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  • 1
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    Munich University Press
    Keywords: pancreatic carcinoma ; carcinoma ; DISEASES ; DISEASE ; PROTEOMICS ; pancreatic
    Type of Publication: Book chapter
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  • 2
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    Pancreatology 4 (2), 67-75 
    Keywords: EXPRESSION ; CELL ; Germany ; DISEASE ; HISTORY ; GENE-EXPRESSION ; PROTEIN ; PROTEINS ; RNA ; DNA ; FIELD ; EXPERIENCE ; AGE ; electrospray ionization ; SPECTROMETRY ; MASS-SPECTROMETRY ; STRATEGIES ; pancreatic carcinoma ; physiology ; PROTEOMICS ; 2-DIMENSIONAL GEL-ELECTROPHORESIS ; IMMOBILIZED PH GRADIENTS ; PROTEIN IDENTIFICATION ; GEL-ELECTROPHORESIS ; MASSES ; 2D ; BINDING-PROTEIN ; pancreas ; review ; genomics ; proteome ; PANCREATITIS ; TISSUE MICROARRAYS ; LASER CAPTURE MICRODISSECTION ; MASS-SPECTROMETRY DATA ; pancreatology ; PROTEIN-ANALYSIS ; SULFATE-POLYACRYLAMIDE GELS
    Abstract: Proteomics represents a novel methodological approach to investigate the expression of all proteins by a cell or organism in its entireness, similar to global strategies for DNA (genomics) and RNA (transcriptomics). This review focuses on the history of protein analysis, which made up the golden age of pancreatic physiology, the current methodology for proteomics (2D gel electrophoresis, mass spectrometry) and the few published experiences with proteomics in the field of pancreatology until now. Finally, potential applications of proteomics for the pancreas, in concert with other techniques, are cited. Copyright (C) 2004 S. Karger AG, Basel and IAP
    Type of Publication: Journal article published
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  • 3
    Keywords: EXPRESSION ; IN-VITRO ; Germany ; TYROSINE KINASE ; DIAGNOSIS ; NETWORKS ; SYSTEM ; TOOL ; DISEASE ; DISEASES ; PROTEIN ; PROTEINS ; TISSUE ; COMPLEX ; COMPLEXES ; RAT ; RATS ; PHOSPHORYLATION ; NERVOUS-SYSTEM ; IDENTIFICATION ; PATTERNS ; NUMBER ; mass spectrometry ; MASS-SPECTROMETRY ; DIETARY ; CENTRAL-NERVOUS-SYSTEM ; HABITS ; protein expression ; POLYACRYLAMIDE GELS ; GEL-ELECTROPHORESIS ; MASSES ; development ; PART ; MASS ; 2-DE ; ADULT-RAT ; enteric nervous system ; ENTERIC NERVOUS-SYSTEM ; MALDI-TOF mass spectrometry ; myenteric plexus ; peripheral nervous system ; PHOSPHOPROTEIN ; Sprague Dawley rats ; STATHMIN ; two-dimensional gel electrophoresis (2-DE)
    Abstract: The enteric nervous system in vertebrates is the most complex part of the peripheral nervous system. Concerning chemical coding, ultrastructure and neuronal circuits, it is more similar to the central than to the peripheral nervous system. Its networks, the myenteric and submucous plexus are integrated in the gut wall. The enteric nervous system is a system of high plasticity, which not only changes during pre- and postnatal development, but also with disease or changing dietary habits. The Aim of this study was to elucidate changes in protein expression during the first two postnatal weeks in the rat myenteric plexus. Colonic and duodenal myenteric plexus from newborn (P1) and fourteen-day old (P14) Sprague-Dawley rats was isolated following a procedure that combines enzymatic digestion and mechanical agitation. The neuronal tissue was collected and processed for two-dimensional gel electrophoresis (2-DE). The obtained 2-D gels were stained with silver for image analysis or with colloidal Coomassie for subsequent protein identification. Gels from the various samples showed a high degree of consistence concerning protein-spots found in all preparations. Nevertheless, there was a number of proteins that were clearly detected in one sample but not, or only in significantly smaller amounts in the other. Several differentially expressed proteins in the postnatal myenteric plexus were identified with MALDI-TOF mass spectrometry. Especially stathmin, polyubiquitin and heterogeneous nuclear ribonucleoprotein seem to play an important role in pre- and postnatal development. 2-DE combined with mass spectrometry can help to identify pathological relevant proteins in the enteric nervous system, and so deliver a valuable tool for the early diagnosis of also central nervous system diseases by using biopsies from the gut. (c) 2005 Elsevier B.V All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 16183334
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  • 4
    Abstract: Pancreatic ductal adenocarcinoma (PDAC) occurs mainly in people older than 50 years of age. Although great strides have been taken in treating PDAC over the past decades its incidence nearly equals its mortality rate and it was quoted as the 4th leading cause of cancer deaths in the U.S. in 2012. This review aims to focus on research models and scientific developments that help to explain the extraordinary resistance of PDAC towards current therapeutic regimens. Furthermore, it highlights the main features of drug resistance including mechanisms promoted by cancer cells or cancer stem cells (CSCs), as well as stromal cells, and the acellular components surrounding the tumor cells-known as peritumoral desmoplasia-that affects intra-tumoral drug delivery. Finally, therapeutic concepts and avenues for future research are suggested, based on the topics discussed.
    Type of Publication: Journal article published
    PubMed ID: 25337831
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  • 5
    Keywords: CANCER ; EXPRESSION ; SURVIVAL ; tumor ; carcinoma ; Germany ; THERAPY ; DISEASE ; PROTEINS ; TISSUE ; TUMORS ; MARKER ; prognosis ; BIOLOGY ; PATTERNS ; mass spectrometry ; MARKERS ; MASS-SPECTROMETRY ; Jun ; adenocarcinoma ; pancreatic cancer ; pancreatic carcinoma ; PROTEOMICS ; 2-DIMENSIONAL GEL-ELECTROPHORESIS ; chemoresistance ; SERUM ; PANCREATIC-CANCER ; DUCTAL ADENOCARCINOMA ; SOLID TUMORS ; analysis ; pancreatic ; PROGNOSTIC MARKER ; TECHNOLOGY ; JUICE ; genomic ; protein profiling
    Abstract: Ductal pancreatic adenocarcinoma is a dismal disease, having the worst prognosis of all solid tumors. While genomics and transcriptomics have provided a wealth of data, no contribution has been made to clinical medicine in terms of diagnostic or prognostic markers. Hope lies in yet another novel technology, proteomics. Conceptually, proteomics bears the advantage of incorporating both posttranslational modifications as well as host factors. This is thought to be important in factors influencing survival such as chemoresistance. This tutorial review discusses the state of the art in pancreatic cancer proteomics in light of technical developments. At this moment, proteomics is still at the beginning in clinical application. First results, however, suggest some hope for the development of a new understanding of the molecular biology in pancreatic cancer yielding into very specific markers of disease or allowing a rational and individualized therapy
    Type of Publication: Journal article published
    PubMed ID: 16773365
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  • 6
    Keywords: CELLS ; EXPRESSION ; IN-VITRO ; tumor ; carcinoma ; CELL ; Germany ; MODEL ; VITRO ; GENE ; GENES ; HYBRIDIZATION ; PROTEIN ; PROTEINS ; SAMPLES ; TUMORS ; MARKER ; prognosis ; CARCINOGENESIS ; SEQUENCE ; SUPPRESSION ; ALPHA ; MOUSE ; COMPARATIVE GENOMIC HYBRIDIZATION ; CANCER-CELLS ; TRANSFORMATION ; adenocarcinoma ; ki-ras ; K-RAS ; HUMAN BREAST-TUMORS ; MOLECULAR-CLONING ; PROTEOMICS ; Ras ; PROTEOMIC ANALYSIS ; 2-DIMENSIONAL GEL-ELECTROPHORESIS ; DRUG-INDUCED APOPTOSIS ; RE ; TRANSFECTION ; development ; pancreatic ; BOVINE ; UNIT ; BINDING PROTEINS ; pancreatic carcinogenesis ; ANNEXIN-I ; SV40 large T ; transcriptomics
    Abstract: Pancreatic carcinoma has an extremely bad prognosis due to lack of early diagnostic markers and lack of effective therapeutic strategies. Recently, we have established an in vitro model recapitulating the first steps in the carcinogenesis of the pancreas. SV40 large T antigen-immortalized bovine pancreatic duct cells formed intrapancreatic adenocarcinoma tumors on k-ras(mut) transfection after orthotopic injection in the nude mouse pancreas. Here we identified genes and proteins differentially expressed in the course of malignant transformation using reciprocal suppression subtractive hybridization and 2D gel electrophoresis and mass spectrometry, respectively. We identified 34 differentially expressed genes, expressed sequence tags, and 15 unique proteins. Differential expression was verified for some of the genes or proteins in samples from pancreatic carcinoma. Among these genes and proteins, the majority had already been described either to be influenced by a mutated ras or to be differentially expressed in pancreatic adenocarcinoma, thus proving the feasibility of our model. Other genes and proteins (e.g., BBC1, GLTSCR2, and rhoGDI alpha), up to now, have not been implicated in pancreatic tumor development. Thus, we were able to establish an in vitro model of pancreatic carcinogenesis, which enabled us to identify genes and proteins differentially expressed during the early steps of malignant transformation
    Type of Publication: Journal article published
    PubMed ID: 17356710
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  • 7
    Keywords: CANCER ; CELLS ; EXPRESSION ; carcinoma ; CELL ; human ; PROTEIN ; PROTEINS ; RNA ; LINES ; primary ; CELL-LINES ; 5-FLUOROURACIL ; BREAST ; breast cancer ; BREAST-CANCER ; ASSAY ; resistance ; CARCINOMA CELLS ; CELL-LINE ; chemotherapy ; LINE ; CARCINOMA-CELLS ; sensitivity ; MULTIDRUG-RESISTANCE ; pancreatic cancer ; pancreatic carcinoma ; protein expression ; CYTOTOXICITY ; multidrug resistance ; PANCREATIC-CANCER ; INTERFERENCE ; RNA INTERFERENCE ; P-GLYCOPROTEIN ; TRANSPORTER ; mRNA ; methods ; multidrug resistance protein ; MRP3 ; MRP4 ; MULTIDRUG-RESISTANCE-PROTEIN ; MULTIDRUG ; quantitative ; PROFILE ; CANCER RESISTANCE PROTEIN ; MDR1 P-GLYCOPROTEIN ; expression profile ; ABC
    Abstract: Pancreatic cancer is characterized by high resistance to chemotherapy. Such chemoresistance can be mediated by multidrug resistance proteins (MRPs), breast cancer resistance protein (BCRP), and MDR1 P-glycoprotein. However, the contribution of individual MRP isoforms to chemoresistance in pancreatic carcinoma is unclear. We studied ATP-binding cassette (ABC) transporter expression in human pancreatic carcinoma cell lines as compared to primary pancreatic duct cells, and analyzed the MRP expression profile in 5-fluorouracil-resistant cells. Methods: Transporter expression was analyzed by quantitative and qualitative RT-PCR, by immunoblot, and chemoresistance by cytotoxicity assay. Results: Primary pancreatic duct cells expressed MRP1, MRP3, MRP4, and MRP5, but not MRP2 mRNA. The established carcinoma cell lines expressed MRP1, MRP4, and MRP5, most of them also MRP2, MRP3, MRP7, and BCRP, but none contained detectable amounts of MRP6, MRP8, or MRP9 mRNA. Immunoblot analyses demonstrated presence of MRP1, MRP4, and MRP5 protein in all, but MRP3 and BCRP protein only in some of these cells. Compared to parental Capan-1 cells, Capan-1 cells with acquired chemoresistance towards 5-fluorouracil showed an upregulated mRNA and protein expression of MRP3, MRP4, and MRP5. In addition, silencing of MRP5 by RNA interference resulted in enhanced sensitivity of parental Capan-1 cells towards 5-fluorouracil cytotoxicity. Conclusion: MRP3, MRP4, and MRP5 are upregulated in 5-fluorouracil-resistant cells, and MRP5 contributes to 5-FU resistance in pancreatic carcinoma cells. and IAP
    Type of Publication: Journal article published
    PubMed ID: 19077464
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  • 8
    Keywords: CANCER ; ANTIGEN ; PROGNOSTIC VALUE ; SERUM ; GEMCITABINE ; PANCREATIC-CANCER ; CEA ; BIOLOGICAL VARIATION ; CA19-9 gastrointestinal cancer antigen ; GI Monitor,pancreatic cancer ; IMMUNOASSAYS MARKER CA-19-9 ; method comparison,diagnosis ; TUMOR-ASSOCIATED ANTIGEN ; UTILITY
    Abstract: Background: This study was designed to investigate the clinical performance of the Access GI Monitor (Beckman Coulter) on the UniCel DxI 800, a method for CA19-9 antigen determination, and to compare with CA19-9 assay on the AxSYM system (Abbott). Methods: 1,063 serum samples from unselected patients with different underlying diagnoses were tested with both methods. Passing-Bablok regression analysis and Bland Altman analysis was performed. In addition, using ROC analysis, the distribution of Access Cl Monitor and AxSYM CA19-9 antigen levels was tested in patients with pancreatic cancer (n = 50), acute inflammatory disease (n = 20), and with chronic inflammation of the pancreatic gland (n = 18). Furthermore, four patients with pancreatic cancer were monitored individually in their courses of the disease (before, during, and after therapeutic procedures) to compare their CA19-9 values with regard to inter-method concordance. Results: Passing-Bablok analysis showed a systematic difference with R = 0.93, slope 0.75, and intercept -1.0. Bland Altman analysis showed a wide scatter of relative differences between both methods, especially in the low end measuring range. In the selected group of patients with pancreatic diseases the analysis of concordance revealed 95.5 % agreement between both methods with a comparable area under the ROC curves (0.73 vs. 0.76). A clear concordance was found for all four selected patients. Conclusions: Although we found significant systematic measuring variations in the global analysis, the two different automated methods for the quantitative determination of CA19-9 antigen were comparable with respect to their clinical accuracy and applicability to support decision making in the management of pancreatic cancer.
    Type of Publication: Journal article published
    PubMed ID: 20857896
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  • 9
    Abstract: OBJECTIVES: Autoimmune pancreatitis (AIP) is thought to be an immune-mediated inflammatory process, directed against the epithelial components of the pancreas. The objective was to identify novel markers of disease and to unravel the pathogenesis of AIP. METHODS: To explore key targets of the inflammatory process, we analyzed the expression of proteins at the RNA and protein level using genomics and proteomics, immunohistochemistry, western blot, and immunoassay. An animal model of AIP with LP-BM5 murine leukemia virus-infected mice was studied in parallel. RNA microarrays of pancreatic tissue from 12 patients with AIP were compared with those of 8 patients with non-AIP chronic pancreatitis. RESULTS: Expression profiling showed 272 upregulated genes, including those encoding for immunoglobulins, chemokines and their receptors, and 86 downregulated genes, including those for pancreatic proteases such as three trypsinogen isoforms. Protein profiling showed that the expression of trypsinogens and other pancreatic enzymes was greatly reduced. Immunohistochemistry showed a near-loss of trypsin-positive acinar cells, which was also confirmed by western blotting. The serum of AIP patients contained high titers of autoantibodies against the trypsinogens PRSS1 and PRSS2 but not against PRSS3. In addition, there were autoantibodies against the trypsin inhibitor PSTI (the product of the SPINK1 gene). In the pancreas of AIP animals, we found similar protein patterns and a reduction in trypsinogen. CONCLUSIONS: These data indicate that the immune-mediated process characterizing AIP involves pancreatic acinar cells and their secretory enzymes such as trypsin isoforms. Demonstration of trypsinogen autoantibodies may be helpful for the diagnosis of AIP.
    Type of Publication: Journal article published
    PubMed ID: 20407433
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  • 10
    Keywords: INHIBITOR ; Germany ; MICROSCOPY ; THERAPY ; PROTEIN ; PROTEINS ; COMPONENTS ; PATIENT ; MECHANISM ; mechanisms ; IDENTIFICATION ; mass spectrometry ; MASS-SPECTROMETRY ; LENGTH ; Jun ; DEGRADATION ; CALCIUM ; PROTEASOME ; chronic pancreatitis ; MANAGEMENT ; GEL-ELECTROPHORESIS ; INHIBITORS ; MASSES ; albumin ; PRODUCTS ; LIGHT ; PH ; WEIGHT ; SODIUM ; development ; methods ; pancreatic ; MASS ; PLACEMENT ; CRITERIA ; CRYSTAL ; JUICE ; LITHOSTATHINE ; STENTS ; STONE PROTEIN ; SULFATE ; technique
    Abstract: Background: Endoscopic management of chronic pancreatitis (CP), especially pancreatic stent placement, has made tremendous advances. However, good clinical results are hampered by rapid occlusion. The objective of this study was to understand mechanisms and materials that cause stent occlusion. Methods: The clogging material of 50 lyophilized pancreatic endoprostheses (length 8.5 cm, range 5-14 cm, diameter 7-11F) from patients with CP was completely removed and weighed. Protein solubilization was achieved at pH 8.0 by using sodium dodecyl sulfate (SDS) and 2-mercaptoethanol in the presence of proteasome inhibitors. Proteins were separated by using a SDS-polyacrylamide gel electrophoresis. Protein identification was performed by the Western blot technique, as well as by mass spectrometry. Insoluble components were examined by polarized light microscopy and after staining (periodic acid-Schiff [PAS]). Results: Clogging material was found in 49 prostheses, mainly at the duodenal flap (80%). More than a third of the prostheses contained visible calcium carbonate calculi. Light microscopy and PAS staining showed plant debris (80%), crystals (73.5%), and mucopolysaccharides (100%). The dry weight of clogging material (18 +/- 13 mg, range 3-72 mg) correlated significantly with the stent diameter (p = 0.029) but not with any other stent- or patient-related criteria. Albumin, its degradation products, and lithostathine were identified as the main proteinaceous components. Conclusions: Almost all pancreatic stents had clogging material, predominantly located at the duodenal flap, which contained plant material, mucopolysaccharides, and crystals, as well as visible calcium carbonate calculi. Albumin and lithostathine may play an important role in the development of stent occlusion
    Type of Publication: Journal article published
    PubMed ID: 15933688
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