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  • 1
    Keywords: MICROSCOPY ; CELL ; BIOLOGY ; ELECTRON ; ELECTRON-MICROSCOPY ; electron microscopy
    Type of Publication: Book chapter
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  • 2
    Keywords: GROWTH ; IN-VITRO ; CELL ; Germany ; IN-VIVO ; KINASE ; VITRO ; VIVO ; GENE ; GENES ; PROTEIN ; PROTEINS ; RNA ; transcription ; COMPLEX ; DNA ; MESSENGER-RNA ; PHOSPHORYLATION ; ASSOCIATION ; antibodies ; antibody ; MOUSE ; CHROMATIN ; REQUIRES ; LOCALIZATION ; NUCLEUS ; OVEREXPRESSION ; POLYMERASE-I ; RNA-POLYMERASE-I ; MOTOR ; RECOMBINANT ; NUCLEAR ACTIN ; FACTOR TIF-IA ; INITIATION-FACTOR
    Abstract: The presence of actin and nuclear myosin I (NMI) in the nucleus suggests a role for these motor proteins in nuclear functions. We have investigated the role of actin and nuclear myosin I ( NMI) in the transcription of ribosomal RNA genes ( rDNA). Both proteins are associated with rDNA and are required for RNA polymerase I (Pol I) transcription. Microinjection of antibodies against actin or NMI, as well as short interfering RNA-mediated depletion of NMI, decreased Pol I transcription in vivo, whereas overexpression of NMI augmented pre-rRNA synthesis. In vitro, recombinant NMI activated Pol I transcription, and antibodies to NMI or actin inhibited Pol I transcription both on naked DNA and pre-assembled chromatin templates. Whereas actin associated with Pol I, NMI bound to Pol I through the transcription-initiation factor TIF-IA. The association with Pol I requires phosphorylation of TIF-IA at Ser 649 by RSK kinase, indicating a role for NMI in the growth-dependent regulation of rRNA synthesis
    Type of Publication: Journal article published
    PubMed ID: 15558034
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  • 3
    Keywords: CELLS ; EXPRESSION ; Germany ; MODEL ; screening ; GENE ; GENE-EXPRESSION ; PROTEIN ; PROTEINS ; DOMAIN ; CELL-CYCLE ; antibodies ; antibody ; gene expression ; MEMBRANE ; REGION ; EGG EXTRACTS ; MUSCULAR-DYSTROPHY ; DREIFUSS MUSCULAR-DYSTROPHY ; lamin ; LEM DOMAIN ; embryogenesis ; MASSES ; muscular dystrophy ; SINGLE ; molecular ; DEFICIENCY ; Xenopus laevis ; XENOPUS-LAEVIS ; assembly ; C-ELEGANS ; OOCYTES ; LAEVIS ; ENVELOPE ; TRANSMEMBRANE DOMAIN ; early development ; emerin ; NUCLEAR-MEMBRANE PROTEIN ; oocyte ; POLYPEPTIDE 2
    Abstract: Emerin is an integral protein of the inner nuclear membrane in the majority of differentiated vertebrate cells. In humans, deficiency of emerin causes a progressive muscular dystrophy of the Emery-Dreifuss type. The physiological role of emerin is poorly understood. By screening and sequencing of EST clones we have identified two emerin homologues in Xenopus laevis, Xemerin1 and Xemerin2. Xemerins share with mammalian emerins the N-terminal LEM domain and a single transmembrane domain at the C-terminus. As shown by immunoblot analysis with Xemerin-specific antibodies, both proteins have an apparent molecular mass of 24kDa but differ in their isoelectric points. Xemerin1 and Xemerin2 proteins are not detectable in oocytes nor during early embryogenesis. Protein expression is first found at stage 43 and persists in somatic cells. However, RT-PCR and Northern blot analysis show Xemerin mRNAs of similar to 4.0 kb to be present in oocytes and throughout embryogenesis. During embryogenesis the level of Xemerin mRNAs increases at stage 22 and is particularly abundant in mesodermal and neuro-ectodermal regions of the embryo. These data provide the necessary background to further investigate the role of emerin in nuclear envelope assembly, gene expression and organ development of X. laevis as a model organism. (c) 2005 Elsevier GmbH. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 15819409
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  • 4
    Keywords: RECEPTOR ; CELLS ; EXPRESSION ; IN-VITRO ; INHIBITOR ; Germany ; IN-VIVO ; MICROSCOPY ; VITRO ; GENE ; PROTEIN ; PROTEINS ; TISSUE ; ACTIVATION ; kidney ; FAMILY ; DOMAIN ; MOUSE ; Drosophila ; MEMBRANE ; NUMBER ; LINE ; SUPERFAMILY ; Jun ; INVOLVEMENT ; OVEREXPRESSION ; HEALTHY ; ORGANIZATION ; electron microscopy ; BINDS ; INHIBITORS ; ELECTRON-MICROSCOPY ; interaction ; MT1-MMP ; MYOBLAST FUSION ; NEPHROTIC SYNDROME
    Abstract: The NEPH family comprises three transmembrane proteins of the Ig superfamily interacting with the glomerular slit diaphragm proteins podocin and ZO-1. NEPH1 binds to nephrin, another component of the slit diaphragm, and loss of either partner causes heavy proteinuria. NEPH2, which is strongly conserved among a large number of species, is also expressed in the kidney; however, its function is unknown. The authors raised NEPH2 antisera. to demonstrate NEPH2 expression in a variety of mouse tissues, including the kidney and a podocyte cell line. The authors localized the expression of NEPH2 to the glomerular slit diaphragm by electron microscopy and show NEPH2 homodimerization and specific interactions with the extracellular domain of nephrin in vitro and in vivo. NEPH1, however, failed to interact with NEPH2. The authors detected immunoreactive NEPH2 in urine of healthy subjects, suggesting that the extracellular domain is cleaved under physiologic conditions. These findings were confirmed in vitro in podocyte cell. culture. Shedding is increased by tyrosine phosphatase inhibitors and diminished by GM6001, an inhibitor of metalloproteinases. Overexpression experiments indicate an involvement of the MT1-matrix metalloproteinase. The results suggest a role for NEPH2 in the organization and/or maintenance of the glomerular slit diaphragm that may differ from the functions of NEPH1 and nephrin
    Type of Publication: Journal article published
    PubMed ID: 15843475
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  • 5
    Keywords: Germany ; MICROSCOPY ; CT ; DISEASE ; PATIENT ; DNA ; INFECTION ; ASSOCIATION ; bone marrow ; BONE-MARROW ; PCR ; POLYMERASE-CHAIN-REACTION ; electron microscopy ; inflammation ; DEFICIENCY ; ELECTRON-MICROSCOPY ; IRON ; immunofluorescence ; BM ; PERSISTENCE ; sequencing ; anaemia ; CHLAMYDIA-PNEUMONIAE ; Chlamydiales ; Chlamydophila pneumoniae
    Abstract: Anaemia of chronic disease (ACD) is a common finding involving iron deficiency and signs of inflammation. Here, we report on two patients with ACD where a persistent infection with Chlamydophila (Chlamydia) pneumoniae (CP) was detected in bone marrow (BM) biopsies. Infection was suspected by routine cytology and confirmed by immunofluorescence, electron microscopy, polymerase chain reaction (PCR) including different primer sets and laboratories and sequencing of the PCR product. This is a first report of chlamydial presence in the BM of anaemic patients. The cases are presented because persistent chlamydial infection may contribute more frequently to chronic refractory anaemia than previously suspected
    Type of Publication: Journal article published
    PubMed ID: 15613113
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  • 6
    Keywords: CELLS ; Germany ; human ; INHIBITION ; KINASE ; PATHWAY ; DISEASE ; DISEASES ; PROTEIN ; PROTEINS ; kidney ; MECHANISM ; MARKER ; mechanisms ; BINDING ; PHOSPHORYLATION ; ACID ; TRANSPORT ; NUMBER ; MUTATION ; genetics ; MARKERS ; TRAFFICKING ; MUTATIONS ; EPITHELIAL-CELLS ; INTERACTS ; AMINO-ACIDS ; CLUSTER ; targeting ; DISORDERS ; CHILDHOOD ; RESIDUES ; TRANSITION ; AMINO-ACID ; interaction ; INDUCE ; LOSSES ; INTERACT ; cilia ; cystic kidney disease ; INTRAFLAGELLAR TRANSPORT ; KIDNEY-DISEASE ; nephrocystin ; NEPHRONOPHTHISIS ; NPHP1 ; PACS-1 ; TRANS-GOLGI NETWORK
    Abstract: Mutations in proteins localized to cilia and basal bodies have been implicated in a growing number of human diseases. Access of these proteins to the ciliary compartment requires targeting to the base of the cilia. However, the mechanisms involved in transport of cilia proteins to this transitional zone are elusive. Here we show that nephrocystin, a ciliary protein mutated in the most prevalent form of cystic kidney disease in childhood, is expressed in respiratory epithelial cells and accumulates at the base of cilia, overlapping with markers of the basal body area and the transition zone. Nephrocystin interacts with the phosphofurin acidic cluster sorting protein (PACS)-1. Casein kinase 2 (CK2)-mediated phosphorylation of three critical serine residues within a cluster of acidic amino acids in nephrocystin mediates PACS-I binding, and is essential for colocalization of nephrocystin with PACS-1 at the base of cilia. Inhibition of CK2 activity abrogates this interaction and results in the loss of correct nephrocystin targeting. These data suggest that CK2-dependent transport processes represent a novel pathway of targeting proteins to the cilia
    Type of Publication: Journal article published
    PubMed ID: 16308564
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  • 7
    Keywords: RECEPTOR ; CANCER ; CANCER CELLS ; CELLS ; EXPRESSION ; GROWTH ; GROWTH-FACTOR ; CELL ; Germany ; TISSUE ; LINES ; TIME ; FAMILY ; INDUCTION ; TISSUES ; CONTRAST ; CELL-LINES ; DOWN-REGULATION ; MEMBER ; MEMBERS ; PHOSPHORYLATION ; BREAST-CANCER ; antibodies ; antibody ; immunohistochemistry ; ASSAY ; CARCINOMA CELLS ; CELL-LINE ; LINE ; CANCER-CELLS ; BETA ; RT-PCR ; adenocarcinoma ; p21 ; CELL-SURFACE ; RECEPTORS ; DIFFERENTIAL EXPRESSION ; cell lines ; pancreatic cancer ; CELL-GROWTH ; signaling ; PANCREATIC-CANCER ; FAMILIES ; DUCTAL ADENOCARCINOMA ; independent growth ; ENHANCED EXPRESSION ; TGF-beta 1 ; HEPARAN-SULFATE PROTEOGLYCANS ; LEVEL ; pancreatic ; ASSAYS ; SULFATE ; downregulation ; lymph node ; LYMPH-NODE ; correlation ; VIEW ; DECREASED SURVIVAL ; activin ; bone morphogenic protein ; CONTROLS CELLULAR-RESPONSES ; glypican ; heparan sulfate proteoglycans ; SMAD PROTEINS
    Abstract: Glypican 1 (GPC1) is a cell surface heparan sulfate proteoglycan that acts as a co-receptor for heparin-binding growth factors as well as for members of the TGF-beta family. GPC1 plays a role in pancreatic cancer by regulating growth factor responsiveness. In view of the importance of members of the TGF-beta family in pancreatic cancer, in the present study, the role of GPC1 in TGF-beta, BMP and activin signaling was analyzed. Quantitative RT-PCR and immunohistochemistry were utilized to analyze GPC1 and TGF-beta, BMP and activin receptor expression levels. Panc-1 and T3M4 pancreatic cancer cells were transfected in a stable manner with a GPC1 antisense expression construct. Anchorage-dependent and -independent growth was determined by MTT and soft agar assays. TGF-beta 1, activin-A and BMP-2 responsiveness was determined by MTT assays and immunoblotting with p21, p-Smad1, and p-Smad2 antibodies. QRT-PCR demonstrated increased GPC1 mRNA levels in pancreatic ductal adenocarcinoma (PDAC) compared to normal pancreatic tissues (NPT), as described previously. There was a significant correlation between GPC1 mRNA levels and T beta RII, act-R1a, act-R1b, act-R2a, BMP-R1a, and BMP-R2 mRNA expression in NPT. In contrast, GPC1 mRNA expression correlated directly with act-R1a and BMP-R1a in NO PDAC cases and with act-R2a and BMP-R1a in lymph node positive cases. Down-regulation of GPC1 resulted in increased doubling time in Panc-1 but not in T3M4 cells, and decreased anchorage-independent growth in both cell lines. GPC1 down-regulation resulted in a slightly altered response towards TGF-beta 1, activin-A and BMP-2 in terms of growth, p21 induction and Smad2 phosphorylation. In conclusion, enhanced GPC1 expression correlates with BMP and activin receptors in pancreatic cancer. GPC1 down-regulation suppresses pancreatic cancer cell growth and slightly modifies signaling of members of the TGF-beta family of growth factors
    Type of Publication: Journal article published
    PubMed ID: 17016645
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  • 8
    Keywords: CELLS ; EXPRESSION ; IRRADIATION ; proliferation ; carcinoma ; CELL ; COMBINATION ; Germany ; human ; EXPOSURE ; PROTEIN ; PROTEINS ; DIFFERENTIATION ; LINES ; MICE ; MARKER ; CONTRAST ; SKIN ; E7 ; papillomavirus ; ALPHA ; TRANSGENIC MICE ; LESIONS ; NUMBER ; MOUSE SKIN ; LINE ; MARKERS ; p53 ; human papillomavirus ; HPV ; E6 ; BENIGN ; HUMAN KERATINOCYTES ; HUMAN-PAPILLOMAVIRUS ; keratin ; squamous cell carcinoma ; SQUAMOUS-CELL CARCINOMAS ; CLUSTERS ; P53 MUTATIONS ; HIGH-LEVEL ; CLUSTER ; MUTANT P53 ; CELL CARCINOMA ; EPIDERMODYSPLASIA-VERRUCIFORMIS ; LEVEL ; P63 ; E6 PROTEINS ; EPIDERMAL-CELLS ; E6 and E7 ; granular layer ; HPV 20 ; CESSATION ; E7 PROTEIN ; EARLY ADAPTIVE RESPONSES ; ULTRAVIOLET-B-LIGHT
    Abstract: The functional role of UV irradiation, in combination with the E6 and E7 proteins of the cutaneous human papillomavirus (HPV) types in the malignant conversion of benign papillomatous lesions, has not been elucidated. Transgenic SKH-hr1 hairless mice expressing HPV-20 and HPV-27 E6 and E7 proteins in the suprabasal compartment were generated and exposed to chronic UV irradiation. Histological and immunohistochemical examination of skin samples revealed enhanced proliferation of the epidermal layers and papilloma formation in both transgenic strains in comparison to what was observed with nontransgenic mice. Squamous cell carcinoma developed in the HPV-20 E6/E7 transgenic line as well as in the HPV-27 E6/E7 transgenic line. Several weeks after cessation of UV-B exposure, enhanced proliferation, as measured by BrdU incorporation, was maintained only in HPV-20 transgenic skin. Keratin 6 expression was increased in the transgenic mice throughout all cell layers. Expression of the differentiation markers involucrin and loricrin was reduced and disturbed. p63 alpha expression was differentially regulated with high levels of cytoplasmic expression in clusters of cells in the granular layer of the skin in the transgenic lines 20 weeks after cessation of UV-B exposure, in contrast to uninterrupted staining in the nontransgenic lines. p53 was expressed in clusters of cells in nontransgenic and HPV-27 transgenic mice, in contrast to an even distribution in a higher number of cells in HPV-20 transgenic animals
    Type of Publication: Journal article published
    PubMed ID: 16971438
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  • 9
    Keywords: PEPTIDE ; APOPTOSIS ; TUMOR-CELLS ; Germany ; human ; INHIBITION ; PROTEIN ; PROTEINS ; MECHANISM ; DOMAIN ; CYCLE ; virus ; E6 ; ONCOPROTEIN ; REPLICATION ; BODY ; INHIBITORS ; AGGREGATION ; LIFE ; GENETIC SELECTION ; BLOCKS ; function ; SIGNALS ; E6 PROTEIN ; CORE-PROTEIN
    Abstract: Peptide aptamers (PAs) can be employed to block the intracellular function of target proteins. Little is known about the mechanism of PA-mediated protein inhibition. Here, we generated PAs that specifically bound to the duck hepatitis B virus (HBV) core protein. Among them, PA34 strongly blocked duck HBV replication by inhibiting viral capsid formation. We found that PA34 led to a dramatic intracellular redistribution of its target protein into perinuclear inclusion bodies, which exhibit the typical characteristics of aggresomes. As a result, the core protein is efficiently removed from the viral life cycle. Corresponding findings were obtained for bioactive PAs that bind to the HBV core protein or to the human papillomavirus-16 (HPV16) E6 protein, respectively. The observation that PAs induce the specific sequestration of bound proteins into aggresomes defines a novel mechanism as to how this new class of intracellular inhibitors blocks the function of their target proteins
    Type of Publication: Journal article published
    PubMed ID: 16717089
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  • 10
    Keywords: CANCER ; CANCER CELLS ; CELLS ; EXPRESSION ; GROWTH ; tumor ; CELL ; Germany ; human ; PATHWAY ; PATHWAYS ; DISEASE ; DISEASES ; PROTEIN ; PROTEINS ; COMPLEX ; COMPLEXES ; kidney ; MECHANISM ; DYNAMICS ; MOUSE ; NUMBER ; MUTATION ; CANCER-CELLS ; MUTATIONS ; STABILITY ; INTERACTS ; GENE-PRODUCT ; DISORDERS ; TUMOR-SUPPRESSOR ; CDC42 ; cilia ; DEFECT ; POLARITY ; KIDNEY CANCER ; POLARIZATION ; NUCLEATION ; PRIMARY CILIUM
    Abstract: Cilia are specialized organelles that play an important role in several biological processes, including mechanosensation, photoperception, and osmosignaling. Mutations in proteins localized to cilia have been implicated in a growing number of human diseases. In this study, we demonstrate that the von Hippel-Lindau (VHL) protein (pVHL) is a ciliary protein that controls ciliogenesis in kidney cells. Knockdown of pVHL impeded the formation of cilia in mouse inner medullary collecting duct 3 kidney cells, whereas the expression of pVHL in VHL-negative renal cancer cells rescued the ciliogenesis defect. Using green fluorescent protein-tagged end-binding protein 1 to label microtubule plus ends, we found that pVHL does not affect the microtubule growth rate but is needed to orient the growth of microtubules toward the cell periphery, a prerequisite for the formation of cilia. Furthermore, pVHL interacts with the Par3-Par6-atypical PKC complex, suggesting a mechanism for linking polarity pathways to microtubule capture and ciliogenesis
    Type of Publication: Journal article published
    PubMed ID: 17101696
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