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  • 1
    Online Resource
    Online Resource
    Growth, lifetime, directional movement and myosin-dependent motility of mutant keratin granules in cultured cells
    Springer Science and Business Media LLC ; 2021
    In:  Scientific Reports Vol. 11, No. 1 ( 2021-01-27)
    Details
    In: Scientific Reports, Springer Science and Business Media LLC, Vol. 11, No. 1 ( 2021-01-27)
    Abstract: Intermediate filament polypeptides (IFPs) are prominent components of cytoplasmic aggregates, which are pathognomonic for multiple diseases. Recent observations in cultured cells suggest that they are dynamic and subject to regulated turnover. The emerging concept is that multiple factors contribute to motility and turnover of IFP-containing aggregates. To understand their relative contribution, quantitative tools are needed. The current study addresses this need using epithelial cells producing mutant keratin IFPs that have been identified as the cause of the hereditary blister-forming skin disease epidermolysis bullosa simplex . Digital image analysis of individual granules allowed mapping of their complete life cycle, with information on multiple characteristics at any given time-point. The deduced signet features revealed rapid granule fusion and directed transport from the periphery towards the cell centre, and a limited, ~ 30 min lifetime with a slow, continuous growth phase followed by fast disassembly. As paradigmatic proof-of-principle, we demonstrate that inhibition of myosin II selectively reduces granule movement, linking keratin granule motility to retrograde cortical acto-myosin flow. The newly developed methods and established parameters will help in the characterization of known and the identification of novel regulators of IFP-containing aggregates.
    Type of Medium: Online Resource
    ISSN: 2045-2322
    URL: Article
    DOI: 10.1038/s41598-021-81542-8
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2021
    detail.hit.zdb_id: 2615211-3
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  • 2
    Online Resource
    Online Resource
    Identification of amino acid sequence motifs in desmocollin, a desmosomal glycoprotein, that are required for plakoglobin binding and plaque formation.
    Proceedings of the National Academy of Sciences ; 1994
    In:  Proceedings of the National Academy of Sciences Vol. 91, No. 23 ( 1994-11-08), p. 10790-10794
    Details
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 91, No. 23 ( 1994-11-08), p. 10790-10794
    Abstract: By transfecting epithelial cells with gene constructs encoding chimeric proteins of the transmembrane part of the gap junction protein connexin 32 in combination with various segments of the cytoplasmic part of the desmosomal cadherin desmocollin 1a, we have determined that a relatively short sequence element is necessary for the formation of desmosome-like plaques and for the specific anchorage of bundles of intermediate-sized filaments (IFs). Deletion of as little as the carboxyl-terminal 37 aa resulted in a lack of IF anchorage and binding of the plaque protein plakoglobin, as shown by immunolocalization and immunoprecipitation experiments. In addition, we show that the sequence requirements for the recruitment of desmoplakin, another desmosomal plaque protein, differ and that a short (10 aa) segment of the desmocollin 1a tail, located close to the plasma membrane, is also required for the binding of plakoglobin, as well as of desmoplakin, and also for IF anchorage. The importance of the carboxyl-terminal domain, homologous in diverse types of cadherins, is emphasized, as it must harbor, in a mutually exclusive pattern, the information for assembly of the IF-anchoring desmosomal plaque in desmocollins and for formation of the alpha-/beta-catenin- and vinculin-containing, actin filament-anchoring plaque in E- and N-cadherin.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    URL: Article
    DOI: 10.1073/pnas.91.23.10790
    RVK:
    TA 1000
    RVK:
    WA 15000
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 1994
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Synaptophysin: molecular organization and mRNA expression as determined from cloned cDNA.
    Wiley ; 1987
    In:  The EMBO Journal Vol. 6, No. 11 ( 1987-11), p. 3261-3268
    Details
    In: The EMBO Journal, Wiley, Vol. 6, No. 11 ( 1987-11), p. 3261-3268
    Type of Medium: Online Resource
    ISSN: 0261-4189
    URL: Issue
    URL: Article
    DOI: 10.1002/embj.1987.6.issue-11
    DOI: 10.1002/j.1460-2075.1987.tb02644.x
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1987
    detail.hit.zdb_id: 1467419-1
    detail.hit.zdb_id: 586044-1
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    The binding of plakoglobin to desmosomal cadherins: patterns of binding sites and topogenic potential.
    Rockefeller University Press ; 1996
    In:  The Journal of cell biology Vol. 133, No. 2 ( 1996-04-15), p. 359-369
    Details
    In: The Journal of cell biology, Rockefeller University Press, Vol. 133, No. 2 ( 1996-04-15), p. 359-369
    Abstract: Plakoglobin is the only protein that occurs in the cytoplasmic plaques of all known adhering junctions and has been shown to be crucially involved in the formation and maintenance of desmosomes anchoring intermediate-sized filaments (IFs) by its interaction with the desmosomal cadherins, desmoglein (Dsg), and desmocollin (Dsc). This topogenic importance of plakoglobin is now directly shown in living cells as well as in binding assays in vitro. We show that, in transfected human A-431 carcinoma cells, a chimeric protein combining the vesicle-forming transmembrane glycoprotein synaptophysin, with the complete human plakoglobin sequence, is sorted to small vesicles many of which associate with desmosomal plaques and their attached IFs. Immunoprecipitation experiments have further revealed that the chimeric plakoglobin-containing transmembrane molecules of these vesicles are tightly bound to Dsg and Dsc but not to endogenous plakoglobin, thus demonstrating that the binding of plakoglobin to desmosomal cadherins does not require its soluble state and is strong enough to attach large structures such as vesicles to desmosomes. To identify the binding domains and the mechanisms involved in the interaction of plakoglobin with desmosomal cadherins, we have developed direct binding assays in vitro in which plakoglobin or parts thereof, produced by recombinant DNA technology in E. coli, are exposed to molecules containing the "C-domains" of several cadherins. These assays have shown that plakoglobin associates most tightly with the C-domain of Dsg, to a lesser degree with that of Dsc and only weakly with the C-domain of E-cadherin. Three separate segments of plakoglobin containing various numbers of the so-called arm repeats exhibit distinct binding to the desmosomal cadherins comparable in strength to that of the entire molecule. The binding pattern of plakoglobin segments in vitro is compared with that in vivo. Paradoxically, in vitro some internal plakoglobin fragments bind even better to the C-domain of E-cadherin than the entire molecule, indicating that elements exist in native plakoglobin that interfere with the interaction of this protein with its various cadherin partners.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.133.2.359
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 1996
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 5
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    Online Resource
    Molecular characterization and expression of the stratification-related cytokeratins 4 and 15.
    Rockefeller University Press ; 1988
    In:  The Journal of cell biology Vol. 106, No. 4 ( 1988-04-01), p. 1249-1261
    Details
    In: The Journal of cell biology, Rockefeller University Press, Vol. 106, No. 4 ( 1988-04-01), p. 1249-1261
    Abstract: A number of human cytokeratins are expressed during the development of stratified epithelia from one-layered polar epithelia and continue to be expressed in several adult epithelial tissues. For studies of the regulation of the synthesis of stratification-related cytokeratins in internal tissues, we have prepared cDNA and genomic clones encoding cytokeratin 4, as a representative of the basic (type II) cytokeratin subfamily and cytokeratin 15, as representative of the acidic (type I) subfamily, and determined their nucleotide sequences. The specific expression of mRNAs encoding these two polypeptides in certain stratified tissues and cultured cell lines is demonstrated by Northern blot hybridization. Hybridization in situ with antisense riboprobes and/or synthetic oligonucleotides shows the presence of cytokeratin 15 mRNA in all layers of esophagus, whereas cytokeratin 4 mRNA tends to be suprabasally enriched, although to degrees varying in different regions. We conclude that the expression of the genes encoding these stratification-related cytokeratins starts already in the basal cell layer and does not depend on vertical differentiation and detachment from the basal lamina. Our results also show that simple epithelial and stratification-related cytokeratins can be coexpressed in basal cell layers of certain stratified epithelia such as esophagus. Implications of these findings for epithelial differentiation and the formation of squamous cell carcinomas are discussed.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.106.4.1249
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 1988
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Expression of simple epithelial type cytokeratins in stratified epithelia as detected by immunolocalization and hybridization in situ.
    Rockefeller University Press ; 1988
    In:  The Journal of cell biology Vol. 106, No. 5 ( 1988-05-01), p. 1635-1648
    Details
    In: The Journal of cell biology, Rockefeller University Press, Vol. 106, No. 5 ( 1988-05-01), p. 1635-1648
    Abstract: Multi-layered ("stratified") epithelia differ from one-layered ("simple") polar epithelia by various architectural and functional properties as well as by their cytoskeletal complements, notably a set of cytokeratins characteristic of stratified tissue. The simple epithelial cytokeratins 8 and 18 have so far not been detected in any stratified epithelium. Using specific monoclonal antibodies we have noted, in several but not all samples of stratified epithelia, including esophagus, tongue, exocervix, and vagina, positive immunocytochemical reactions for cytokeratins 8, 18, and 19 which in some regions were selective for the basal cell layer(s) but extended into suprabasal layers in others. In situ hybridization with different probes (riboprobes, synthetic oligonucleotides) for mRNAs of cytokeratin 8 on esophageal epithelium has shown, in extended regions, relatively strong reactivity for cytokeratin 8 mRNA in the basal cell layer. In contrast, probes to cytokeratin 18 have shown much weaker hybridization which, however, was rather evenly spread over basal and suprabasal strata. These results, which emphasize the importance of in situ hybridization in studies of gene expression in complex tissues, show that the genes encoding simple epithelial cytokeratins can be expressed in stratified epithelia. This suggests that continual expression of genes coding for simple epithelial cytokeratins is compatible with the formation of squamous stratified tissues and can occur, at least in basal cell layers, simultaneously with the synthesis of certain stratification-related cytokeratins. We also emphasize differences of expression and immunoreactivity of these cytokeratins between different samples and in different regions of the same stratified epithelium and discuss the results in relation to changes of cytokeratin expression during fetal development of stratified epithelia, in response to environmental factors and during the formation of squamous cell carcinomas.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.106.5.1635
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 1988
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Identification of the plakoglobin-binding domain in desmoglein and its role in plaque assembly and intermediate filament anchorage.
    Rockefeller University Press ; 1994
    In:  The Journal of cell biology Vol. 127, No. 1 ( 1994-10-01), p. 151-160
    Details
    In: The Journal of cell biology, Rockefeller University Press, Vol. 127, No. 1 ( 1994-10-01), p. 151-160
    Abstract: The carboxyterminal cytoplasmic portions (tails) of desmosomal cadherins of both the desmoglein (Dsg) and desmocollin type are integral components of the desmosomal plaque and are involved in desmosome assembly and the anchorage of intermediate-sized filaments. When additional Dsg tails were introduced by cDNA transfection into cultured human epithelial cells, in the form of chimeras with the aminoterminal membrane insertion domain of rat connexin32 (Co32), the resulting stably transfected cells showed a dominant-negative defect specific for desmosomal junctions: despite the continual presence of all desmosomal proteins, the endogenous desmosomes disappeared and the formation of Co32-Dsg chimeric gap junctions was inhibited. Using cell transfection in combination with immunoprecipitation techniques, we have examined a series of deletion mutants of the Dsg1 tail in Co32-Dsg chimeras. We show that upon removal of the last 262 amino acids the truncated Dsg tail still effects the binding of plakoglobin but not of detectable amounts of any catenin and induces the dominant-negative phenotype. However, further truncation or excision of the next 41 amino acids, which correspond to the highly conserved carboxyterminus of the C-domain in other cadherins, abolishes plakoglobin binding and allows desmosomes to reform. Therefore, we conclude that this short segment provides a plakoglobin-binding site and is important for plaque assembly and the specific anchorage of either actin filaments in adherens junctions or IFs in desmosomes.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.127.1.151
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 1994
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 8
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    Online Resource
    Pantophysin is a ubiquitously expressed synaptophysin homologue and defines constitutive transport vesicles.
    Rockefeller University Press ; 1996
    In:  The Journal of cell biology Vol. 134, No. 3 ( 1996-08-01), p. 731-746
    Details
    In: The Journal of cell biology, Rockefeller University Press, Vol. 134, No. 3 ( 1996-08-01), p. 731-746
    Abstract: Certain properties of the highly specialized synaptic transmitter vesicles are shared by constitutively occurring vesicles. We and others have thus identified a cDNA in various nonneuroendocrine cell types of rat and human that is related to synaptophysin, one of the major synaptic vesicle membrane proteins, which we termed pantophysin. Here we characterize the gene structure, mRNA and protein expression, and intracellular distribution of pantophysin. Its mRNA is detected in murine cell types of nonneuroendocrine as well as of neuroendocrine origin. The intron/exon structure of the murine pantophysin gene is identical to that of synaptophysin except for the last intron that is absent in pantophysin. The encoded polypeptide of calculated mol wt 28,926 shares many sequence features with synaptophysin, most notably the four hydrophobic putative transmembrane domains, although the cytoplasmic end domains are completely different. Using antibodies against the unique carboxy terminus pantophysin can be detected by immunofluorescence microscopy in both exocrine and endocrine cells of human pancreas, and in cultured cells, colocalizing with constitutive secretory and endocytotic vesicle markers in nonneuroendocrine cells and with synaptophysin in cDNA-transfected epithelial cells. By immunoelectron microscopy, the majority of pantophysin reactivity is detected at vesicles with a diameter of & lt; 100 nm that have a smooth surface and an electron-translucent interior. Using cell fractionation in combination with immunoisolation, these vesicles are enriched in a light fraction and shown to contain the cellular vSNARE cellubrevin and the ubiquitous SCAMPs in epithelial cells and synaptophysin in neuroendocrine or cDNA-transfected nonneuroendocrine cells and neuroendocrine tissues. Pantophysin is therefore a broadly distributed marker of small cytoplasmic transport vesicles independent of their content.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.134.3.731
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 1996
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 9
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    Online Resource
    Sorting of synaptophysin into special vesicles in nonneuroendocrine epithelial cells.
    Rockefeller University Press ; 1994
    In:  The Journal of cell biology Vol. 127, No. 6 ( 1994-12-15), p. 1589-1601
    Details
    In: The Journal of cell biology, Rockefeller University Press, Vol. 127, No. 6 ( 1994-12-15), p. 1589-1601
    Abstract: Synaptophysin is a major transmembrane glycoprotein of a type of small vesicle with an electron-translucent content (SET vesicles), including the approximately 50-nm presynaptic vesicles in neuronal cells, and of similar, somewhat larger ( & lt; or = approximately 90 nm) vesicles (SLMV) in neuroendocrine (NE) cells. When certain epithelial non-NE cells, such as human hepatocellular carcinoma PLC cells, were cDNA transfected to synthesize synaptophysin, the new molecules appeared in specific SET vesicles. As this was in contrast to other reports that only NE cells were able to sort synaptophysin away from other plasma membrane proteins into presynaptic- or SLMV-type vesicles, we have further characterized the vesicles containing synaptophysin in transfected PLC cells. Using fractionation and immunoisolation techniques, we have separated different kinds of vesicles, and we have identified a distinct type of synaptophysin-rich, small (30-90-nm) vesicle that contains little, if any, protein of the constitutive secretory pathway marker hepatitis B surface antigen, of the fluid phase endocytosis marker HRP, and of the plasma membrane recycling endosomal marker transferrin receptor. In addition, we have found variously sized vesicles that contained both synaptophysin and transferrin receptor. A corresponding result was also obtained by direct visualization, using double-label immunofluorescence microscopy for the endocytotic markers and synaptophysin in confocal laser scan microscopy and in double-immunogold label electron microscopy. We conclude that diverse non-NE cells of epithelial nature are able to enrich the "foreign" molecule synaptophysin in a category of SET vesicles that are morphologically indistinguishable from SLMV of NE cells, including one type of vesicle in which synaptophysin is sorted away from endosomal marker proteins. Possible mechanisms of this sorting are discussed.
    Type of Medium: Online Resource
    ISSN: 0021-9525 , 1540-8140
    URL: Article
    DOI: 10.1083/jcb.127.6.1589
    RVK:
    WA 15000
    Language: English
    Publisher: Rockefeller University Press
    Publication Date: 1994
    detail.hit.zdb_id: 1421310-2
    SSG: 12
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  • 10
    Online Resource
    Online Resource
    Tissue expression of the vesicle protein pantophysin
    Springer Science and Business Media LLC ; 1999
    In:  Cell and Tissue Research Vol. 296, No. 3 ( 1999-5-20), p. 499-510
    Details
    In: Cell and Tissue Research, Springer Science and Business Media LLC, Vol. 296, No. 3 ( 1999-5-20), p. 499-510
    Type of Medium: Online Resource
    ISSN: 0302-766X , 1432-0878
    URL: Article
    DOI: 10.1007/s004410051310
    RVK:
    WA 15000
    Language: Unknown
    Publisher: Springer Science and Business Media LLC
    Publication Date: 1999
    detail.hit.zdb_id: 1458496-7
    SSG: 12
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