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  1. Article ; Online: Bridging the gap: Super-resolution microscopy of epithelial cell junctions.

    Bartle, Emily I / Rao, Tejeshwar C / Urner, Tara M / Mattheyses, Alexa L

    Tissue barriers

    2018  Volume 6, Issue 1, Page(s) e1404189

    Abstract: Cell junctions are critical for cell adhesion and communication in epithelial tissues. It is evident that the cellular distribution, size, and architecture of cell junctions play a vital role in regulating function. These details of junction architecture ...

    Abstract Cell junctions are critical for cell adhesion and communication in epithelial tissues. It is evident that the cellular distribution, size, and architecture of cell junctions play a vital role in regulating function. These details of junction architecture have been challenging to elucidate in part due to the complexity and size of cell junctions. A major challenge in understanding these features is attaining high resolution spatial information with molecular specificity. Fluorescence microscopy allows localization of specific proteins to junctions, but with a resolution on the same scale as junction size, rendering internal protein organization unobtainable. Super-resolution microscopy provides a bridge between fluorescence microscopy and nanoscale approaches, utilizing fluorescent tags to reveal protein organization below the resolution limit. Here we provide a brief introduction to super-resolution microscopy and discuss novel findings into the organization, structure and function of epithelial cell junctions.
    MeSH term(s) Adherens Junctions/metabolism ; Epithelial Cells/metabolism ; Humans ; Microscopy, Fluorescence/methods ; Tight Junctions/metabolism
    Language English
    Publishing date 2018-02-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ISSN 2168-8370
    ISSN (online) 2168-8370
    DOI 10.1080/21688370.2017.1404189
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Desmoglein 3 Order and Dynamics in Desmosomes Determined by Fluorescence Polarization Microscopy.

    Bartle, Emily I / Urner, Tara M / Raju, Siddharth S / Mattheyses, Alexa L

    Biophysical journal

    2017  Volume 113, Issue 11, Page(s) 2519–2529

    Abstract: Desmosomes are macromolecular cell-cell junctions that provide adhesive strength in epithelial tissue. Desmosome function is inseparably linked to structure, and it is hypothesized that the arrangement, or order, of desmosomal cadherins in the ... ...

    Abstract Desmosomes are macromolecular cell-cell junctions that provide adhesive strength in epithelial tissue. Desmosome function is inseparably linked to structure, and it is hypothesized that the arrangement, or order, of desmosomal cadherins in the intercellular space is critical for adhesive strength. However, due to desmosome size, molecular complexity, and dynamics, the role that order plays in adhesion is challenging to study. Herein, we present an excitation resolved fluorescence polarization microscopy approach to measure the spatiotemporal dynamics of order and disorder of the desmosomal cadherin desmoglein 3 (Dsg3) in living cells. Simulations were used to establish order factor as a robust metric for quantifying the spatiotemporal dynamics of order and disorder. Order factor measurements in keratinocytes showed the Dsg3 extracellular domain is ordered at the individual desmosome, single cell, and cell population levels compared to a series of disordered controls. Desmosomal adhesion is Ca
    MeSH term(s) Cell Survival ; Desmoglein 3/chemistry ; Desmoglein 3/metabolism ; Desmosomes/metabolism ; Humans ; Keratinocytes/cytology ; Microscopy, Fluorescence ; Microscopy, Polarization ; Models, Molecular ; Protein Conformation
    Chemical Substances Desmoglein 3
    Language English
    Publishing date 2017-12-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2017.09.028
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 235: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MO 2: Show issues

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  3. Article ; Online: Protein exchange is reduced in calcium-independent epithelial junctions.

    Bartle, Emily I / Rao, Tejeshwar C / Beggs, Reena R / Dean, William F / Urner, Tara M / Kowalczyk, Andrew P / Mattheyses, Alexa L

    The Journal of cell biology

    2020  Volume 219, Issue 6

    Abstract: Desmosomes are cell-cell junctions that provide mechanical integrity to epithelial and cardiac tissues. Desmosomes have two distinct adhesive states, calcium-dependent and hyperadhesive, which balance tissue plasticity and strength. A highly ordered ... ...

    Abstract Desmosomes are cell-cell junctions that provide mechanical integrity to epithelial and cardiac tissues. Desmosomes have two distinct adhesive states, calcium-dependent and hyperadhesive, which balance tissue plasticity and strength. A highly ordered array of cadherins in the adhesive interface is hypothesized to drive hyperadhesion, but how desmosome structure confers adhesive state is still elusive. We employed fluorescence polarization microscopy to show that cadherin order is not required for hyperadhesion induced by pharmacologic and genetic approaches. FRAP experiments in cells treated with the PKCα inhibitor Gö6976 revealed that cadherins, plakoglobin, and desmoplakin have significantly reduced exchange in and out of hyperadhesive desmosomes. To test whether this was a result of enhanced keratin association, we used the desmoplakin mutant S2849G, which conferred reduced protein exchange. We propose that inside-out regulation of protein exchange modulates adhesive function, whereby proteins are "locked in" to hyperadhesive desmosomes while protein exchange confers plasticity on calcium-dependent desmosomes, thereby providing rapid control of adhesion.
    MeSH term(s) Cadherins/genetics ; Cadherins/metabolism ; Calcium/metabolism ; Calcium/pharmacology ; Carbazoles/pharmacology ; Cell Adhesion/drug effects ; Cell Adhesion/genetics ; Cell Line ; Desmoglein 3/genetics ; Desmoglein 3/metabolism ; Desmoplakins/genetics ; Desmoplakins/metabolism ; Desmosomes/drug effects ; Desmosomes/metabolism ; Desmosomes/ultrastructure ; Humans ; Keratinocytes/drug effects ; Keratinocytes/metabolism ; Microscopy, Electron ; Microscopy, Fluorescence ; Mutation ; Phosphorylation ; Protein Binding/genetics ; Protein Kinase C-alpha/antagonists & inhibitors ; Protein Kinase Inhibitors/pharmacology ; gamma Catenin/genetics ; gamma Catenin/metabolism
    Chemical Substances Cadherins ; Carbazoles ; DSG3 protein, human ; Desmoglein 3 ; Desmoplakins ; Protein Kinase Inhibitors ; gamma Catenin ; Go 6976 (136194-77-9) ; Protein Kinase C-alpha (EC 2.7.11.13) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2020-05-12
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.201906153
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Molecular organization of the desmosome as revealed by direct stochastic optical reconstruction microscopy.

    Stahley, Sara N / Bartle, Emily I / Atkinson, Claire E / Kowalczyk, Andrew P / Mattheyses, Alexa L

    Journal of cell science

    2016  Volume 129, Issue 15, Page(s) 2897–2904

    Abstract: Desmosomes are macromolecular junctions responsible for providing strong cell-cell adhesion. Because of their size and molecular complexity, the precise ultrastructural organization of desmosomes is challenging to study. Here, we used direct stochastic ... ...

    Abstract Desmosomes are macromolecular junctions responsible for providing strong cell-cell adhesion. Because of their size and molecular complexity, the precise ultrastructural organization of desmosomes is challenging to study. Here, we used direct stochastic optical reconstruction microscopy (dSTORM) to resolve individual plaque pairs for inner and outer dense plaque proteins. Analysis methods based on desmosomal mirror symmetry were developed to measure plaque-to-plaque distances and create an integrated map. We quantified the organization of desmoglein 3, plakoglobin and desmoplakin (N-terminal, rod and C-terminal domains) in primary human keratinocytes. Longer desmosome lengths correlated with increasing plaque-to-plaque distance, suggesting that desmoplakin is arranged with its long axis at an angle within the plaque. We next examined whether plaque organization changed in different adhesive states. Plaque-to-plaque distance for the desmoplakin rod and C-terminal domains decreased in PKP-1-mediated hyperadhesive desmosomes, suggesting that protein reorganization correlates with function. Finally, in human epidermis we found a difference in plaque-to-plaque distance for the desmoplakin C-terminal domain, but not the desmoplakin rod domain or plakoglobin, between basal and suprabasal cells. Our data reveal the molecular organization of desmosomes in cultured keratinocytes and skin as defined by dSTORM.
    MeSH term(s) Cell Adhesion ; Desmosomes/metabolism ; Humans ; Male ; Microscopy/methods ; Optical Phenomena ; Plakophilins/metabolism ; Skin/metabolism ; Stochastic Processes
    Chemical Substances Plakophilins
    Language English
    Publishing date 2016-08-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.185785
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 14: Show issues

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