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  • PROTEIN  (9)
  • AREA-COMPOSITA  (5)
  • Germany  (4)
  • ARRHYTHMOGENIC CARDIOMYOPATHY  (2)
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  • 1
    Keywords: CELLS ; EXPRESSION ; PROTEIN ; PROTEINS ; EPITHELIA ; KERATINOCYTES ; IDENTIFICATION ; MERKEL CELLS ; MELANOMA-CELLS ; ADHERENS JUNCTIONS ; plakophilin-2 ; Asymmetric junctions ; CONTACTS ; CYTOKERATIN ; Heterotypic junctions ; HUMAN-FETAL SKIN
    Abstract: Merkel cells (MCs) are special neuroendocrine epithelial cells that occur as individual cells or as cell groups within the confinements of a major epithelium formed and dominated by other epithelial cells. In the epidermis and some of its appendages MCs are mostly located in the basal cell layer, occasionally also in suprabasal layers and generally occur in linear arrays in outer root sheath cell layers of hair follicles. As MCs are connected to the adjacent keratinocytes by a series of adhering junctions (AJs), of which the desmosomes are the most prominent, these junctions represent heterotypic cell-cell connections, i.e. a kind of structure not yet elucidated in molecular terms. Therefore, we have studied these AJs in order to examine the molecular composition of the desmosomal halves. Using light- and electron-microscopic immunolocalization and keratin 20 as the MC-specific cell type marker we show that the plaques of the MC half of the desmosomes specifically and constitutively contain plakophilin Pkp2. This protein, however, is absent in the keratinocyte half of such heterotypic desmosomes which instead contains Pkp1 and/or Pkp3. We discuss the developmental, tissue-architectonic and functional importance of such asymmetric junctions in normal physiology as well as in diseases, in particular in the formation of distant tumor cell metastasis.
    Type of Publication: Journal article published
    PubMed ID: 22006253
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  • 2
    Keywords: RIGHT-VENTRICULAR CARDIOMYOPATHY ; DESMOPLAKIN-CONTAINING JUNCTIONS ; adhering junctions ; INTERCALATED DISC ; HEART-MUSCLE CELLS ; AREA-COMPOSITA ; PROTEIN PHOSPHATASE 2A ; ARRHYTHMOGENIC CARDIOMYOPATHY ; CALMODULIN-BINDING PROTEIN ; SODIUM CURRENT DEFICIT
    Abstract: Proteins of the striatin family (striatins 1-4; sizes ranging from 90 to 110 kDa on SDS-polyacrylamide gel electrophoresis) are highly homologous in their amino acid sequences but can differ in their cell-type-specific gene expression patterns and biological functions. In various cell types, we have found one, two or three polypeptides of this evolutionarily old and nearly ubiquitous family of proteins known to serve as scaffold proteins for diverse protein complexes. Light and electron microscopic immunolocalization methods have revealed striatins in mammalian cell-cell adherens junctions (AJs). In simple epithelia, we have localized striatins as constitutive components of the plaques of the subapical zonulae adhaerentes of cells, including intestinal, glandular, ductal and urothelial cells and hepatocytes. Striatins colocalize with E-cadherin or E-N-cadherin heterodimers and with the plaque proteins alpha- and beta-catenin, p120 and p0071. In some epithelia and carcinomas and in cultured cells derived therefrom, striatins are also seen in lateral AJs. In stratified epithelia and in corresponding squamous cell carcinomas, striatins can be found in plaques of some forms of tessellate junctions. Moreover, striatins are major plaque proteins of composite junctions (CJs; areae compositae) in the intercalated disks connecting cardiomyocytes, colocalizing with other CJ molecules, including plectin and ankyrin-G. We discuss the "multimodulator" scaffold roles of striatins in the initiation and regulation of the formation of various complex particles and structures. We propose that striatins are included in the diagnostic candidate list of proteins that, in the CJs of human hearts, can occur in mutated forms in the pathogeneses of hereditary cardiomyopathies, as seen in some types of genetically determined heart damage in boxer dogs.
    Type of Publication: Journal article published
    PubMed ID: 25501894
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  • 3
    Keywords: brain ; CELLS ; ENDOTHELIAL-CELLS ; EXPRESSION ; IN-VITRO ; CELL ; Germany ; human ; MODEL ; VITRO ; GENE ; GENES ; PROTEIN ; cell line ; TISSUE ; MARKER ; BIOLOGY ; E7 ; immunohistochemistry ; resistance ; CELL-LINE ; LINE ; human papillomavirus ; E6 ; HUMAN-PAPILLOMAVIRUS ; MORPHOLOGY ; BARRIER FUNCTION ; TIGHT JUNCTIONS ; CONJUGATE EXPORT PUMP ; MRP2 ; ORIGIN ; RE ; TRANSFECTION ; P-GLYCOPROTEIN ; blood-brain barrier ; human brain ; ENDOTHELIAL-CELL ; brain capillary endothelial cell ; ATP-BINDING ; BLOOD-BRAIN ; ABC-TRANSPORTERS ; DRUG EFFLUX TRANSPORTERS ; endothelial markers
    Abstract: Primary human brain capillary endothelial cells (hBCECs) are available only in small quantities and have a short life span in vitro; this restricts their use as in vitro model for the blood-brain barrier (BBB). To overcome these limitations, we have established an immortalized hBCEC line (NKIM-6) by transfection with pLXSN16-E6E7, which encodes the human papillomavirus type 16 E6 and E7 genes. The cell line exhibits an extended life span in vitro and retains its characteristic endothelial morphology, endothelial markers, and physiology. Likewise, as demonstrated by immunohistochemistry and reverse transcription/polymerase chain reaction (RT-PCR), NKIM-6 cells express BBB markers, and the lack of glial, neuronal, and epithelial markers confirms their endothelial origin. Moreover, with quantitative RT-PCR, we have been able to demonstrate that several ATP-binding cassette-transporters are expressed in NKIM-6 cells with a conserved expression order compared with primary hBCECs. Our results suggest that this cell line might be suitable as in vitro model for several aspects of the BBB
    Type of Publication: Journal article published
    PubMed ID: 17180596
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  • 4
    Keywords: PROTEIN ; TISSUE ; FUSION ; MUTATIONS ; review ; EMBRYONIC HEART ; RIGHT-VENTRICULAR CARDIOMYOPATHY ; desmosomes ; MOLECULAR-GENETICS ; ADHERENS JUNCTIONS ; WOOLLY HAIR ; intercalated disk ; PLAKOPHILIN-2 MUTATIONS ; SUDDEN-DEATH ; Arrhythmogenic ventricular cardiomyopathy ; CARDIAC RYANODINE RECEPTOR ; Carvajal disease ; Composite junction ; GENOTYPE-PHENOTYPE ASSESSMENT ; Naxos disease ; PALMOPLANTAR KERATODERMA ; PLAKOGLOBIN-DEFICIENT MICE
    Abstract: In the past decade, an avalanche of findings and reports has correlated arrhythmogenic ventricular cardiomyopathies (ARVC) and Naxos and Carvajal diseases with certain mutations in protein constituents of the special junctions connecting the polar regions (intercalated disks) of mature mammalian cardiomyocytes. These molecules, apparently together with some specific cytoskeletal proteins, are components of (or interact with) composite junctions. Composite junctions contain the amalgamated fusion products of the molecules that, in other cell types and tissues, occur in distinct separate junctions, i.e. desmosomes and adherens junctions. As the pertinent literature is still in an expanding phase and is obviously becoming important for various groups of researchers in basic cell and molecular biology, developmental biology, histology, physiology, cardiology, pathology and genetics, the relevant references so far recognized have been collected and are presented here in the following order: desmocollin-2 (Dsc2, DSC2), desmoglein-2 (Dsg2, DSG2), desmoplakin (DP, DSP), plakoglobin (PG, JUP), plakophilin-2 (Pkp2, PKP2) and some non-desmosomal proteins such as transmembrane protein 43 (TMEM43), ryanodine receptor 2 (RYR2), desmin, lamins A and C, striatin, titin and transforming growth factor-beta 3 (TGF beta 3), followed by a collection of animal models and of reviews, commentaries, collections and comparative studies
    Type of Publication: Journal article published
    PubMed ID: 22450909
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  • 5
    Keywords: brain ; CELLS ; EXPRESSION ; IN-VITRO ; SURVIVAL ; AGENTS ; Germany ; MODEL ; THERAPY ; GENE ; PROTEIN ; PROTEINS ; gene therapy ; MICE ; TUMOR-NECROSIS-FACTOR ; IFN-GAMMA ; INFECTION ; ALPHA ; culture ; MOUSE ; VECTOR ; NECROSIS-FACTOR-ALPHA ; CELL-LINE ; LINE ; MINUTE VIRUS ; REPLICATION ; MOUSE MODEL ; INTERFERON ; sensitivity ; autonomous parvovirus ; mannose receptor ; CYTOTOXICITY ; FACTOR-ALPHA ; BRAIN-TUMORS ; CAPACITY ; GLIOMA ; parvovirus ; VIRIONS ; FUNCTIONAL-CHARACTERIZATION ; astrocytoma ; uptake ; CANDIDATE ; glial cells ; IMMUNE FUNCTION ; lipopolysaccharide ; MICROGLIAL CELLS
    Abstract: The sensitivity of brain tumour cells to wild-type or recombinant parvoviruses H1-PV and MVMp makes these agents promising candidates for gene therapy of astrocytoma. This application raises the question of whether parvoviruses exert deleterious or bystander effects on normal glial cells surrounding tumours. We addressed this question in the mouse model by using cell cultures derived from BALB/c, C57BL/6 and VM/Dk strains. Astrocytes and a large proportion of microglia cultures were competent for MVMp uptake. Infection was, however, abortive as replication-associated viral proteins synthesis took place in less than 10% of astrocytes and no progeny virions were produced. This restriction was even more pronounced for microglia in which no viral protein expression could be detected, save for a minute fraction of VM/Dk-derived cells. Infection with MVMp had no significant effect on glial cell survival and did not interfere with their immune potential. Indeed, neither the lipopolysaccharide (LPS)/interferon (IFN-gamma)-induced cytotoxicity of VM/Dk-derived microglia towards the mouse glioma (MT539MG) cell line, nor the glial cells capacity for tumour necrosis factor alpha production upon LPS stimulation or LPS/IFN-gamma stimulation were affected by infection with MVMp. Moreover, stimulation with LPS and/or IFN-gamma resulted in a decreased expression of the viral replicative and cytotoxic protein NS1. Together, our data indicate that, in the natural host, a majority of normal glial cells are not competent for MVMp replication and that the abortive infection taking place in a minor fraction of these cells fails to impede their survival and immunocompetence, giving credit to the consideration of autonomous parvoviruses for glioma therapy
    Type of Publication: Journal article published
    PubMed ID: 16699801
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  • 6
    Keywords: immunohistochemistry ; ADHESION ; TIGHT JUNCTIONS ; HUMAN EPIDERMIS ; desmosomes ; STRATIFIED EPITHELIA ; ADHERENS JUNCTIONS ; cardiomyocytes ; HEART-MUSCLE CELLS ; plakophilin-2 ; AREA-COMPOSITA ; VERTEBRATES ; Epithelial cells ; Junction plaques ; Protein myozap
    Abstract: The protein myozap, a polypeptide of 54 kDa, has recently been identified as a component of the cytoplasmic plaques of the composite junctions (areae compositae) in the myocardiac intercalated disks and of the adherens junctions (AJs) in vascular endothelia. Now we report that using very sensitive new antibodies and drastic localization methods, we have also identified this protein as a component of the AJ plaques in simple and complex epithelia, in the adluminal cell layer of the transitional epithelium of the urinary tract and in certain cell layers of diverse stratified epithelia, including gingiva, tongue, pharynx and esophagus, cervix, vagina and epidermis. Myozap has not been identified in desmosomal and tight junction plaques. We have also detected protein myozap in AJ structures of carcinomas. The discovery of a novel major protein in AJ plaques now calls for re-examinations of molecular interactions in AJ formation and maintenance and also offers a new marker for diagnostic immunocytochemistry. We also discuss the need for progressive unravelling, extractive treatments and buffer rinses of sections and cultured cells to reveal obscured or masked antigens, before definitive negative conclusions in immunohistochemistry can be made.
    Type of Publication: Journal article published
    PubMed ID: 22160502
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  • 7
    Keywords: TISSUE ; TUMORS ; EXTRACELLULAR-MATRIX ; RIGHT-VENTRICULAR CARDIOMYOPATHY ; ADHERENS JUNCTIONS ; adhering junctions ; MESENCHYMAL STEM-CELLS ; plakophilin-2 ; AREA-COMPOSITA ; Puncta adhaerentia ; RECESSIVE MUTATION ; Heart valves ; MUSCLE CELLS ; PORCINE AORTIC-VALVE ; ATRIOVENTRICULAR VALVES ; CARDIAC-VALVE ; CUSHION DEVELOPMENT ; Myxomata ; Valvular interstitial cells
    Abstract: The interstitial cells of cardiac valves represent one of the most frequent cell types in the mammalian heart. In order to provide a cell and molecular biological basis for the growth of isolated valvular interstitial cells (VICs) in cell culture and for the use in re-implantation surgery we have examined VICs in situ and in culture, in fetal, postnatal and adult hearts, in re-associations with scaffolds of extracellular matrix (ECM) material and decellularized heart valves. In all four mammalian species examined (human, bovine, porcine and ovine), the typical mesenchymal-type cell-cell adherens junctions (AJs) connecting VICs appear as normal N-cadherin based puncta adhaerentia. Their molecular ensemble, however, changes under various growth conditions insofar as plakophilin-2 (Pkp2), known as a major cytoplasmic plaque component of epithelial desmosomes, is recruited to and integrated in the plaques of VIC-AJs as a major component under growth conditions characterized by enhanced proliferation, i.e., in fetal heart valves and in cell cultures. Upon re-seeding onto decellularized heart valves or in stages of growth in association with artificial scaffolds, Pkp2 is - for the most part - lost from the AJs. As Pkp2 has recently also been detected in AJs of cardiac myxomata and diverse other mesenchymal tumors, the demonstrated return to the normal Pkp2-negative state upon re-association with ECM scaffolds and decellularized heart valves may now provide a safe basis for the use of cultured VICs in valve replacement surgery. Even more surprising, this type of transient acquisition of Pkp2 has also been observed in distinct groups of endothelial cells of the endocardium, where it seems to correspond to the cell type ready for endothelial-mesenchymal transition (EMT)
    Type of Publication: Journal article published
    PubMed ID: 22290634
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  • 8
  • 9
  • 10
    Keywords: PEPTIDE ; CELLS ; EXPRESSION ; Germany ; human ; KINASE ; MICROSCOPY ; NEW-YORK ; PROTEIN ; PROTEINS ; cell line ; TISSUE ; FAMILY ; ACTIVATED PROTEIN-KINASE ; PHOSPHORYLATION ; treatment ; cell culture ; ACIDS ; antibodies ; antibody ; MAP KINASE ; DISRUPTION ; PLASMA ; MEMBRANE ; STRESS ; LOCALIZATION ; CHROMATOGRAPHY ; AMINO-ACIDS ; PHORBOL-ESTER ; serine ; CHANNEL ; GAP-JUNCTIONAL COMMUNICATION ; growth factors ; hyperosmosis ; INTERCELLULAR COMMUNICATION ; LIVER EPITHELIAL-CELLS ; plasma membranes ; sorbitol ; threonine phosphorylation
    Abstract: We have developed polyclonal antibodies (SA226P) to a peptide of the human connexin43 (Cx43) protein between amino acids 271 and 288 containing phosphorylated S279 and S282. Antibodies specific for the phosphorylated form of the peptide were isolated by double immunoaffinity chromatography and were characterised using proteins of the cell line WB-F344, known to contain large amounts of Cx43. SA226P recognises specifically the slowest migrating Cx43 band in immunoblots of proteins isolated from untreated cells. In immunofluorescence experiments SA226P scarcely stains the plasma membrane in untreated cells in contrast to a commercial antibody recognising all isoforms of the Cx43 protein. EGF or stress treatment of the cells results in a rapid increase in the phosphorylated forms of Cx43 as revealed by immunoblotting. Immunofluorescence experiments reveal that both phosphorylated and non-phosphorylated Cx43 could be found at the plasma membrane. Whether phosphorylation of S279/S282 takes place before or after incorporation of Cx43 into the membranes is so far unknown. More interestingly, confocal microscopy using our antibodies and a commercial antibody recognising all isoforms of Cx43 shows the coexistence of differentially phosphorylated forms of the protein at the plasma membrane. Our results indicate that MAP kinases erk1/2 are mainly responsible for this phosphorylation, as already published. Nevertheless, treatment of the cells with anisomycin, known to activate stress kinase p38 but not erk1/2, also results in a weak but reproducible Cx43 phosphorylation
    Type of Publication: Journal article published
    PubMed ID: 12483281
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