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  • 1
    Keywords: brain ; CANCER ; CELLS ; ENDOTHELIAL-CELLS ; EXPRESSION ; tumor ; CELL ; Germany ; LUNG-CANCER ; SYSTEM ; DISEASE ; PROTEIN ; TISSUE ; MICE ; PATIENT ; ANTIGEN ; T-CELL ; T-CELLS ; BONE-MARROW ; MEMORY ; RECOGNITION ; MOUSE ; IDENTIFICATION ; LYMPHOMA ; EFFICACY ; MELANOMA ; MASS-SPECTROMETRY ; HEAD ; NECK ; EPITOPE ; IMMUNOTHERAPY ; IMMUNOGENICITY ; CANCER PATIENTS ; CALCIUM-BINDING PROTEINS ; TUMOR-ASSOCIATED ANTIGENS ; NECK-CANCER ; brain tumor ; head and neck cancer ; endothelial cells ; proteome ; EGFR ; SEPARATION ; EXPRESSION PROFILES ; Type ; HEAD-AND-NECK
    Abstract: Identifying the antigens that have the potential to trigger endogenous antitumor responses in an individual cancer patient is likely to enhance the efficacy of cancer immunotherapy, but current methodologies do not efficiently identify such antigens. This study describes what we believe to be a new method of comprehensively identifying candidate tissue antigens that spontaneously cause T cell responses in disease situations. We used the newly developed automated, two-dimensional chromatography system PF2D to fractionate the proteome of human tumor tissues and tested protein fractions for recognition by preexisting tumor-specific CD4(+) Th cells and CTLs. Applying this method using mice transgenic for a TCR that recognizes an OVA peptide presented by MHC class I, we demonstrated efficient separation, processing, and cross-presentation to CD8(+) T cells by DCs of OVA expressed by the OVA-transfected mouse lymphoma RMA-OVA. Applying this method to human tumor tissues, we identified MUC1 and EGFR as tumor-associated antigens selectively recognized by T cells in patients with head and neck cancer. Finally, in an exemplary patient with a malignant brain tumor, we detected CD4(+) and CD8(+) T cell responses against two novel antigens, transthyretin and calgranulin B/S100A9, which were expressed in tumor and endothelial cells. The immunogenicity of these antigens was confirmed in 4 of 10 other brain tumor patients. This fast and inexpensive method therefore appears suitable for identifying candidate T cell antigens in various disease situations, such as autoimmune and malignant diseases, without being restricted to expression by a certain cell type or HLA allele
    Type of Publication: Journal article published
    PubMed ID: 20458140
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  • 2
    Keywords: brain ; RECEPTOR ; CELLS ; Germany ; NETWORKS ; SYSTEM ; TOOL ; DISTINCT ; PROTEIN ; PROTEINS ; TRANSDUCTION ; COMPLEX ; MESSENGER-RNA ; RAT ; signal transduction ; MEMBRANE ; SIGNAL-TRANSDUCTION ; mass spectrometry ; MASS-SPECTROMETRY ; CHROMATOGRAPHY ; PROTEOMIC ANALYSIS ; glutathione-S-transferase ; BINDING PROTEIN ; signaling ; molecular ; NEURONS ; analysis ; cilia ; ENGLAND ; XENOBIOTIC-METABOLIZING ENZYMES ; affinity chromatography ; calcium-calmodulin ; CHEMOSENSORY CILIA ; NUCLEOTIDE-GATED CHANNEL ; olfaction ; olfactory receptor neurons ; PHOSPHOLIPID-BINDING ; SENSORY NEURONS
    Abstract: The olfactory neuroepithelium represents a unique interface between the brain and the external environment. Olfactory function comprises a distinct set of molecular tasks: sensory signal transduction, cytoprotection and adult neurogenesis. A multitude of biochemical studies has revealed the central role of Ca2+ signaling in the function of olfactory receptor neurons (ORNs). We set out to establish Ca2+-dependent signaling networks in ORN cilia by proteomic analysis. We subjected a ciliary membrane preparation to Ca2+/calmodulin-affinity chromatography using mild detergent conditions in order to maintain functional protein complexes involved in olfactory Ca2+ signaling. Thus, calmodulin serves as a valuable tool to gain access to novel Ca2+-regulated protein complexes. Tandem mass spectrometry (nanoscale liquid-chromatography-electrospray injection) identified 123 distinct proteins. Ninety-seven proteins (79%) could be assigned to specific olfactory functions, including 32 to sensory signal transduction and 40 to cytoprotection. We point out novel perspectives for research on the Ca2+-signaling networks in the olfactory system of the rat. (C) 2007 IBRO. Published by Elsevier Ltd. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 18155848
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  • 3
    Keywords: CELLS ; EXPRESSION ; carcinoma ; FACTOR RECEPTOR ; IN-VIVO ; PROTEIN ; HEAD ; NECK ; pancreatic cancer ; PROTEOMICS ; EPIDERMAL-GROWTH-FACTOR ; SERUM ; biomarker ; exosome ; METASTATIC BREAST-CANCER ; TARGETED THERAPY ; EGFR forms ; Secretome ; TUMOR AGGRESSIVENESS
    Abstract: Aims: Members of the epidermal growth factor receptor (EGFR) family represent validated targets for anticancer therapy and EGFR inhibitors have also shown efficacy in pancreatic carcinoma. We here described in detail molecular forms of the EGF receptor released by pancreatic cancer cells. We found peptides specific for the EGER in the secretomes of five pancreatic cancer cell lines. Secretomes from cultured cancer cells are widely used as sources for serum biomarker discovery. Main methods: The detailed analysis of EGFR forms in secretomes of human pancreatic cancer cells is a compilation of results from mass spectrometry (MS) and Western blotting with intracellular and extracellular domain specific antibodies. Key findings: Pancreatic cancer cells secrete a 110 kDa soluble form of the EGFR (sEGFR) representing the ligand binding extracellular EGFR domains and presumably released by ectodomain shedding. At the same time, as constituents of exosomes, the EGFR is released as full-length intact receptor (170 kDa) and as a 65 kDa processed form, the C-terminal remnant fragment that corresponds to the intracellular kinase domain. Significance: The detailed characterization of diverse EGER forms released by pancreatic cancer cells in vitro and presumably in vivo bears important implications for functional studies, for the validation of soluble EGFR as a serum biomarker and for the design of targeted therapies.
    Type of Publication: Journal article published
    PubMed ID: 21763319
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