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  • 1
  • 2
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  41. Gemeinsame Tagung der Österreichischen Gesellschaft für Urologie und Andrologie und der Bayerischen Urologenvereinigung; 20150611-20150613; Linz; DOCKV65 /20150519/
    Publication Date: 2015-05-20
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 3
    Keywords: CELLS ; METABOLISM ; SEQUENCES ; INTERFACE ; inflammation ; INNATE ; PROBE LEVEL ; MICROBIAL ECOLOGY ; GUT MICROBIOME
    Abstract: Several features common to a Western lifestyle, including obesity and low levels of physical activity, are known risk factors for gastrointestinal cancers. There is substantial evidence suggesting that diet markedly affects the composition of the intestinal microbiota. Moreover, there is now unequivocal evidence linking dysbiosis to cancer development. However, the mechanisms by which high-fat diet (HFD)-mediated changes in the microbial community affect the severity of tumorigenesis in the gut remain to be determined. Here we demonstrate that an HFD promotes tumour progression in the small intestine of genetically susceptible, K-rasG12Dint, mice independently of obesity. HFD consumption, in conjunction with K-ras mutation, mediated a shift in the composition of the gut microbiota, and this shift was associated with a decrease in Paneth-cell-mediated antimicrobial host defence that compromised dendritic cell recruitment and MHC class II molecule presentation in the gut-associated lymphoid tissues. When butyrate was administered to HFD-fed K-rasG12Dint mice, dendritic cell recruitment in the gut-associated lymphoid tissues was normalized, and tumour progression was attenuated. Importantly, deficiency in MYD88, a signalling adaptor for pattern recognition receptors and Toll-like receptors, blocked tumour progression. The transfer of faecal samples from HFD-fed mice with intestinal tumours to healthy adult K-rasG12Dint mice was sufficient to transmit disease in the absence of an HFD. Furthermore, treatment with antibiotics completely blocked HFD-induced tumour progression, suggesting that distinct shifts in the microbiota have a pivotal role in aggravating disease. Collectively, these data underscore the importance of the reciprocal interaction between host and environmental factors in selecting a microbiota that favours carcinogenesis, and they suggest that tumorigenesis is transmissible among genetically predisposed individuals.
    Type of Publication: Journal article published
    PubMed ID: 25174708
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  • 4
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  12. Deutscher Kongress für Versorgungsforschung; 20131023-20131025; Berlin; DOCT3-11-288 /20131025/
    Publication Date: 2013-10-26
    Keywords: Demenz ; Wohngemeinschaft ; Pflege ; Kosten ; ddc: 610
    Language: German
    Type: conferenceObject
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  • 5
    Abstract: The atypical chemokine receptor 2 (ACKR2), also named D6, regulates local levels of inflammatory chemokines by internalization and degradation. To explore potential anti-inflammatory functions of ACKR2 in glomerulonephritis, we induced autologous nephrotoxic nephritis in C57/BL6 wild-type and Ackr2-deficient mice. Renal ACKR2 expression increased and localized to interstitial lymphatic endothelium during nephritis. At two weeks Ackr2(-/-)mice developed increased albuminuria and urea levels compared to wild-type mice. Histological analysis revealed increased structural damage in the glomerular and tubulointerstitial compartments within Ackr2(-/-) kidneys. This correlated with excessive renal leukocyte infiltration of CD4(+) T cells and mononuclear phagocytes with increased numbers in the tubulointerstitium but not glomeruli in knockout mice. Expression of inflammatory mediators and especially markers of fibrotic tissue remodeling were increased along with higher levels of ACKR2 inflammatory chemokine ligands like CCL2 in nephritic Ackr2(-/-) kidneys. In vitro, Ackr2 deficiency in TNF-stimulated tubulointerstitial tissue but not glomeruli increased chemokine levels. These results are in line with ACKR2 expression in interstitial lymphatic endothelial cells, which also assures efflux of activated leukocytes into regional lymph nodes. Consistently, nephritic Ackr2(-/-) mice showed reduced adaptive cellular immune responses indicated by decreased regional T-cell activation. However, this did not prevent aggravated injury in the kidneys of Ackr2(-/-) mice with nephrotoxic nephritis due to simultaneously increased tubulointerstitial chemokine levels, leukocyte infiltration and fibrosis. Thus, ACKR2 is important in limiting renal inflammation and fibrotic remodeling in progressive nephrotoxic nephritis. Hence, ACKR2 may be a potential target for therapeutic interventions in immune complex glomerulonephritis.
    Type of Publication: Journal article published
    PubMed ID: 29395335
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  • 6
    Keywords: Germany ; INHIBITION ; EXPOSURE ; RAT ; RATS ; WATER ; PATTERNS ; HEALTH ; WEIGHT ; COMMUNITIES ; xanthohumol ; PRENYLFLAVONOIDS ; chalcone ; HOPS HUMULUS-LUPULUS ; PRENYLATED FLAVONOIDS ; 16S RIBOSOMAL-RNA ; FECAL SAMPLES ; FECES ; FLORA ; GRADIENT GEL-ELECTROPHORESIS ; intestinal microbiota ; microbial diversity ; PCR-DGGE ; TANNIC-ACID
    Abstract: Xanthohumol (XN), a prenylated chalcone, has been proposed to have beneficial effects on human health, including antimicrobial activity. To clarify whether the exposure to XN has an impact on the composition of the intestinal microbiota, 100 mg XN/kg body weight was given daily to rats for 4 wk. Diversity of the fecal microbial community was analyzed using PCR-DGGE. Although intact XN was detected in the feces of the rats at a concentration of up to 2.3 mg/g fecal dry weight, major shifts in the PCR-DGGE patterns in response to this flavonoid were not observed. The similarity index decreased slightly from 70 to 62% for the XN-treated rats and from 71 to 63% for the untreated animals. Thus, changes in the rat fecal microbiota observed in the course of the XN application are most likely due to intraindividual variability. However, the water content of the feces increased significantly during the XN treatment period
    Type of Publication: Journal article published
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  • 7
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  43. Gemeinsame Tagung der Österreichischen Gesellschaft für Urologie und Andrologie und der Bayerischen Urologenvereinigung; 20170518-20170520; Wien; DOC17oegu018 /20170403/
    Publication Date: 2017-04-03
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 8
    ISSN: 1432-072X
    Keywords: Archaebacteria ; methanogenesis ; energy conservation ; membranes ; F420-dependent hydrogenase ; Methanosarcina
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The distribution of the F420-reactive and F420-nonreactive hydrogenases from the methylotrophic Methanosarcina strain Gö1 indicated a membrane association of the F420-nonreactive enzyme. The membrane-bound F420-nonreactive hydrogenase was purified 42-fold to electrophoretic homogeneity with a yield of 26.7%. The enzyme had a specific activity of 359 μmol H2 oxidized · min-1 · mg protein-1. The purification procedure involved dispersion of the membrane fraction with the detergent Chaps followed by anion exchange, hydrophobic and hydroxylapatite chromatography. The aerobically prepared enzyme had to be reactivated anaerobically. Maximal activity was observed at 80°C. The molecular mass as determined by native gel electrophoresis and gel filtration was 77000 and 79000, respectively. SDS gel electrophoresis revealed two polypeptides with molecular masses of 60000 and 40000 indicating a 1:1 stoichiometry. The purified enzyme contained 13.3 mol S2-, 15.1 mol Fe and 0.8 mol Ni/mol enzyme. Flavins were not detected. The amino acid sequence of the N-termini of the subunits showed a higher degree of homology to cubacterial uptake-hydrogenases than to F420-dependent hydrogenases from other methanogenic bacteria. The physiological function of the F420-nonreactive hydrogenase from Methanosarcina strain Gö1 is discussed.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-072X
    Keywords: Cytochromes ; Redox difference spectroscopy ; Midpoint potential ; Betaine ; Formate ; Acetoin ; Acetyl-CoA pathway ; Sporomusa ovata ; Sporomusa sphaeroides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The homoacetogenic bacteria Sporomusa ovata and Sporomusa sphaeroides were grown on betaine, betaine + formate, and acetoin in the absence of carbon dioxide, and the formation of membrane-bound cytochromes was determined. In S. sphaeroides, the growth substrate had little influence on the expression of cytochromes. In contrast, membranes from betaine-or acetoin-grown S. ovata cells had an 11-or 3-fold higher cytochrome b content than cells grown on betaine + formate. The cytochrome c content was reduced below the detection level after growth on the latter two substrates. The cytochromes in the membranes of S. sphaeroides and S. ovata were characterized by low-temperature difference spectroscopy, hemochrome difference spectroscopy, and redox potentiometry. Membranes of S. ovata were shown to contain two b-type cytochromes with Em,7=-153±10 mV and Em,7=-226±14 mV and two c-type cytochromes with Em,7=-86±6 mV and Em,7=-265±10 mV. In S. sphaeroides also two b-type cytochromes with Em,7=-165±7 mV and Em,7=-241±2 mV and two c-type cytochromes with Em,7=-101±4 mV and Em, 8.5=-338±9 mV could be distinguished. Cell extracts of S. sphaeroides were shown to contain all the enzymes of the acetyl-CoA (Wood) pathway. The degradation pathways of the substrates tested and the possible role of the cytochromes are discussed.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-072X
    Keywords: Key words Homoacetogens ; Hydrogenase ; Cytochromes ; Energy conservation ; Acetyl CoA ; pathway ; Membranes ; Sporomusa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Hydrogenase was solubilized from the cytoplasmic membrane fraction of betaine-grown Sporomusa sphaeroides, and the enzyme was purified under oxic conditions. The oxygen-sensitive enzyme was partially reactivated under reducing conditions, resulting in a maximal activity of 19.8 μmol H2 oxidized min–1 (mg protein)–1 with benzyl viologen as electron acceptor and an apparent K m value for H2 of 341 μM. The molecular mass of the native protein estimated by native PAGE and gel filtration was 122 and 130 kDa, respectively. SDS-PAGE revealed two polypeptides with molecular masses of 65 and 37 kDa, present in a 1:1 ratio. The native protein contained 15.6 ± 1.7 mol Fe, 11.4 ± 1.4 mol S2–, and 0.6 mol Ni per mol enzyme. The hydrogenase coupled with viologen dyes, but not with other various artificial electron carriers, FAD, FMN, or NAD(P)+. The amino acid sequence of the N-termini of the subunits showed a high degree of similarity to eubacterial membrane-bound uptake hydrogenases. Washed membranes catalyzed a H2-dependent cytochrome b reduction at a rate of 0.18 nmol min–1 (mg protein)–1.
    Type of Medium: Electronic Resource
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