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  • ddc: 610  (23)
  • CANCER  (16)
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  • 1
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  65. Kongress der Nordrhein-Westfälischen Gesellschaft für Urologie; 20190328-20190329; Münster; DOCP 2.16 /20190225/
    Publication Date: 2019-02-26
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 2
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  86. Jahresversammlung der Deutschen Gesellschaft für Hals-Nasen-Ohren-Heilkunde, Kopf- und Hals-Chirurgie; 20150513-20150516; Berlin; DOC15hnod272 /20150326/
    Publication Date: 2015-03-27
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 3
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  86. Jahresversammlung der Deutschen Gesellschaft für Hals-Nasen-Ohren-Heilkunde, Kopf- und Hals-Chirurgie; 20150513-20150516; Berlin; DOC15hnod282 /20150326/
    Publication Date: 2015-03-27
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 4
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  86. Jahresversammlung der Deutschen Gesellschaft für Hals-Nasen-Ohren-Heilkunde, Kopf- und Hals-Chirurgie; 20150513-20150516; Berlin; DOC15hnod266 /20150326/
    Publication Date: 2015-03-27
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 5
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  84. Jahresversammlung der Deutschen Gesellschaft für Hals-Nasen-Ohren-Heilkunde, Kopf- und Hals-Chirurgie; 20130508-20130512; Nürnberg; DOC13hnod306 /20130415/
    Publication Date: 2013-04-16
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 6
    Keywords: RECEPTOR ; CANCER ; EXPRESSION ; tumor ; carcinoma ; Germany ; human ; HYBRIDIZATION ; PROTEIN ; PROTEINS ; TISSUE ; TUMORS ; PATIENT ; FAMILY ; MARKER ; hormone ; IN-SITU ; PROGRESSION ; immunohistochemistry ; PATTERNS ; prostate cancer ; PROSTATE-CANCER ; MARKERS ; BENIGN ; GLYCATION END-PRODUCTS ; RAGE ; CARCINOMAS ; adenocarcinoma ; intraepithelial neoplasia ; NEURITE OUTGROWTH ; KAPPA-B ; CANCER PATIENTS ; HEALTHY ; prostate carcinoma ; OXIDANT STRESS ; SERUM ; in situ hybridization ; ELISA ; RE ; END ; TUMORIGENESIS ; HUMAN PROSTATE ; HYPERPLASIA ; TUMOR TISSUE ; MOLECULAR-GENETICS ; HUMAN-PROSTATE ; S100 PROTEINS ; EXPRESSION PATTERNS ; SERUM-LEVELS ; TUMOR DIFFERENTIATION
    Abstract: Purpose: S100 proteins comprise a family of calcium-modulated proteins that have recently been associated with epithelial tumors. We examined the expression of two members of this family, S10OA8 and S100A9, together with the S100 receptor RAGE (receptor for advanced glycation end products) in human prostate adenocarcinomas and in prostatic intraepithelial neoplasia. Experimental Design:Tissue specimens of 75 patients with organ-confined prostate cancer of different grades were analyzed by immunohistochemistry for expression of S10OA8, S100A9, and RAGE. In addition, in situ hybridization of S10OA8 and S10OA9 was done for 20 cases. An ELISA was applied to determine serum concentrations of S10OA9 in cancer patients compared with healthy controls or to patients with benign prostatic hyperplasia (BPH). Results: S100A8, S100A9, and RAGE were up-regulated in prostatic intraepithelial neoplasia and preferentially in high-grade adenocarcinomas, whereas benign tissue was negative or showed weak expression of the proteins. There was a high degree of overlap of S10OA8 and S10OA9 expression patterns and of S100A8 or S100A9 and RAGE, respectively. Frequently, a gradient within the tumor tissue with an increased expression toward the invaded stroma of the prostate was observed. S100A9 serum levels were significantly elevated in cancer patients compared with BPH patients or healthy individuals. Conclusion: Our data suggest that enhanced expression of S100A8, S100A9, and RAGE is an early event in prostate tumorigenesis and may contribute to development and progression or extension of prostate carcinomas. Furthermore, S100A9 in serum may serve as useful marker to discriminate between prostate cancer and BPH
    Type of Publication: Journal article published
    PubMed ID: 16033829
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  • 7
    Keywords: APOPTOSIS ; CANCER ; EXPRESSION ; GROWTH ; proliferation ; carcinoma ; CELL ; CELL-PROLIFERATION ; Germany ; LUNG ; DIAGNOSIS ; lung cancer ; LUNG-CANCER ; DEATH ; GENE ; GENES ; microarray ; PROTEIN ; cell line ; meningioma ; TISSUE ; LINES ; primary ; DOMAIN ; tumour ; SKIN ; BIOLOGY ; CELL-LINES ; MEMBER ; MOLECULAR-BIOLOGY ; SIGNAL ; PROGRESSION ; ASSAY ; INDUCED APOPTOSIS ; genetics ; COUNTRIES ; skin cancer ; CELL-LINE ; LINE ; ONCOGENE ; SUPERFAMILY ; EPITHELIAL-CELLS ; Jun ; PHENOTYPE ; STRATEGIES ; OVEREXPRESSION ; cell lines ; heredity ; LUNG-CARCINOMA ; SKIN-CANCER ; tumour suppressor gene ; ORIGIN ; molecular biology ; molecular ; ONCOLOGY ; non-small cell lung carcinoma ; SUPPRESSOR GENE ; cell proliferation ; SUPPRESSOR ; tumour suppressor ; NSCLC ; SET ; BREAST-CANCER CELLS ; DAL-1 ; ferm containing 3 ; GROWTH SUPPRESSION ; protein 4.1 ; PROTEIN 4.1B
    Abstract: Lung cancer including non-small cell lung carcinoma (NSCLC) represents a leading cause of cancer death in Western countries. Yet, understanding its pathobiology to improve early diagnosis and therapeutic strategies is still a major challenge of today's biomedical research. We analyzed a set of differentially regulated genes that were identifi. ed in skin cancer by a comprehensive microarray study, for their expression in NSCLC. We found that ferm domain containing protein 3 (FRMD3), a member of the protein 4.1 superfamily, is expressed in normal lung tissue but silenced in 54 out of 58 independent primary NSCLC tumours compared to patient-matched normal lung tissue. FRMD3 overexpression in different epithelial cell lines resulted in a decreased clonogenicity as measured by colony formation assay. Although cell attachment capabilities and cell proliferation rate remained unchanged, this phenotype was most likely owing to induced apoptosis. Our data identify FRMD3 as a novel putative tumour suppressor gene suggesting an important role in the origin and progression of lung cancer
    Type of Publication: Journal article published
    PubMed ID: 17260017
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  • 8
    Keywords: CANCER ; EXPRESSION ; TUMORS ; RECURRENCE ; REVEALS ; nucleolus ; MYB-BINDING PROTEIN
    Abstract: ABSTRACT: BACKGROUND: Head and neck squamous cell carcinoma (HNSCC) is one of the most prevalent and lethal cancers worldwide and mortality mostly results from loco-regional recurrence and metastasis. Despite its significance, our knowledge on molecular, cellular and environmental mechanisms that drive disease pathogenesis remains largely elusive, and there are limited therapeutic options, with only negligible clinical benefit. METHODS: We applied global gene expression profiling with samples derived from a recently established mouse model for oral cancer recurrence and identified a list of genes with differential expression between primary and recurrent tumors. RESULTS: One differentially expressed gene codes for Myb-binding protein 1a (MYBBP1A), which is known as a transcriptional co-regulator that physically interacts with nuclear transcription factors, such as NFkappaB and p53. We confirmed significantly reduced MYBBP1A protein levels on tissue sections of recurrent mouse tumors compared to primary tumors by immunohistochemistry, and found aberrant MYBBP1A protein levels also in tumor samples of HNSCC patients. Interestingly, silencing of MYBBP1A expression in murine SCC7 and in human HNSCC cell lines elicited increased migration but decreased cell growth. CONCLUSION: We provide experimental evidence that MYBBP1A is an important molecular switch in the regulation of tumor cell proliferation versus migration in HNSCC and it will be a major challenge for the future to proof the concept whether regulation MYBBP1A expression and/or function could serve as a novel option for anti-cancer therapy.
    Type of Publication: Journal article published
    PubMed ID: 22339894
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  • 9
    Keywords: RECEPTOR ; CANCER ; IN-VITRO ; DIFFERENTIATION ; FAMILY ; CARCINOGENESIS ; HUMAN-PAPILLOMAVIRUS ; HEAD ; inflammation ; DEPENDENT PATHWAY
    Abstract: S100/calgranulins (S100A8, S100A9 and S100A12) are key players of innate immune function and elevated levels are a characteristic feature of acute and chronic inflammation, and inflammation-associated carcinogenesis. However, reduced S100A8 and S100A9 expression has been detected for squamous cell carcinoma, including the head and neck region (HNSCC), which originate from mucosal epithelia with abundant expression of both proteins under physiological conditions. In contrast to S100A8 and S100A9, only sparse information is available for S100A12 and a comparative study of all three S100/calgranulins in HNSCC is still missing. We analyzed S100/calgranulin protein levels in a retrospective patient cohort (n=131) of oropharyngeal squamous cell carcinoma (OPSCC) by immunohistochemical staining of tissue microarrays. Common characteristics of all three S100/calgranulins were: (i) abundant expression in supra-basal keratinocytes of normal mucosa with predominant nuclear staining, (ii) low expression in 30.4-51.9% of primary OPSCCs and (iii) variable accumulation of S100/calgranulin-positive immune cells in the tumor stroma. These features were associated with histopathological characteristics, such as tumor grade, lymph node metastasis and tumor stage. Furthermore, univariate and multivariate analysis revealed worse overall survival of OPSCC patients with simultaneous reduction of S100A8 and S100A12 expression, while expression of S100A9 or presence of the S100A8/S100A9 heterodimer had no impact, suggesting distinct regulation and function of individual S100/calgranulins in the pathogenesis of HNSCCs. What's new? Inflammation can alter the expression of specific proteins, and in the context of head and neck squamous cell carcinoma (HNSCC), which involves a high degree of inflammation, those changes may be of diagnostic or prognostic significance. Here, reduced expression of calcium-binding S100/calgranulin proteins was found to be a common feature of oropharyngeal SCC. Moreover, simultaneous low protein expression of S100A8 and S100A12 in tumor cells was an independent risk factor for unfavorable overall survival. The regulation and function of S100/calgranulins likely is context-dependent, with differences between mucosal and squamous epithelia.
    Type of Publication: Journal article published
    PubMed ID: 25302747
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  • 10
    Keywords: CANCER ; EXPRESSION ; carcinoma ; PROTEINS ; MICE ; ACTIVATION ; murine ; RAGE ; ROLES ; PROMOTES
    Abstract: The S100A8/A9 heterodimer (calprotectin) acts as a danger signal when secreted into the extracellular space during inflammation and tissue damage. It promotes proinflammatory responses and drives tumor development in different models of inflammation-driven carcinogenesis. S100A8/A9 is strongly expressed in several human tumors, including hepatocellular carcinoma (HCC). Apart from this evidence, the role of calprotectin in hepatocyte transformation and tumor microenvironment is still unknown. The aim of this study was to define the function of S100A8/A9 in inflammation-driven HCC. Mice lacking S100a9 were crossed with the Mdr2(-/-) model, a prototype of inflammation-induced HCC formation. S100a9(-/-) Mdr2(-/-) (dKO) mice displayed no significant differences in tumor incidence or multiplicity compared to Mdr2(-/-) animals. Chronic liver inflammation, fibrosis and oval cell activation were not affected upon S100a9 deletion. Our data demonstrate that, although highly upregulated, calprotectin is dispensable in the onset and development of HCC, and in the maintenance of liver inflammation. What's new? Liver cancers often overexpress a protein, S100A9, which functions as a danger signal during inflammation. It promotes inflammation and can drive the development of some tumors. In this paper, the authors sought to define the role of S100A9 in liver cancer. When they eliminated the protein from mice prone to inflammation-driven hepatocellular cancer, the liver tumors continued to develop unabated. Although it's highly upregulated in liver cancers, S100A9 isn't required for liver tumors to form, and wouldn't be useful as a therapeutic target.
    Type of Publication: Journal article published
    PubMed ID: 25331529
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