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  • 1
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  126. Kongress der Deutschen Gesellschaft für Chirurgie; 20090428-20090501; München; DOC09dgch11255 /20090423/
    Publication Date: 2009-05-06
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 2
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    German Medical Science; Düsseldorf, Köln
    In:  Evidenzbasierte Medizin - Anspruch und Wirklichkeit; 102. Jahrestagung der Deutschen Ophthalmologischen Gesellschaft; 20040923-20040926; Berlin; DOC04dogP 012 /20040922/
    Publication Date: 2004-09-21
    Keywords: ddc: 610
    Language: English
    Type: conferenceObject
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  • 3
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  43. Jahrestagung der Deutschen Gesellschaft der Plastischen, Rekonstruktiven und Ästhetischen Chirurgen (DGPRÄC), 17. Jahrestagung der Vereinigung der Deutschen Ästhetisch-Plastischen Chirurgen (VDÄPC); 20120913-20120915; Bremen; DOCFTIP11 /20120910/
    Publication Date: 2012-09-11
    Keywords: ddc: 610
    Language: German
    Type: conferenceObject
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  • 4
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    German Medical Science GMS Publishing House; Düsseldorf
    In:  59. Jahrestagung der Deutschen Gesellschaft für Neurochirurgie e.V. (DGNC), 3. Joint Meeting mit der Italienischen Gesellschaft für Neurochirurgie (SINch); 20080601-20080604; Würzburg; DOCDI.03.06 /20080530/
    Publication Date: 2008-05-30
    Keywords: Apoptosis ; Glioblastoma therapy ; Redox regulation ; Apoptose ; Glioblastom-Therapie ; Redox-Regulation ; ddc: 610
    Language: English
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  • 5
    Keywords: PEPTIDE ; SPECTRA ; Germany ; DIAGNOSIS ; DISEASE ; GENE ; HEART ; PATIENT ; COMPLEX ; COMPLEXES ; SERA ; BIOLOGY ; MOLECULAR-BIOLOGY ; ACID ; PROGRESSION ; MUTATION ; MUTATIONS ; INVOLVEMENT ; SCINTIGRAPHY ; FAILURE ; DIMER ; DILATED CARDIOMYOPATHY ; RELATIVES ; BIOPSY ; SERUM ; molecular biology ; molecular ; VARIANT ; INCREASE ; HEART-FAILURE ; LEVEL ; analysis ; function ; Male ; ONSET ; SPECTRUM ; SUBSTITUTION ; cardiomyopathies ; CARDIOMYOPATHY ; THICKNESS ; ENGLAND ; BIOPSIES ; systemic ; MEDICINE ; amyloidosis ; DYSFUNCTION ; SYSTEMIC AMYLOIDOSIS ; cardiac amyloidosis ; PREALBUMIN ; transthyretin
    Abstract: A 63-year-old Caucasian male, diagnosed with dilated cardiomyopathy in 1993, remained clinically stable for several years. In 2003, a marked increase of N-terminal pro-natriuretic peptide serum level (611 ng/ml to 4926 ng/ml) was observed; left ventricular (IN) septum thickness was 10 mm. In addition, sensorimotor polyneuropathy and autonomic dysfunction occurred. Further progression of heart failure occurred despite unchanged systolic LV function. Endomyocardial biopsy in 2006 revealed transthyretin amyloidosis by Congo red and immunohistochemical staining, as well as Val94Ala substitution by transthyretin gene analysis. Cardiac amyloid deposition was quantified by technetium-99m-3,3-diphosphono-1,2-propanodicarboxylic acid (Tc-99m-DPD) scintigraphy. Mutational search of the relatives (n= 1) was unremarkable. The transthyretin Val94Ala mutation is characterized by sensorimotor polyneuropathy, autonomic dysfunction, and gastrointestinal and cardiac involvement with amyloid. This mutation is an addition to the growing spectrum of transthyretin mutations with late onset of clinical symptoms, but noteworthy because of progressive, finally disabling disease course. Final clinical assessment of severity of cardiac involvement in the present patient is rendered complex by possible concomitant or preceding idiopathic dilated cardiomyopathy
    Type of Publication: Journal article published
    PubMed ID: 17968688
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  • 6
    Keywords: brain ; SPECTRA ; CELLS ; IN-VITRO ; tumor ; AGENTS ; CELL ; human ; MODEL ; VITRO ; DISEASE ; TUMORS ; MICE ; ACTIVATION ; LIGAND ; BINDING ; SUPPRESSION ; MOLECULE ; RECOGNITION ; ACID ; GLYCOPROTEIN ; PATHOGENESIS ; DOSE-RESPONSE ; LIGANDS ; EPITHELIAL-CELLS ; specificity ; DMBT1 ; AGENT ; AGGREGATION ; MOTIF ; PRODUCTS ; brain tumor ; BRAIN-TUMORS ; COLITIS ; interaction ; SODIUM ; pattern recognition ; structure ; brain tumors ; LPS ; Genetic ; genetic study ; BRAIN-TUMOR ; A
    Abstract: Deleted in malignant brain tumors 1 (DMBT1) is a secreted glycoprotein displaying a broad bacterial-binding spectrum. Recent functional and genetic studies linked DMBT1 to the suppression of LPS-induced TLR4-mediated NF-kappaB activation and to the pathogenesis of Crohn's disease. Here, we aimed at unraveling the molecular basis of its function in mucosal protection and of its broad pathogen-binding specificity. We report that DMBT1 directly interacts with dextran sulfate sodium (DSS) and carrageenan, a structurally similar sulfated polysaccharide, which is used as a texturizer and thickener in human dietary products. However, binding of DMBT1 does not reduce the cytotoxic effects of these agents to intestinal epithelial cells in vitro. DSS and carrageenan compete for DMBT1-mediated bacterial aggregation via interaction with its bacterial-recognition motif. Competition and ELISA studies identify poly-sulfated and poly-phosphorylated structures as ligands for this recognition motif, such as heparansulfate, LPS, and lipoteichoic acid. Dose-response studies in Dmbt1(-/-) and Dmbt1(+/+) mice utilizing the DSS-induced colitis model demonstrate a differential response only to low but not to high DSS doses. We propose that DMBT1 functions as pattern-recognition molecule for poly-sulfated and poly-phosphorylated ligands providing a molecular basis for its broad bacterial-binding specificity and its inhibitory effects on LPS-induced TLR4-mediated NF-kappaB activation.
    Type of Publication: Journal article published
    PubMed ID: 19189310
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  • 7
    Keywords: EXPRESSION ; CELL ; Germany ; human ; GENE ; GENES ; PROTEIN ; PROTEINS ; DIFFERENTIATION ; DOMAIN ; CONTRAST ; MEMBERS ; antibodies ; antibody ; PATTERNS ; REGION ; keratin ; TERMINAL DIFFERENTIATION ; CUTICLE CELLS ; GENE DOMAIN ; human hair follicle ; MAMMALIAN-TISSUES ; FOLLICLE ; INNER-ROOT-SHEATH ; RE ; keratins ; HAIR FOLLICLE ; hair ; hair keratins ; GENE FAMILY ; EPITHELIAL CYTOKERATINS ; EXPRESSION PATTERNS ; HUMAN ANAGEN HAIR ; EPITHELIAL KERATINS ; I KERATINS
    Abstract: The recent elucidation of the human type I keratin gene domain allowed the completion of the so far only partially characterized subcluster of type I keratin genes, KRT25-KRT28 (formerly KRT25A-KRT25D), representing he counterparts of the type II inner root sheath (IRS) keratin genes, KRT71-KRT74 (encoding proteins K71-K74, formerly K6irs1-K6irs4). Here, we describe the expression patterns of the type I IRS keratin proteins K25-K28 (formerly K25irs1-K25irs4) and their mRNAs. We found that K25 (K25irs1), K27 (K25irs3), and K28 (K25irs4) occur in the Henle layer, the Huxley layer, and in the IRS cuticle. Their expression extends from the bulb region up to the points of terminal differentiation of the three layers. In contrast, K26 (K25irs2) is restricted to the upper IRS cuticle. Apart from the three IRS layers, K25 (K25irs1), K27 (K25irs3), and K28 ( K25irs4) are also present in the hair medulla. Based on previous, although controversial claims of the occurrence in the IRS of various ''classical'' epithelial keratins, we undertook a systematic study using antibodies against the presently described human epithelial and hair keratins and show that the type I keratins K25-K28 (K25irs1-K25irs4) and the type II keratins K71-K74 (K6irs1-K6irs4) represent the IRS keratins of the human hair follicle
    Type of Publication: Journal article published
    PubMed ID: 16874310
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  • 8
    Keywords: brain ; RECEPTOR ; CELLS ; EXPRESSION ; IN-VITRO ; INVASION ; tumor ; CELL ; Germany ; VITRO ; DISEASE ; GENE ; PROTEIN ; PROTEINS ; COMPONENTS ; TUMORS ; PATIENT ; NF-KAPPA-B ; ACTIVATION ; COMPLEX ; COMPLEXES ; BINDING ; RECOGNITION ; TARGET ; MUTATION ; COMPONENT ; LINE ; MUTATIONS ; EPITHELIAL-CELLS ; FACTOR-KAPPA-B ; NF-kappa B ; TNF-ALPHA ; SALIVARY AGGLUTININ ; SURFACTANT PROTEIN-D ; INFLAMMATORY-BOWEL-DISEASE ; MALIGNANT BRAIN-TUMORS ; SCAVENGER RECEPTOR ; CYTOKINE ; BRAIN-TUMORS ; STREPTOCOCCUS-MUTANS ; secretion ; PATHOGENS ; USA ; function ; immunology ; INHIBIT ; CYSTEINE-RICH DOMAINS ; DYSFUNCTION ; PURPLE SEA-URCHIN ; SEROTYPE-C STRAIN
    Abstract: Mucosal epithelial cell layers are constantly exposed to a complex resident microflora. Deleted in malignant brain tumors 1 (DMBT1) belongs to the group of secreted scavenger receptor cysteine-rich proteins and is considered to be involved in host defense by pathogen binding. This report describes the regulation and function of DMBT1 in intestinal epithelial cells, which form the primary immunological barrier for invading pathogens. We report that intestinal epithelial cells up-regulate DMBT1 upon proinflammatory stimuli (e.g., TNF-alpha, LPS). We demonstrate that DMBT1 is a target gene for the intracellular pathogen receptor NOD2 via NF-kappa B activation. DMBT1 is strongly up-regulated in the inflamed intestinal mucosa of Crohn's disease patients with wild-type, but not with mutant NOD2. We show that DMBT1 inhibits cytoinvasion of Salmonella enterica and LPS- and muramyl dipeptide-induced NF-kappa B activation and cytokine secretion in vitro. Thus, DMBT1 may play an important role in the first line of mucosal defense conferring immune exclusion of bacterial cell wall components. Dysregulated intestinal DMBT1 expression due to mutations in the NOD2/CARD15 gene may be part of the complex pathophysiology of barrier dysfunction in Crohn's disease
    Type of Publication: Journal article published
    PubMed ID: 17548659
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  • 9
    Keywords: brain ; CANCER ; CELLS ; EXPRESSION ; tumor ; TUMOR-CELLS ; carcinoma ; CELL ; Germany ; human ; IN-VIVO ; LUNG ; VIVO ; COMMON ; lung cancer ; LUNG-CANCER ; NEW-YORK ; GENE ; GENOME ; EPITHELIA ; TISSUE ; TUMORS ; MICE ; INDUCTION ; TISSUES ; DOWN-REGULATION ; BREAST ; breast cancer ; BREAST-CANCER ; MOUSE ; IN-SITU ; UP-REGULATION ; MUTATION ; EXTRACELLULAR-MATRIX ; MUTATIONS ; SUPERFAMILY ; EPITHELIAL-CELLS ; GLANDS ; BEHAVIOR ; LUNG-CARCINOMA ; TERMINAL DIFFERENTIATION ; galectin-3 ; MALIGNANT BRAIN-TUMORS ; SCAVENGER RECEPTOR ; MATRIX ; AGGLUTININ
    Abstract: Deleted in malignant brain tumors 1 (DIMBT1) has been proposed as a candidate tumor suppressor for brain and epithelial cancer. Initial studies suggested loss of expression rather than mutation as the predominant mode of DMBT1 inactivation. However, in situ studies in lung cancer demonstrated highly sophisticated changes of DMBT1 expression and localization, pointing to a chronological order of events. Here we report on the investigation of DMBT1 in breast cancer in order to test whether these principles might also be attributable to other tumor types. Comprehensive mutational analyses did not uncover unambiguous inactivating DMBT1 mutations in breast cancer. Expression analyses in the human and mouse mammary glands pointed to the necessity of DMBT1 induction. While age-dependent and hormonal effects could be ruled out, 9 of 10 mice showed induction of Dmbt1 expression after administration of the carcinogen 7,12-dimethybenz(alpha)anthracene prior to the onset of tumorigenesis or other histopathological changes. DMBT1 displayed significant up-regulation in human tumor-flanking tissues compared to in normal breast tissues (P 〈 0.05). However, the breast tumor cells displayed a switch from lumenal secretion to secretion to the extracellular matrix and a significant down-regulation compared to that in matched normal flanking tissues (P 〈 0.01). We concluded that loss of expression also is the predominant mode of DMBT1 inactivation in breast cancer. The dynamic behavior of DMBT1 in lung carcinoma is fully reflected in breast cancer, which suggests that this behavior might be common to tumor types arising from monolayered epithelia. (C) 2003 Wiley-Liss, Inc
    Type of Publication: Journal article published
    PubMed ID: 14732920
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  • 10
    Keywords: brain ; RECEPTOR ; CELLS ; EXPRESSION ; tumor ; CELL ; Germany ; IN-VIVO ; VIVO ; DISEASE ; RISK ; GENOME ; HYBRIDIZATION ; PROTEIN ; SAMPLE ; TISSUE ; TUMORS ; MICE ; PATIENT ; DOMAIN ; GENETIC POLYMORPHISMS ; TISSUES ; polymorphism ; POLYMORPHISMS ; SUSCEPTIBILITY ; DELETION ; IN-SITU ; prevention ; immunohistochemistry ; UP-REGULATION ; NUMBER ; PATHOGENESIS ; DISPLAY ; HUMAN GENOME ; SURFACE ; EPITHELIAL-CELLS ; genetic polymorphism ; NORMAL TISSUE ; CHAIN-REACTION ; SMALL-INTESTINE ; ULCERATIVE-COLITIS ; TERMINAL DIFFERENTIATION ; inflammation ; SALIVARY AGGLUTININ ; SURFACTANT PROTEIN-D ; INFLAMMATORY-BOWEL-DISEASE ; MALIGNANT BRAIN-TUMORS ; SCAVENGER RECEPTOR ; in situ hybridization ; CHAIN ; BRAIN-TUMORS ; pathogen ; VARIANT ; ALLELE ; inflammatory bowel disease ; LEVEL ; methods ; SUBTYPES ; SULFATE ; USA ; function ; INCREASED RISK ; odds ratio ; in vivo ; case control ; quantitative ; MUCOSAL ; EXONS ; CRP-DUCTIN ; DEXTRAN SULFATE SODIUM
    Abstract: Background & Aims: Impaired mucosal. defense plays an important role in the pathogenesis of Crohn's disease (CD), one of the main subtypes of inflammatory bowel disease (IBD). Deleted in malignant brain tumors 1(DMBT1) is a secreted scavenger receptor cysteine-rich protein with predominant expression in. the intestine and has been proposed to exert possible functions in regenerative processes and pathogen defense. Here, we aimed at analyzing the role of DMBT1 in IBD. Methods: We studied DMBT1 expression in IBD and normal tissues by quantitative reverse transcription-polymerase chain reaction, immunohistochemistry, and mRNA in situ hybridization. Genetic polymorphisms within DMBT1 were analyzed in an Italian IBD case-control sample. Dmbt1(-/-) mice were generated, characterized, and analyzed for their susceptibility to dextran sulfate sodium-induced colitis. Results: DMBT1 levels correlate with disease activity in inflamed IBD tissues. A highly significant fraction of the patients with IBD displayed up-regulation of DMBT1 specifically in the intestinal epithelial surface cells and Paneth cells. A deletion allele of DMBT1 with a reduced: number of scavenger receptor cysteine-rich domain coding exons is associated with an increased risk of CD (P =.00056; odds ratio, 1.75) but not for ulcerative colitis. Dmbt1(-/-) mice display enhanced susceptibility to dextran sulfate sodium-induced colitis and elevated Tnf, Il6, and Nod2 expression levels during inflammation. Conclusions: DMBT1 may play a role in intestinal mucosal protection and prevention of inflammation. Impaired DMBT1 function may contribute to the pathogenesis of CD
    Type of Publication: Journal article published
    PubMed ID: 17983803
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