl phosphatidylinositol membrane anchoring of melanotransferrin (p97): Apical compartmentalization in intestinal epithelial cells (1993) J Cell Sci, 104, pp. 1155-1162
  • Lisanti, M.P., Caras, I.W., Gilbert, T., Hanzel, D., Rodriguez-Boulan, E., Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells (1990) Proc Natl Acad Sci USA, 87, pp. 7419-7423
  • Devine, P.L., Mucins: Structure, function and associations with malignancy (1992) BioEssay, 14, pp. 619-625
  • Vega-Salas, D.E., San Martino, J.A., Salas, P.I., Baldi, A., Vacuolar apical compartment (VAC) in breast carcinoma cell lines (MCF-7 and T47D): Failure of the cell-cell regulated exocytosis mechanism of apical membrane (1993) Differentiation, 54, pp. 131-141
  • Gouin, E., Ouary, M., Pogu, S., Sai, P., Release of carcinoembryonic antigen from human tumor cells by phosphatidylinositol-specific phospholipase C: Highly effective extraction and upregulation from LS-174T colonic adenocarcinoma cells (1993) Arch Biochem Biophys, 306, pp. 125-132
  • Berridge, M.J., Inositol trisphosphate and calcium signalling (1993) Nature, 361, pp. 315-325
  • Xia, M.Q., Hale, G., Lifely, R.M., Ferguson, M.A.J., Campbell, D., Packman, L., Waldmann, H., Structure of the CAMPATH-1 antigen. a glycosylphosphatidylinositol-anchored glycoprotein which is an exceptionally good target for complement lysis (1993) Biochem J, 293, pp. 633-640
  • Tartakoff, A.M., Singh, N., How to make a glycoinositol phospholipid anchor (1992) Trends Biochem Sci, 17, pp. 470-473
  • De Camilli, P., Emr, S.D., McPherson, P.S., Novick, P., Phosphoinositides as regulators in membrane traffic (1996) Science, 271, pp. 1533-1538
  • Kodukula, K., Cines, D., Amthauer, R., Gerber, L., Udenfriend, S., Biosynthesis of Phosphatidylinositol-Glycan (PI-G)-anchored membrane proteins in cell-free systems: Cleavage of the nascent protein and addition of the PI-G moiety depend on the size of the COOH-terminal signal peptide (1992) Proc Natl Acad Sci USA, 89, pp. 1350-1353
  • Thomas, G.M.H., Cunningham, E., Fensome, A., Ball, A., Totty, N.F., Truong, O., Hsuan, J.J., Cockcroft, S., An essential role for phosphtaidylinositol transfer protein in phospholipase C-mediated inositol lipid signaling (1993) Cell, 74, pp. 919-926
  • Griffiths, G., Back, R., Marsh, M., A quantitative analysis of the endocytic pathway in baby hamster kidney cells (1989) J Cell Biol, 109, pp. 2703-2720
  • Schmid, S.L., The mechanism of receptor-mediated endocytosis: More questions than answers (1995) BioEssays, 14, pp. 589-596
  • Mayor, S., Presley, J.F., Maxfield, F.R., Sorting of membrane components from endosomes and subsequent recycling to the cell Surface occurs by a bulk flow process (1993) J Cell Biol, 121, pp. 1257-1269
  • Shyng, S.L., Heuser, J.E., Harris, D.A., A glycolipid-anchored prion protein is endocytosed via clathrin-coated pits (1994) J Cell Biol, 125, pp. 1239-1250
  • Keller, G.A., Siegel, M.W., Caras, I.W., Endocytosis of glycophospholipid-anchored and transmembrane forms of CD4 by different endocytotic pathways (1995) EMBO J, 11, pp. 863-874
  • Mayor, S., Rothberg, K.G., Maxfield, F.R., Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking (1994) Science, 264, pp. 1948-1951
  • Pastan, I., Willinham, M.C., FitzGerald, D.J.P., Immunotoxins (1986) Cell, 47, pp. 641-648
  • Thrush, G.R., Lark, L.R., Clinchy, B.C., Vitetta, E.S., Immunotoxins: An update (1996) Annu Rev Immunol, 14, pp. 49-71

Citas:

---------- APA ----------
Annibali, N.V. & Baldi, A. (1997) . Characterization of the ETSA-21 antigen, a glycosylphosphatidyl-inositol anchor glycoprotein identified in breast cancer cells using monoclonal antibody B21. Hybridoma, 16(2), 139-145.
http://dx.doi.org/10.1089/hyb.1997.16.139
---------- CHICAGO ----------
Annibali, N.V., Baldi, A. "Characterization of the ETSA-21 antigen, a glycosylphosphatidyl-inositol anchor glycoprotein identified in breast cancer cells using monoclonal antibody B21" . Hybridoma 16, no. 2 (1997) : 139-145.
http://dx.doi.org/10.1089/hyb.1997.16.139
---------- MLA ----------
Annibali, N.V., Baldi, A. "Characterization of the ETSA-21 antigen, a glycosylphosphatidyl-inositol anchor glycoprotein identified in breast cancer cells using monoclonal antibody B21" . Hybridoma, vol. 16, no. 2, 1997, pp. 139-145.
http://dx.doi.org/10.1089/hyb.1997.16.139
---------- VANCOUVER ----------
Annibali, N.V., Baldi, A. Characterization of the ETSA-21 antigen, a glycosylphosphatidyl-inositol anchor glycoprotein identified in breast cancer cells using monoclonal antibody B21. HYBRIDOMA. 1997;16(2):139-145.
http://dx.doi.org/10.1089/hyb.1997.16.139