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  • PROTEOMIC ANALYSIS  (4)
  • 1
    Keywords: CANCER ; EXPRESSION ; INHIBITOR ; tumor ; carcinoma ; CELL ; Germany ; CLASSIFICATION ; DIAGNOSIS ; RISK ; PROTEIN ; SAMPLES ; PATIENT ; BIOLOGY ; ASSOCIATION ; FIELD ; ALPHA ; STAGE ; IDENTIFICATION ; IN-SITU ; immunohistochemistry ; genetics ; ABERRATIONS ; MASS-SPECTROMETRY ; ONCOGENE ; HUMAN-PAPILLOMAVIRUS ; SQUAMOUS-CELL CARCINOMA ; HEAD ; NECK ; RISK ASSESSMENT ; heredity ; BIOPSY ; protein expression ; PROTEOMICS ; PROTEOMIC ANALYSIS ; NECK-CANCER ; CELL CARCINOMA ; ONCOLOGY ; TUMORIGENESIS ; ARRAY ; HNSCC ; LYMPH-NODE METASTASIS ; development ; analysis ; PROFILES ; EVENTS ; protein biomarkers ; HISTOLOGY ; FRAGMENT ; SELDI-TOF-MS ; BIOPSIES ; CLINICAL-IMPLICATIONS ; aberration ; comparison ; acyl-CoA-binding protein ; CANCERIZATION ; field cancerization ; GENETICALLY ALTERED FIELDS ; HUMAN NEUTROPHIL PEPTIDE-1 ; TUMOR-DISTANT EPITHELIA
    Abstract: Development of head and necksquamous cell carcinoma (HNSCC) is a multistep process and in many cases involves a phenomenon coined 'field cancerization'. In order to identify changes in protein expression occurring at different stages of tumorigenesis and field cancerization, we analysed 113 HNSCCs and 73 healthy, 99 tumor-distant and 18 tumor-adjacent squamous mucosae by SELDI-TOF-MS on IMAC30 ProteinChip Arrays. Forty-eight protein peaks were differentially expressed between healthy mucosa and HNSCC. Calgizarrin (S100A11), the Cystein proteinase inhibitor Cystatin A, Acyl-CoA-binding protein, Stratifin (14-3-3 sigma), Histone H4, alpha- and beta-Hemoglobin, a C-terminal fragment of beta-hemoglobin and the alpha-defensins 1-3 were identified by mass spectrometry. The alpha-defensins showed various alterations in expression as validated by immunohistochemistry (IHC). Supervised prediction analysis revealed excellent classification of healthy mucosa (94.5% correctly classified) and tumor samples (92.9% correctly classified). Application of this classifier to the tumor-adjacent and tumor-distant mucosa samples disclosed dramatic changes: only 59.6% of the tumor-distant biopsies were classified as normal, 27.3% were predicted as aberrant or HNSCC. Strikingly, 72% of the tumor-adjacent mucosae were predicted as aberrant. These data provide evidence for the existence of genetically altered fields with inconspicuous histology. Comparison of the protein profiles in the tumor-distant-samples with clinical outcome of 32 patients revealed a significant association between aberrant profiles with tumor relapse events (P = 0.018; Fisher's exact test, two-tailed). We conclude that proteomic pro. ling in conjunction with protein identification greatly outperforms histopathological diagnosis and may have significant predictive power for clinical outcome and personalized risk assessment
    Type of Publication: Journal article published
    PubMed ID: 16819514
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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: RECEPTOR ; EXPRESSION ; Germany ; INFORMATION ; SUPPORT ; TOOL ; SITE ; PROTEIN ; PROTEINS ; TRANSDUCTION ; MECHANISM ; primary ; RAT ; mechanisms ; signal transduction ; MEMBRANE ; SIGNAL-TRANSDUCTION ; mass spectrometry ; MASS-SPECTROMETRY ; LOCALIZATION ; RECEPTORS ; FOOD ; protein expression ; PROTEOMIC ANALYSIS ; POLYACRYLAMIDE GELS ; NEURONS ; analysis ; TECHNOLOGY ; EPITHELIUM ; ENGLAND ; enzymatic ; XENOBIOTIC-METABOLIZING ENZYMES ; CHEMOSENSORY CILIA ; NUCLEOTIDE-GATED CHANNEL ; olfactory receptor neurons ; ODORANT RECEPTORS ; SENSITIVE ADENYLATE-CYCLASE ; sensory cilia
    Abstract: The cilia of mammalian olfactory receptor neurons (ORNs) represent the sensory interface that is exposed to the air within the nasal cavity. The cilia are the site where odorants bind to specific receptors and initiate olfactory transduction that leads to excitation of the neuron. This process involves a multitude of ciliary proteins that mediate chemoelectrical transduction, amplification, and adaptation of the primary sensory signal. Many of these proteins were initially identified by their enzymatic activities using a membrane protein preparation from olfactory cilia. This so-called "calcium-shock" preparation is a versatile tool for the exploration of protein expression, enzyme kinetics, regulatory mechanisms, and ciliary development. To support such studies, we present a first proteomic analysis of this membrane preparation. We subjected the cilia preparation to liquid chromatography-electrospray ionisation (LC-ESI-MS/MS) tandem mass spectrometry and identified 268 proteins, of which 49% are membrane proteins. A detailed analysis of their cellular and subcellular localization showed that the cilia preparation obtained by calcium shock not only is highly enriched in ORN proteins but also contains a significant amount of nonciliary material. Although our proteomic study does not identify the entire set of ciliary and nonciliary proteins, it provides the first estimate of the purity of the calcium-shock preparation and provides valuable biochemical information for further research
    Type of Publication: Journal article published
    PubMed ID: 18032372
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  • 4
    Keywords: RECEPTOR ; Germany ; PATHWAY ; PROTEIN ; PROTEINS ; COMPLEX ; RAT ; signal transduction ; SIGNAL ; MOUSE ; MEMBRANE ; SIGNAL-TRANSDUCTION ; mass spectrometry ; PROTEOMIC ANALYSIS ; signaling ; NEURONS ; EPITHELIUM ; NUCLEOTIDE-GATED CHANNEL ; olfactory receptor neurons ; sensory cilia ; ADENYLYL-CYCLASE ; CHLORIDE ACCUMULATION ; MAMMALIAN ODORANT RECEPTORS ; ORGANELLAR PROTEOMICS
    Abstract: Olfactory sensory neurons expose to the inhaled air chemosensory cilia which bind odorants and operate as transduction organelles. Odorant receptors in the ciliary membrane activate a transduction cascade which uses cAMP and Ca2+ for sensory signaling in the ciliary lumen. Although the canonical transduction pathway is well established, molecular components for more complex aspects of sensory transduction, like adaptation, regulation, and termination of the receptor response have not been systematically identified. Moreover, open questions in olfactory physiology include how the cilia exchange solutes with the surrounding mucus, assemble their highly polarized set of proteins, and cope with noxious substances in the ambient air. A specific ciliary proteome would promote research efforts in all of these fields. We have improved a method to detach cilia from rat olfactory sensory neurons and have isolated a preparation specifically enriched in ciliary membrane proteins. Using LC-ESI-MS/MS analysis, we identified 377 proteins which constitute the olfactory cilia proteome. These proteins represent a comprehensive data set for olfactory research since more than 80% can be attributed to the characteristic functions of olfactory sensory neurons and their cilia: signal processing, protein targeting, neurogenesis, solute transport, and cytoprotection. Organellar proteomics thus yielded decisive information about the diverse physiological functions of a sensory organelle
    Type of Publication: Journal article published
    PubMed ID: 19086097
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