26 results on '"Taylor-Papadimitriou, J"'
Search Results
2. Reactions of Monoclonal Antibodies against Human Milk Fat Globule Membranes with Embryonal Tissue
- Author
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KOLDOVSKY, U., primary, WARGALLA, U., additional, HILKENS, J., additional, TAYLOR-PAPADIMITRIOU, J., additional, HAGEMANN, PH., additional, and HILGERS, J., additional
- Published
- 1984
- Full Text
- View/download PDF
3. Synergism of Toll-like receptor-induced interleukin-12p70 secretion by monocyte-derived dendritic cells is mediated through p38 MAPK and lowers the threshold of T-helper cell type 1 responses.
- Author
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Bohnenkamp HR, Papazisis KT, Burchell JM, and Taylor-Papadimitriou J
- Subjects
- CD8-Positive T-Lymphocytes immunology, Cell Differentiation, Dendritic Cells cytology, Dendritic Cells drug effects, Flagellin pharmacology, Humans, Immunity, Innate immunology, Immunologic Memory immunology, Kinetics, Ligands, Lipopolysaccharides pharmacology, Peptidoglycan pharmacology, Poly I-C pharmacology, Zymosan pharmacology, Dendritic Cells metabolism, Interleukin-12 metabolism, T-Lymphocytes, Helper-Inducer metabolism, Toll-Like Receptors metabolism, p38 Mitogen-Activated Protein Kinases metabolism
- Abstract
Toll-like receptors (TLRs) recognise specific molecular signatures of pathogens and trigger antimicrobial defence responses. Thereby, two independent signalling pathways can be distinguished: The inflammatory signalling pathway acting via the adapter molecule MyD88, leading to the activation of nuclear factor-kappaB (NF-kappaB) and mitogen activated protein kinases (MAPK) such as SAPK/JNK and p38 MAPK and the interferon (IFN) dependent pathway that signals via TRIF and results in the production of IFN-alpha/beta. Several evolutionarily conserved molecular patterns are expressed by pathogens, leading to the question if concerted targeting of different TLRs may induce exaggerated immune responses by signalling via both TLR pathways. Here we report that monocyte-derived dendritic cells (MoDCs) combine and integrate signals received via the IFN-dependent pathway by engagement of TLR3 (poly I:C) and activation of TRIF with the MyD88-dependent pathway by ligation of TLR2 (PGN), TLR2/TLR6 (zymosan) and TLR5 (flagellin). The generally low IL-12p70 inducers resulted in combination of both pathways in cytokine levels similar to LPS, which acts via TLR4 and induces recruitment of MyD88/Tirap and TRIF/TRAM adapter proteins. The combination of TLR3 (poly I:C) or TLR4 (LPS) engagement with TLR8 (R848) ligation induced synergistic effects on cytokine production with a boost especially in IL-12p70 secretion. SB203580, a specific p38 MAPK inhibitor, completely blocked TLR ligand mediated IL-12p70 secretion, whereby specific inhibitors for SAPK/JNK (SP600125) and NF-kappaB (PDTC) only repressed partially the IL-12p70 secretion. Enhanced phosphorylation in poly I:C and R848 activated MoDCs revealed the critical contribution of p38 MAPK in synergistically induced IL-12p70 induction. Further investigation of primary and recall CD8+ T cell responses to the MUC(12-20) M1.2 peptide LLLLTVLTV and the influenza A virus matrix(58-66) peptide GILGFVFTL proved that synergistically activated MoDCs were superior compared with LPS or R848 alone. The results indicate that dendritic cells process, combine and integrate signals delivered by pathogens to launch effective adaptive immune responses.
- Published
- 2007
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- View/download PDF
4. Apoptosis of monocytes and the influence on yield of monocyte-derived dendritic cells.
- Author
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Bohnenkamp HR, Burchell JM, Taylor-Papadimitriou J, and Noll T
- Subjects
- Annexin A5 analysis, Cancer Vaccines immunology, Cancer Vaccines therapeutic use, Cell Differentiation drug effects, Cell Separation, Cells, Cultured, Cytokines pharmacology, Dendritic Cells cytology, Dendritic Cells transplantation, Dinoprostone pharmacology, Histocompatibility Antigens Class I immunology, Humans, Immunotherapy, Adoptive, Lymphocyte Activation drug effects, Lymphocyte Activation immunology, Monocytes cytology, Neoplasms immunology, Neoplasms therapy, Oxytocics pharmacology, Phagocytosis drug effects, Phagocytosis immunology, Phenotype, Propidium chemistry, T-Lymphocytes immunology, Apoptosis, Cell Differentiation immunology, Dendritic Cells immunology, Lipopolysaccharide Receptors immunology, Monocytes immunology
- Abstract
Monocyte-derived dendritic cells (DC) are currently under extensive evaluation as cell vaccines for cancer treatment. The requirement for large-scale cell products demands optimized and standardized protocols. However, the yield of DCs from inoculated monocytes is reported to be always lower than 50%. In this present study we investigated whether this cell loss was caused by the properties of the starting population of inoculated monocytes. CD14 cells were enriched by immunomagnetic-bead selection and analyzed for apoptosis by an annexin V/propidium iodide assay. We found that 37.8+/-11.1% (n=8) of freshly isolated monocytes from buffy coats of healthy donors underwent programmed cell death. Further analysis of the fate of apoptotic cells during differentiation suggested phagocytosis. Monocytes were differentiated with GM-CSF and interleukin-4 into a viable, non-apoptotic population of immature dendritic cells. Addition of tumor necrosis factor-alpha and prostaglandin E2 resulted in fully matured dendritic cells, which were evaluated by phenotypic analysis and by allogeneic and MHC class-I-restricted T-cell responses. About 90.2+/-16.7% of the non-apoptotic monocyte population differentiated to viable matured dendritic cells. These results indicate that the yield of dendritic cells is mainly influenced by the percentage of apoptotic cells in the inoculum, and this has implications for DC generation in clinical applications.
- Published
- 2004
- Full Text
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5. Breast carcinoma cell lysate-pulsed dendritic cells cross-prime MUC1-specific CD8+ T cells identified by peptide-MHC-class-I tetramers.
- Author
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Bohnenkamp HR, Coleman J, Burchell JM, Taylor-Papadimitriou J, and Noll T
- Subjects
- Adjuvants, Immunologic pharmacology, CD8-Positive T-Lymphocytes metabolism, Cell Differentiation drug effects, Cell Line, Tumor, Cell Movement, Cell Proliferation, Cytokines metabolism, Dendritic Cells cytology, Dendritic Cells drug effects, Dendritic Cells metabolism, Dinoprostone metabolism, Dinoprostone pharmacology, Endocytosis, Gene Expression Regulation, Neoplastic, Histocompatibility Antigens Class I chemistry, Histocompatibility Antigens Class I metabolism, Humans, Receptors, Chemokine metabolism, T-Lymphocytes, Helper-Inducer immunology, T-Lymphocytes, Helper-Inducer metabolism, Breast Neoplasms immunology, Breast Neoplasms pathology, CD8-Positive T-Lymphocytes immunology, Cell Extracts immunology, Dendritic Cells immunology, Histocompatibility Antigens Class I immunology, Mucin-1 immunology
- Abstract
For cancer immunotherapy the loading of dendritic cells (DCs) with whole tumor cell lysate preparations represents a simple and promising approach for presentation of tumor-associated antigens (TAAs), avoiding the disadvantages of HLA-matching and definition of TAAs. The aim of this study was to investigate whether lysate-pulsed DCs efficiently cross-prime CD8+ T cells and induce a strong T(H)1 cell response, as compared to DCs pulsed with specific peptides (FLU M1 and Melan-A/Mart-1). As a model system breast carcinoma cell lysate from either MCF-7 or MDA-MB-231 cell lines (both HLA-A*0201+) expressing the TAA MUC1 were selected. Both cell lines expressed MUC1, the epithelial mucin, which is a large molecular weight O-glycosylated protein expressed in the majority of breast, ovarian, and other epithelial malignancies and is under evaluation as a target antigen in cancer immunotherapy. We developed a simple lysate preparation method to solubilize all cell proteins without degradation. For loading of monocyte-derived dendritic cells, 100 microgmL(-1) of breast carcinoma cell lysate was used, accompanied by an adjuvant consisting of tumor necrosis factor-alpha (TNF-alpha) and prostaglandin-E2. T cells were co-cultivated with lysate or peptide pulsed DCs and were restimulated weekly. Before cultivation, and after the 3rd stimulation, tetramer frequencies for the MUC1 epitopes M1.2 and F7 as well as for the FLU M1 and Melan-A/Mart-1 epitopes were determined. After stimulation with lysate, higher frequencies for M1.2-specific T cells were observed compared with the F7 epitope. Furthermore, we found expansion factors for M1.2-specific T cells that had been stimulated with MCF-7 lysate-pulsed DCs of up to 43-fold. The analysis of typical T(H)1/T(H)2 cytokines (IFN-gamma, TNF-alpha, IL-12p70, IL-2, IL-4, IL-5, and IL-10) revealed a strong T(H)1 response. These results provide evidence for a strong T(H)1 polarization and cross-priming of MUC1-specific CD8+ T cells and demonstrate the feasibility of using lysate-pulsed dendritic cells in breast cancer immunotherapy.
- Published
- 2004
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6. Characterisation and developmental expression of mouse Plu-1, a homologue of a human nuclear protein (PLU-1) which is specifically up-regulated in breast cancer.
- Author
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Madsen B, Spencer-Dene B, Poulsom R, Hall D, Lu PJ, Scott K, Shaw AT, Burchell JM, Freemont P, and Taylor-Papadimitriou J
- Subjects
- Animals, Cell Differentiation physiology, DNA-Binding Proteins metabolism, Forkhead Transcription Factors, Gene Expression Regulation, Developmental, Gene Expression Regulation, Neoplastic, Humans, Immunoblotting, Jumonji Domain-Containing Histone Demethylases, Mammary Glands, Animal embryology, Mice embryology, Mice, Knockout, Molecular Sequence Data, Neoplasm Proteins metabolism, Nerve Tissue Proteins metabolism, Nuclear Proteins, PAX9 Transcription Factor, Repressor Proteins, Telencephalon embryology, Telencephalon metabolism, Tooth embryology, Transcription Factors genetics, Transcription Factors metabolism, DNA-Binding Proteins genetics, Mammary Glands, Animal metabolism, Mammary Neoplasms, Animal metabolism, Neoplasm Proteins genetics
- Abstract
PLU-1 is a novel breast cancer associated nuclear protein containing highly conserved domains including the PLU domain, putative DNA/chromatin binding motifs, and PHD/LAP domains. Here we report the cloning of the mouse homologue (Plu-1), and document its expression in adult tissues, mammary tumours and the embryo. The overall homology with human PLU-1 is 94% at the protein level, with almost 100% identity in the conserved domains, suggesting functional conservation. As with human PLU-1 the expression of Plu-1 in adult tissues is restricted, with high expression being seen only in testis, while expression in mammary tumours from c-neu transgenic mice is high. Plu-1 is also differentially expressed in the adult mammary gland. In the developing embryo Plu-1 is expressed in a temporally restricted fashion with tissue specific expression being limited to parts of the developing brain, whisker follicle, mammary bud, thymus, limbs, intervertebral disc, olfactory epithelium, teeth, eye, and stomach. The temporal and spatial expression patterns of the transcription factors Bf-1 and Pax9, recently found to bind to PLU-1 through the PLU domain overlap with Plu-1 expression during development. Thus Plu-1 appears to play an important role in mouse embryonic development which may involve interaction with Pax9 and Bf-1.
- Published
- 2002
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7. Crystal structure at 1.95 A resolution of the breast tumour-specific antibody SM3 complexed with its peptide epitope reveals novel hypervariable loop recognition.
- Author
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Dokurno P, Bates PA, Band HA, Stewart LM, Lally JM, Burchell JM, Taylor-Papadimitriou J, Snary D, Sternberg MJ, and Freemont PS
- Subjects
- Amino Acid Sequence, Antigen-Antibody Reactions, Models, Molecular, Antibodies, Neoplasm chemistry, Breast Neoplasms immunology, Epitopes chemistry, Immunoglobulin Fab Fragments chemistry, Mucins chemistry, Peptides chemistry
- Abstract
The anti-breast tumour antibody SM3 has a high selectivity in reacting specifically with carcinoma-associated mucin. SM3 recognises the core repeating motif (Pro-Asp-Thr-Arg-Pro) of aberrantly glycosylated epithelial mucin MUC1, and has potential as a therapeutic and diagnostic tool. Here we report the crystal structure of the Fab fragment of SM3 in complex with a 13-residue MUC1 peptide antigen (Thr1P-Ser2P-Ala3P-Pro4P-Asp5P-Thr6P -Arg7P-Pro8P-Ala9P-Pro10P-Gly11P- Ser12P-Thr13P). The SM3-MUC1 peptide structure was solved by molecular replacement, and the current model is refined at 1.95 A resolution with an R-factor of 21.3% and R-free 28.3%. The MUC1 peptide is bound both by non-polar interactions and hydrogen bonds in an elongated groove in the antibody-combining site through interactions with Complimentarity Determining Regions (CDRs), three of the light chain (L1, L2, L3) and two of the heavy chain (H1 and H3). The conformation of the peptide is mainly extended with no discernable standard secondary structure. There is a single non-proline cis-peptide bond in H3 (Val95H-Gly96H-Gln97H-Phe98H-Ala101H-Ty r102H) between Gly96H and Gln97H, which appears to play a role in SM3-peptide antigen interactions, and represents the first such example within an antibody hypervariable loop. The SM3-MUC1 peptide structure has implications for rational therapeutic and diagnostic antibody engineering., (Copyright 1998 Academic Press)
- Published
- 1998
- Full Text
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8. Breast cancer: have we lost our way?
- Author
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Taylor-Papadimitriou J
- Subjects
- Female, Humans, Breast Neoplasms therapy
- Published
- 1993
9. The product of the human MUC1 gene when secreted by mouse cells transfected with the full-length cDNA lacks the cytoplasmic tail.
- Author
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Boshell M, Lalani EN, Pemberton L, Burchell J, Gendler S, and Taylor-Papadimitriou J
- Subjects
- Animals, Cloning, Molecular, DNA, Single-Stranded genetics, Epithelial Cells, Mammary Neoplasms, Experimental, Membrane Glycoproteins genetics, Membrane Glycoproteins immunology, Mice, Mucin-1, Mucins genetics, Mucins immunology, Protein Conformation, Protein Processing, Post-Translational, RNA Splicing, Recombinant Proteins biosynthesis, Tumor Cells, Cultured, Membrane Glycoproteins metabolism, Mucins metabolism, Transfection
- Abstract
The polymorphic epithelial mucin (PEM) is found as a cell associated transmembrane protein with an extracellular domain made up largely of tandem repeats and also as a soluble form in some body fluids and culture supernatants. To determine whether the soluble form can arise without the mechanism of alternative splicing mouse cells have been transfected with an expression construct containing the full-length cDNA, and the supernatants of the transfectants analyzed for the presence of the mucin. The presence of mucin in the supernatants could indeed be detected in a radioimmunoassay and by immunoprecipitation using monoclonal antibodies to the tandem repeat region of the core protein, indicating that release of the soluble form can occur without alternative splicing. The soluble form was not however precipitated with a polyclonal antiserum to the cytoplasmic tail, suggesting that it was released from the membrane by the action of a protease.
- Published
- 1992
- Full Text
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10. Antibodies to the cytoplasmic domain of the MUC1 mucin show conservation throughout mammals.
- Author
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Pemberton L, Taylor-Papadimitriou J, and Gendler SJ
- Subjects
- Amino Acid Sequence, Animals, Antibody Formation, Mammals genetics, Mice genetics, Mice immunology, Molecular Sequence Data, Mucins genetics, Peptide Fragments genetics, Protein Conformation, Species Specificity, Tissue Distribution, Biological Evolution, Mammals immunology, Mucins immunology, Peptide Fragments immunology
- Abstract
An antiserum against the carboxy-terminal seventeen amino acids of the human MUC1 mucin has been raised and extensively characterized. This antiserum, CT1, immunoprecipitates two high molecular weight polymorphic bands (greater than 200 kDa) from a metabolically labelled breast cancer cell line corresponding to the two alleles which have previously been shown to contain different numbers of a twenty amino acid repeat. The CT1 antiserum reacted with tissues from many mammalian species and immunoprecipitated large polymorphic proteins, suggesting that the cytoplasmic portion of the molecule is well conserved. The cell and tissue distribution of Muc-1 mucin in the mouse has been studied by immunocytochemistry. This protein is abundant at the apical surfaces of epithelial tissues and is found expressed in the stomach, kidney, mammary gland, pancreas, salivary gland, lung, trachea, uterus, cervix and vagina.
- Published
- 1992
- Full Text
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11. Structure and expression of the human polymorphic epithelial mucin gene: an expressed VNTR unit.
- Author
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Lancaster CA, Peat N, Duhig T, Wilson D, Taylor-Papadimitriou J, and Gendler SJ
- Subjects
- Amino Acid Sequence, Base Sequence, Consensus Sequence, Cosmids, Epithelium metabolism, Exons, Gene Expression, Humans, Introns, Molecular Sequence Data, Mucins biosynthesis, RNA Splicing, RNA, Messenger chemistry, Restriction Mapping, Tumor Cells, Cultured, Mucins genetics, Repetitive Sequences, Nucleic Acid
- Abstract
The human polymorphic epithelial mucin (PEM) is expressed apically by glandular epithelium and by the carcinomas that develop from these tissues. Previously isolated cDNA clones revealed that the core protein contained a large domain consisting of variable numbers of 60 bp tandem repeats (TR), making it an expressed minisatellite. We now report the full genomic sequence of the PEM gene, including 803 bp of 5' flanking sequence. The gene is composed of 7 exons and varies in size from approximately 4 to approximately 7 kb, depending on the number of tandem repeats in exon 2. Expression of PEM was obtained from a genomic clone in an Epstein-Barr virus based vector, after transfection into a human epithelial cell line, indicating the presence of effective regulatory sequences in this clone.
- Published
- 1990
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12. Immunohistochemical analysis of benign and malignant breast tumours.
- Author
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Taylor-Papadimitriou J
- Subjects
- Breast Neoplasms genetics, Breast Neoplasms pathology, Female, Humans, Neoplasm Invasiveness, Breast Neoplasms immunology, Keratins immunology
- Published
- 1990
13. A cytidine specific endonuclease activity associated with purified reovirus virions.
- Author
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Kortsaris A, Georgatsos JG, and Taylor-Papadimitriou J
- Subjects
- Animals, Kinetics, L Cells, Mice, Poly C, Poly I, Substrate Specificity, Endonucleases metabolism, Reoviridae enzymology, Virion enzymology
- Published
- 1980
- Full Text
- View/download PDF
14. Effects of SV40 transformation on the cytoskeleton and behavioural properties of human keratinocytes.
- Author
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Taylor-Papadimitriou J, Purkis P, Lane EB, McKay IA, and Chang SE
- Subjects
- Cell Differentiation, Cell Division drug effects, Cell Line, Growth Substances biosynthesis, Humans, Interferons pharmacology, Keratins metabolism, Male, Simian virus 40, Cell Transformation, Viral, Cytoskeleton ultrastructure, Epithelium ultrastructure, Neoplasms, Experimental ultrastructure
- Abstract
A cloned cell line (SVK14) with apparently unlimited growth potential was isolated from simian virus 40 (SV40)-infected human foreskin keratinocytes which did not appear to pass through any obvious 'crisis' (Girardi et al., J. Cell. Comp. Physiol., 1965, 65, 69-84). Indirect immunofluorescence microscopy showed that the transformed cells have the SV40 large T antigen in their nuclei and stain positively with LE61, a monoclonal antibody that reacts with a tonofilament determinant normally only found in non-keratinizing simple epithelia. SVK14 cells can be grown in the absence of 3T3 feeders and show an impaired ability to differentiate into squames, and this impairment becomes more marked with passage. At later passages the cells acquire the ability to form colonies in agar and to produce a factor with mitogenic activity which stimulates DNA synthesis in quiescent 3T3 cells. Concomitantly, the SVK14 cells become less sensitive to the growth inhibitory effect of human alpha interferons.
- Published
- 1982
- Full Text
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15. Identification of immunoreactive monoclonal antibody fragments for improved immunoscintigraphy.
- Author
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Mather SJ, Durbin H, and Taylor-Papadimitriou J
- Subjects
- Alkaline Phosphatase, Animals, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, GPI-Linked Proteins, Isoenzymes immunology, Mice, Mice, Nude, Neoplasm Proteins immunology, Neoplasms, Experimental immunology, Peptide Hydrolases, Radionuclide Imaging, Antibodies, Monoclonal, Immunoglobulin Fab Fragments isolation & purification, Immunoglobulin G, Neoplasms, Experimental diagnostic imaging
- Abstract
Results obtained in animal models suggest that antibody fragments may have advantages over whole immunoglobulin for in vivo localisation studies. Proteolytic digestion of monoclonal antibodies may however yield a mixture of products unsuitable for in vivo use. This report describes a method whereby the immunoreactive products of antibody digestion can be identified by probing nitrocellulose blots of the gel-separated digest with the specific antigen. Optimum conditions for the production of the reactive fragments can then be determined and once identified they can be purified to homogeneity. Using this method conditions have been defined for the production of F(ab)2 and Fab fragments from a papain digest of an antibody to placental alkaline phosphatase (H17E2). In this case the antigen has enzyme activity which can be used to detect binding to the immunoreactive bands on the Western blots. In vivo experiments in nude mice carrying xenografts of a tumour expressing the H17E2 reactive antigen were performed to determine the efficacy of localisation of the purified fragments as compared to the whole antibody. As expected the absolute levels of radioactivity localised in the tumour was highest using whole antibody, whereas the F(ab)2 fragments produced the highest tumour:blood ratios.
- Published
- 1987
- Full Text
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16. Modulation of phenotype in cultures of human milk epithelial cells and its relation to the expression of a membrane antigen.
- Author
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Chang SE and Taylor-Papadimitriou J
- Subjects
- Antibodies, Monoclonal, Cells, Cultured, Epithelial Cells, Epithelium immunology, Female, Fibronectins metabolism, Humans, Keratins metabolism, Milk, Human immunology, Milk, Human metabolism, Phenotype, Pregnancy, Antigens, Surface, Milk, Human cytology
- Abstract
Primary cultures of human milk epithelial cells, labelled with HMFG-1, a monoclonal antibody that recognises a differentiation antigen on the membranes of breast epithelia, were separated from unlabelled cells in a fluorescence-activated cell sorter (FACS). Cells not expressing the HMFG-1 antigen have a greater in vitro growth potential than the positive ones, and give rise to cultures containing both HMFG-1 antigen positive and negative cells. The cultures derived from negative cells usually contain colonies with 'open' cuboidal cells and these do not express the HMFG-1 antigen. However, when they differentiate into other phenotypes such as the 'closed' cuboidal cell type, expression of the differentiation antigen becomes evident and the cultures then show a reduced growth potential. When milk cells are subcultured several times, a new cell type emerges which does not express the HMFG-1 antigen or the intermediate filaments typical of epithelial cells but instead express high levels of fibronectin which is found in an extracellular matrix. Whether these cells emerge by selection of an existing phenotype or by phenotypic modulation is discussed.
- Published
- 1983
- Full Text
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17. Radioimmunodiagnosis of ovarian cancer using 123I-labelled, tumor-associated monoclonal antibodies.
- Author
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Epenetos AA, Shepherd J, Britton KE, Hawkins L, Nimmon CC, Taylor-Papadimitriou J, Durbin H, Malpas JS, Mather S, and Granowska M
- Subjects
- Adenocarcinoma diagnostic imaging, Animals, Antibodies, Neoplasm immunology, Autoradiography, Disease Models, Animal, Female, Humans, Immunoenzyme Techniques, Immunoglobulin G immunology, Iodine Radioisotopes, Mice, Mice, Nude, Middle Aged, Neoplasm Transplantation, Ovarian Neoplasms diagnostic imaging, Radionuclide Imaging, Adenocarcinoma diagnosis, Antibodies, Monoclonal, Ovarian Neoplasms diagnosis
- Abstract
Monoclonal antibodies to epithelial cells, antigenic determinants labelled with I123 and I125, were administered to 10 immunodeficient mice bearing subcutaneous xenografts of human ovarian cancer. Radio scans of the body taken with a gamma camera at various time intervals demonstrated the presence of the cancer in all the mice. The smallest detectable tumor was approximately 1 mm in diameter. In a subsequent clinical study using 123I-labelled monoclonal antibodies in 10 patients with ovarian cancer, tumor detection was achieved in 8 patients, with tumor uptake of labelled antibody ranging between 0.2-2.6%. As a complementary method to existing forms of diagnosis, the targeting of monoclonal antibodies to ovarian cancer cells in vivo raises the hope of achieving early diagnosis in otherwise undetectable ovarian cancer, and provides encouragement to the concept of selective therapy in oncology.
- Published
- 1984
18. Targeting of iodine-123-labelled tumour-associated monoclonal antibodies to ovarian, breast, and gastrointestinal tumours.
- Author
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Epenetos AA, Britton KE, Mather S, Shepherd J, Granowska M, Taylor-Papadimitriou J, Nimmon CC, Durbin H, Hawkins LR, Malpas JS, and Bodmer WF
- Subjects
- Adenocarcinoma diagnostic imaging, Aged, Antibodies, Neoplasm immunology, Female, Humans, Immunoenzyme Techniques, Immunoglobulin G immunology, Middle Aged, Ovarian Neoplasms secondary, Radionuclide Imaging, Antibodies, Monoclonal immunology, Breast Neoplasms diagnostic imaging, Gastrointestinal Neoplasms diagnostic imaging, Iodine Radioisotopes, Ovarian Neoplasms diagnostic imaging
- Abstract
Two tumour-associated monoclonal antibodies, HMFG1 and HMFG2, were labelled with iodine-123 and used to detect primary and metastatic ovarian, breast, and gastrointestinal neoplasms by external body scintigraphy in twenty patients with advanced disease. Tumours became visible 3 min to 18 h after injection of labelled antibody. The presence of antibody in the tumours was confirmed by autoradiography and immunoperoxidase staining of surgically removed tissues. The mean tumour uptake of radiolabel was 0.6% of the injected amount. These antibodies can therefore localise specifically to tumours and successful imaging can thus be achieved. This method can complement existing diagnostic techniques and also provide a basis for a selective therapeutic approach to malignant disease.
- Published
- 1982
- Full Text
- View/download PDF
19. Monoclonal antibodies to epithelial membrane antigen and human milk fat globule mucin define epitopes expressed on other molecules.
- Author
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Taylor-Papadimitriou J, Burchell J, Moss F, and Beverley P
- Subjects
- Epitopes immunology, Humans, Lipids immunology, Mucin-1, Mucins immunology, Antibodies, Monoclonal immunology, Membrane Proteins immunology, Milk, Human immunology
- Published
- 1985
- Full Text
- View/download PDF
20. Mitochondrial protein synthesis is inhibited by 2'-5' linked oligoadenylic acid triphosphate.
- Author
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Kortsaris A, Karemfillis T, Koliais SI, and Taylor-Papadimitriou J
- Subjects
- Burkitt Lymphoma, Cell Line, Chloramphenicol pharmacology, Cycloheximide pharmacology, Humans, Kinetics, Mitochondria drug effects, Poly U, Protein Biosynthesis drug effects, T-Lymphocytes, Adenine Nucleotides pharmacology, Mitochondria metabolism, Neoplasm Proteins biosynthesis, Oligonucleotides pharmacology, Oligoribonucleotides pharmacology
- Published
- 1980
- Full Text
- View/download PDF
21. Interferon inhibition of DNA synthesis in Swiss 3T3 cells: dissociation from protein kinase C activation.
- Author
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Mehmet H, Morris CM, Taylor-Papadimitriou J, and Rozengurt E
- Subjects
- Animals, Carcinogens pharmacology, Cells, Cultured, Enzyme Activation drug effects, Epidermal Growth Factor pharmacology, Kinetics, Mice, Phorbol 12,13-Dibutyrate, Phorbol Esters pharmacology, Phosphorylation, DNA Replication drug effects, Interferon Type I physiology, Protein Kinase C metabolism
- Abstract
We have examined the role of protein kinase C in the anti-proliferative effects of interferon in Swiss 3T3 cells. Treatment of these cells with interferon did not stimulate the phosphorylation of an acidic Mr 80,000 cellular protein which serves as a substrate for protein kinase C. In addition, interferon did not inhibit the binding of 125I-epidermal growth factor to specific receptors or induce the expression of the proto-oncogene, c-fos in Swiss 3T3 cells. Thus, interferon does not activate protein kinase C. Moreover, interferon can still inhibit DNA synthesis in protein kinase C down-regulated 3T3 cells, indicating that the presence of this phosphotransferase is not essential for the anti-proliferative effects of interferon.
- Published
- 1987
- Full Text
- View/download PDF
22. Interferon inhibition of protein synthesis by isolated mitochondria.
- Author
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Kortsaris A, Taylor-Papadimitriou J, and Georgatsos JG
- Subjects
- Animals, Chloramphenicol pharmacology, Cycloheximide pharmacology, L Cells drug effects, L Cells metabolism, Mice, Mitochondria drug effects, RNA metabolism, Rabbits, Reticulocytes metabolism, Interferons pharmacology, Mitochondria metabolism, Protein Biosynthesis drug effects
- Published
- 1976
- Full Text
- View/download PDF
23. Use of two epithelium-specific monoclonal antibodies for diagnosis of malignancy in serous effusions.
- Author
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Epenetos AA, Canti G, Taylor-Papadimitriou J, Curling M, and Bodmer WF
- Subjects
- Adolescent, Adult, Aged, Antibody Specificity, Ascitic Fluid immunology, Cytodiagnosis, Epithelium immunology, Female, Humans, Immunoenzyme Techniques, Male, Middle Aged, Pleural Effusion immunology, Antibodies, Monoclonal immunology, Ascitic Fluid cytology, Neoplasms diagnosis, Pleural Effusion cytology
- Abstract
Two monoclonal antibodies, HMFG2 and AUA1, raised against epithelial-cell determinants were used to detect carcinoma cells in smears of serous effusions. Both antibodies react strongly with malignant epithelial cells but not with normal mesothelial or endothelial cells. A third antibody, 11-4.1, which does not react with any human tissue, was used as a negative control. An immunoperoxidase-staining technique was applied to smears of cells from serous effusions. The immunohistochemical diagnosis was in agreement with the cytological diagnosis. In cases with equivocal cytology in which the diagnosis became clear in later samples, the immunohistochemical diagnosis gave the correct result. With this combination of tumour-associated monoclonal antibodies a confident diagnosis of malignancy in serous effusions can be made.
- Published
- 1982
- Full Text
- View/download PDF
24. Selective inhibition by interferon of serum-stimulated biochemical events in 3T3 cells.
- Author
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Sreevalsan T, Taylor-Papadimitriou J, and Rozengurt E
- Subjects
- Animals, Biological Transport, Active drug effects, Cell Line, Dose-Response Relationship, Drug, Kinetics, Mice, Carboxy-Lyases metabolism, Deoxy Sugars metabolism, Deoxyglucose metabolism, Interferons pharmacology, Ornithine Decarboxylase metabolism, Phosphates metabolism, Rubidium metabolism, Uridine metabolism
- Published
- 1979
- Full Text
- View/download PDF
25. Monoclonal antibodies, electrophoretically transferred from polyacrylamide gels, retain their ability to bind specific antigens.
- Author
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Mather S and Taylor-Papadimitriou J
- Subjects
- Antibody Specificity, Collodion, Electrophoresis, Polyacrylamide Gel, Humans, Immunochemistry, Antibodies, Monoclonal isolation & purification, Antibody Affinity, Antigen-Antibody Reactions
- Abstract
Antibodies subjected to SDS-polyacrylamide gel electrophoresis and transferred to nitrocellulose paper, have been found to retain the ability to bind specific antigen. This has been demonstrated for two groups of antibodies, directed to a) a large molecular weight glycoprotein of the human milk fat globule and b) human interferon alpha 2. Immunoreactive antibody fragments produced by protease digestion could also be identified in this way on Western blots, thus permitting the development of optimal conditions for digestion, without the need for extensive purification procedures.
- Published
- 1985
- Full Text
- View/download PDF
26. An endonuclease activity associated with preparations of chick interferon.
- Author
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Taylor-Papadimitriou J, Spandidos D, and Georgatsos JG
- Subjects
- Animals, Cattle, Chick Embryo, Chromatography, Ion Exchange, Culture Techniques, DNA, Fibroblasts, Hydrogen-Ion Concentration, Newcastle disease virus radiation effects, Poly I-C, Radiation Effects, Thymus Gland, Ultraviolet Rays, Viscosity, Deoxyribonucleases, Interferons isolation & purification
- Published
- 1971
- Full Text
- View/download PDF
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