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  • 1
    Electronic Resource
    Electronic Resource
    Carbohydrate Recognition on MUC1-Expressing Targets Enhances Cytotoxicity of a T Cell Subpopulation (1997)
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 46 (1997), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The influence of the epithelial mucin MUC1 on T cell-mediated lysis was analysed using lymph node lymphocytes (LNL) from patients with colorectal carcinoma. LNL were stimulated with allogeneic, MUC1-transfected B cells and the bulk cultures were cloned. Alloreactive cytotoxic T cell clones were obtained which preferentially lysed MUC1-expressing targets. The majority was CD4+ and MHC-class II-restricted, and a minor group was CD8+ and MHC-class I-restricted. All the clones expressed CD3 and TCRαβ, and were CD56−. The capacity to preferentially kill MUC1-expressing targets was stable in several clones for up to 6 months in culture. The enhancing effect of MUC1 on the lysis was investigated in more detail. It was only seen after inhibition of O-linked glycosylation in the targets. Furthermore, this effect was completely abrogated by the monoclonal antibody 3C9, directed against the Thomsen–Friedenreich antigen (T-antigen, Galβ1–3GalNAc bound α1–3 to Ser/Thr) as well as by the soluble disaccharide Galβ1–3GalNAc, but not by other similar disaccharides. The authors conclude that in their system the preferential killing of MUC1-expressing targets is due to the recognition of an internal carbohydrate epitope accessible on underglycosylated MUC1, possibly T-antigen, by an auxiliary receptor molecule on T cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-91.x
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  • 2
    Electronic Resource
    Electronic Resource
    Preface to the symposium in writing on therapeutic cancer vaccines (1996)
    Springer
    Cancer immunology immunotherapy 43 (1996), S. 125-125 
    Details
    ISSN: 1432-0851
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002620050312
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    A survivor of breast cancer with immunity to MUC-1 mucin, and lactational mastitis (1997)
    Springer
    Cancer immunology immunotherapy 43 (1997), S. 355-360 
    Details
    ISSN: 1432-0851
    Keywords: Key words Immunization ; Carcinoma ; Lymphocyte ; Glycosylation ; Tumor antigen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The human mucin, MUC-1, is a transmembrane glycoprotein that is produced by both normal an malignant epithelium. The MUC-1 produced by malignant epithelium is underglycosylated, which leads to the expression by tumors of novel T and B cell epitopes on the mucin polypeptide core. Similar underglycosylation occurs in the lactating breast. In this report, we describe a long-term survivor of breast cancer whose tumor strongly expressed the T- and B-cell-stimulatory epitopes. Five years after presenting with the tumor, the patient had her first pregnancy, at which time she developed fulminant lymphocytic mastitis. We demonstrate that the lactating breast produced mucin expressing the same “tumor-specific” epitopes as the original cancer. The patient had circulating anti-mucin antibodies of both the IgM and IgG isotypes (these are not found in normal controls), and mucin-specific cytotoxic T lymphocytes in the peripheral blood. Limiting  –  dilution analysis for mucin  –  specific cytotoxic T lymphocytes in three different experiments yielded frequencies of 1 in 3086, 1 in 673, and 1 in 583, compared to approximately 1 in 106 in normal controls. The patient remains clinically free of carcinoma after 5 additional years of follow-up. We propose that the original tumor primed the patient’s immune response against the mucin epitopes, and that the re-expression of these epitopes on the lactating breast evoked a secondary immune response. It is tempting to speculate that the vigor of her anti-mucin immunity may have helped protect this patient against recurrent tumor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002620050344
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  • 4
    Electronic Resource
    Electronic Resource
    Differential glycosylation of MUC1 in tumors and transfected epithelial and lymphoblastoid cell lines (1997)
    Springer
    Glycoconjugate journal 14 (1997), S. 89-96 
    Details
    ISSN: 1573-4986
    Keywords: MUC1 ; mucin-like protein ; O-linked glycosylation ; apical targeting in epithelial cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The membrane-bound mucin-like protein MUC1 with a specified number of tandem repeats has been expressed by transfection of the cDNAs in both the epithelial cell lines MDCK and LLC-PK1, and human lymphoblastoid cell lines T2 and C1R. The structure and glycosylation states of the MUC1 in these four lines were compared with that of the endogenous MUC1 found in the human pancreatic (HPAF) and breast (BT-20) tumor cell lines using flow cytometry and Western blot analysis with anti-MUC1 antibodies, which are either sensitive or insensitive to the glycosylation state of the tandem repeat, and pretreatment of cells with phenyl-α-galactosaminide, an inhibitor of mucin sialylation. A similar analysis of MUC1 expression in transfected normal and O-glycosylation defective CHO cells reveals that the addition of galactose to the core oligosaccharide structure is apparently responsible for the anomalous difference in Mr between the mature and propeptide forms of the MUC1. Both the tumor cells and the transfected lymphoblastoid cells consistently express significant steady state levels of both the heavily glycosylated mature forms and the poorly glycosylated propeptide forms of the MUC1, whereas MUC1 is found predominantly as the mature extensively glycosylated species in the transfected epithelial cells. Immunofluoresence microscopy of cross sections of the polarized epithelial cells grown on culture filter inserts reveals that the MUC1 is clearly present at the apical surface of the cells, consistent with its expression in normal tissues. Thus, the successful expression of the MUC1 by transfection of either lymphoblastoid cells or epithelial cells yields model systems both for studying the natural structure/function relationships of the protein domains within the MUC1 molecule and for further elucidating the previously reported MHC-independent T-cell recognition of the MUC1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018569100438
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  • 5
    Electronic Resource
    Electronic Resource
    Differential expression of MUC1 on transfected cell lines influences its recognition by MUC1 specific T cells (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 749-756 
    Details
    ISSN: 1573-4986
    Keywords: MUC1 ; MHC-unrestricted ; tandem repeats ; tumour immunotherapy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In adenocarcinomas of the breast and pancreas, underglycosylation of the glycoprotein MUC1, also expressed by normal breast and pancreatic ductal epithelial cells, results in new protein epitopes to which the immune system mounts a cytotoxic T cell response. This cytotoxic immune response is directed primarily against epitopes on the tandem repeat domain of MUC1, and is unconventional in that it is major histocompatibility complex (MHC)-unrestricted. It is therefore necessary to investigate the molecular basis of this immune response in order to enhance and optimize it for immune therapy purposes. In the present study, we characterize new MUC1 transfected human lymphoblastoid cell lines C1R and T2, and a pig kidney epithelial line LLC-PK1, that express MUC1 with either two repeats (MUC1–2R) or 22 repeats (MUC1–22R), and use them as stimulators and targets for cytotoxic T cells (CTL)in vitro. We show that MUC1–2R is processed and glycosylated similarly to MUC1–22R. In contrast to MUC1–22R, MUC1–2R is not recognized by CTL on T2 and C1R cells known for no or low MHC class I expression. It is however recognized when expressed at high density on xenogeneic LLC-PK1 cells. We propose that in MHC-unrestricted recognition, a large number of MUC1 epitopes is necessary to effectively engage the T cell receptor, and that in the presence of a low number of epitopes, engagement of the CD8 co-receptor by MHC class I molecules may be required for completing the signal through the T cell receptor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00702339
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