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[PMID]: 29522173
[Au] Autor:Giuliodori A; Beffagna G; Marchetto G; Fornetto C; Vanzi F; Toppo S; Facchinello N; Santimaria M; Vettori A; Rizzo S; Della Barbera M; Pilichou K; Argenton F; Thiene G; Tiso N; Basso C
[Ad] Address:Department of Cardiac, Thoracic and Vascular Sciences, University of Padova.
[Ti] Title:Loss of cardiac Wnt/ß-catenin signalling in Desmoplakin-deficient AC8 zebrafish models is rescuable by genetic and pharmacological intervention.
[So] Source:Cardiovasc Res;, 2018 Mar 07.
[Is] ISSN:1755-3245
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Aims: Arrhythmogenic cardiomyopathy (AC) is an inherited heart disease characterized by life-threatening ventricular arrhythmias and fibro-fatty replacement of the myocardium. More than 60% of AC patients show pathogenic mutations in genes encoding for desmosomal proteins. By focusing our attention on the AC8 form, linked to the junctional protein Desmoplakin (DSP), we present here a zebrafish model of DSP deficiency, exploited to identify early changes of cell signalling in the cardiac region. Methods and results: To obtain an embryonic model of DSP deficiency, we first confirmed the orthologous correspondence of zebrafish dsp genes (dspa and dspb) to the human DSP counterpart. Then, we verified their cardiac expression, at embryonic and adult stages, and subsequently we targeted them by antisense morpholino strategy, confirming specific and disruptive effects on desmosomes, like those identified in AC patients. Finally, we exploited our DSP-deficient models for an in vivo cell signalling screen, using pathway-specific reporter transgenes. Out of nine considered, three pathways (Wnt/ß-catenin, TGFß/Smad3 and Hippo/YAP-TAZ) were significantly altered, with Wnt as the most dramatically affected. Interestingly, under persistent DSP deficiency, Wnt signalling is rescuable both by a genetic and a pharmacological approach. Conclusion: Our data point to Wnt/ß-catenin as the final common pathway underlying different desmosomal AC forms and support the zebrafish as a suitable model for detecting early signalling pathways involved in the pathogenesis of DSP-associated diseases, possibly responsive to pharmacological or genetic rescue.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher
[do] DOI:10.1093/cvr/cvy057

  2 / 5907 MEDLINE  
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[PMID]: 29515024
[Au] Autor:Besnard V; Dagher R; Madjer T; Joannes A; Jaillet M; Kolb M; Bonniaud P; Murray LA; Sleeman MA; Crestani B
[Ad] Address:INSERM U1152, Paris, France.
[Ti] Title:Identification of periplakin as a major regulator of lung injury and repair in mice.
[So] Source:JCI Insight;3(5), 2018 Mar 08.
[Is] ISSN:2379-3708
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Periplakin is a component of the desmosomes that acts as a cytolinker between intermediate filament scaffolding and the desmosomal plaque. Periplakin is strongly expressed by epithelial cells in the lung and is a target antigen for autoimmunity in idiopathic pulmonary fibrosis. The aim of this study was to determine the role of periplakin during lung injury and remodeling in a mouse model of lung fibrosis induced by bleomycin. We found that periplakin expression was downregulated in the whole lung and in alveolar epithelial cells following bleomycin-induced injury. Deletion of the Ppl gene in mice improved survival and reduced lung fibrosis development after bleomycin-induced injury. Notably, Ppl deletion promoted an antiinflammatory alveolar environment linked to profound changes in type 2 alveolar epithelial cells, including overexpression of antiinflammatory cytokines, decreased expression of profibrotic mediators, and altered cell signaling with a reduced response to TGF-ß1. These results identify periplakin as a previously unidentified regulator of the response to injury in the lung.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher

  3 / 5907 MEDLINE  
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[PMID]: 29512980
[Au] Autor:Giannetti L; Generali L; Bertoldi C
[Ad] Address:Dipartimento Chirurgico, Medico, Odontoiatrico e di Scienze Morfologiche con Interesse Trapiantologico, Oncologico e di Medicina Rigenerativa, Università degli Studi di Modena e Reggio Emilia, Modena, Italy - Luca.giannetti@unimore.it.
[Ti] Title:Oral pemphigus.
[So] Source:G Ital Dermatol Venereol;, 2018 Mar 06.
[Is] ISSN:1827-1820
[Cp] Country of publication:Italy
[La] Language:eng
[Ab] Abstract:Involvement of the oral mucosa in patients affected by Pemphigus Vulgaris (PV), Paraneoplastic, IgA Pemphigus and in some cases of Iatrogenic Pemphigus is common, and precede skin lesions in the majority of cases. Intraepidermal bullae are caused by acantholysis, induced by IgG autoantibodies directed against the desmosomes and the domain of numerous keratinocytes self-antigens desmogleins (namely cadherins), thus supporting the autoimmune nature of the disease. Apoptosis may contribute to the acantholysis.The oral mucosal lesions tend more often to be refractory to treatment than skin lesions, and have been associated with disease duration, disease location and possibly the presence of HSV DNA in the oral cavity. Recent publications have stressed the positive role of Rituximab in early disease treatment.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:Publisher
[do] DOI:10.23736/S0392-0488.18.05887-X

  4 / 5907 MEDLINE  
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[PMID]: 29508067
[Au] Autor:Vanslembrouck B; Kremer A; Pavie B; van Roy F; Lippens S; van Hengel J
[Ad] Address:Department of Basic Medical Science, Faculty of Medicine and Health Sciences, Ghent University, Corneel Heymanslaan 10, Building B, 9000, Ghent, Belgium.
[Ti] Title:Three-dimensional reconstruction of the intercalated disc including the intercellular junctions by applying volume scanning electron microscopy.
[So] Source:Histochem Cell Biol;, 2018 Mar 05.
[Is] ISSN:1432-119X
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:The intercalated disc (ID) contains different kinds of intercellular junctions: gap junctions (GJs), desmosomes and areae compositae, essential for adhesion and communication between adjacent cardiomyocytes. The junctions can be identified based on their morphology when imaged using transmission electron microscopy (TEM), however, only with very limited information in the z-dimension. The application of volume EM techniques can give insight into the three-dimensional (3-D) organization of complex biological structures. In this study, we generated 3-D datasets using serial block-face scanning electron microscopy (SBF-SEM) and focused ion beam SEM (FIB-SEM), the latter resulting in datasets with 5 nm isotropic voxels. We visualized cardiomyocytes in murine ventricular heart tissue and, for the first time, we could three-dimensionally reconstruct the ID including desmosomes and GJs with 5 nm precision in a large volume. Results show in three dimensions a highly folded structure of the ID, with the presence of GJs and desmosomes in both plicae and interplicae regions. We observed close contact of GJs with mitochondria and a variable spatial distribution of the junctions. Based on measurements of the shape of the intercellular junctions in 3-D, it is seen that GJs and desmosomes vary in size, depending on the region within the ID. This demonstrates that volume EM is essential to visualize morphological changes and its potential to quantitatively determine structural changes between normal and pathological conditions, e.g., cardiomyopathies.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180306
[Lr] Last revision date:180306
[St] Status:Publisher
[do] DOI:10.1007/s00418-018-1657-x

  5 / 5907 MEDLINE  
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[PMID]: 29444101
[Au] Autor:Gjessing MC; Aamelfot M; Batts WN; Benestad SL; Dale OB; Thoen E; Weli SC; Winton JR
[Ad] Address:Norwegian Veterinary Institute, Oslo, Norway.
[Ti] Title:Development and characterization of two cell lines from gills of Atlantic salmon.
[So] Source:PLoS One;13(2):e0191792, 2018.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Gill disease in Atlantic salmon, Salmo salar L., causes big losses in the salmon farming industry. Until now, tools to cultivate microorganisms causing gill disease and models to study the gill responses have been lacking. Here we describe the establishment and characterization of two cell lines from the gills of Atlantic salmon. Atlantic salmon gill cell ASG-10 consisted of cells staining for cytokeratin and e-cadherin and with desmosomes as seen by transmission electron microscopy suggesting the cells to be of epithelial origin. These structures were not seen in ASG-13. The cell lines have been maintained for almost 30 passages and both cell lines are fully susceptible to infection by infectious hematopoietic necrosis virus (IHNV), viral hemorrhagic septicemia virus (VHSV), infectious pancreatic necrosis virus (IPNV), Atlantic salmon reovirus TS (TSRV) and Pacific salmon paramyxovirus (PSPV). While infectious salmon anemia virus (ISAV) did not cause visible CPE, immunofluorescent staining revealed a sub-fraction of cells in both the ASG-10 and ASG-13 lines may be permissive to infection. ASG-10 is able to proliferate and migrate to close scratches in the monolayer within seven days in vitro contrary to ASG-13, which does not appear to do have the same proliferative and migratory ability. These cell lines will be useful in studies of gill diseases in Atlantic salmon and may represent an important contribution for alternatives to experimental animals and studies of epithelial-mesenchymal cell biology.
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Entry month:1802
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[St] Status:In-Process
[do] DOI:10.1371/journal.pone.0191792

  6 / 5907 MEDLINE  
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[PMID]: 29470947
[Au] Autor:Vázquez-Carretero MD; García-Miranda P; Balda MS; Matter K; Peral MJ; Ilundain AA
[Ad] Address:Departamento de Fisiología, Facultad de Farmacia, Universidad de Sevilla, Spain.
[Ti] Title:Small and large intestine express a truncated Dab1 isoform that assembles in cell-cell junctions and co-localizes with proteins involved in endocytosis.
[So] Source:Biochim Biophys Acta;1860(5):1231-1241, 2018 Feb 19.
[Is] ISSN:0006-3002
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Disabled-1 (Dab1) is an essential intracellular adaptor protein in the reelin pathway. Our previous studies in mice intestine showed that Dab1 transmits the reelin signal to cytosolic signalling pathways. Here, we determine the Dab1 isoform expressed in rodent small and large intestine, its subcellular location and co-localization with clathrin, caveolin-1 and N-Wasp. PCR and sequencing analysis reveal that rodent small and large intestine express a Dab1 isoform that misses three (Y , Y and Y ) of the five tyrosine phosphorylation sites present in brain Dab1 isoform (canonical) and contains nuclear localization and export signals. Western blot assays show that both, crypts, which shelter progenitor cells, and enterocytes express the same Dab1 isoform, suggesting that epithelial cell differentiation does not regulate intestinal generation of alternatively spliced Dab1 variants. They also reveal that the canonical and the intestinal Dab1 isoforms differ in their total degree of phosphorylation. Immunostaining assays show that in enterocytes Dab1 localizes at the apical and lateral membranes, apical vesicles, close to adherens junctions and desmosomes, as well as in the nucleus; co-localizes with clathrin and with N-Wasp but not with caveolin-1, and in Caco-2 cells Dab1 localizes at cell-to-cell junctions by a Ca -dependent process. In conclusion, the results indicate that in rodent intestine a truncated Dab1 variant transmits the reelin signal and may play a role in clathrin-mediated apical endocytosis and in the control of cell-to-cell junction assembly. A function of intestinal Dab1 variant as a nucleocytoplasmic shuttling protein is also inferred from its sequence and nuclear location.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180302
[Lr] Last revision date:180302
[St] Status:Publisher

  7 / 5907 MEDLINE  
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[PMID]: 29198699
[Au] Autor:Kippenberger S; Kleemann J; Meissner M; Steinhorst K; Müller J; Zouboulis CC; Kaufmann R; Zöller N
[Ad] Address:Clinic of Dermatology, Venereology and Allergology, Johann Wolfgang Goethe University, Frankfurt/Main, Germany. Electronic address: kippenberger@em.uni-frankfurt.de.
[Ti] Title:Activation of PKB/Akt and p44/42 by mechanical stretch utilizes desmosomal structures and the keratin filament.
[So] Source:J Dermatol Sci;89(3):241-247, 2018 Mar.
[Is] ISSN:1873-569X
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:BACKGROUND: Mechanical stress is an ubiquitous challenge of human cells with fundamental impact on cell physiology. Previous studies have shown that stretching promotes signalling cascades involved in proliferation and tissue enlargement. OBJECTIVE: The present study is dedicated to learn more about cellular structures contributing to perception and signal transmission of cell stretch. In particular, we hypothesized that desmosmal contacts and the adjacent keratin filament build an intercellular matrix providing information about the mechanical load. METHODS: Epidermal cells with different keratin equipment were seeded on flexible silicon dishes and stretched. As read out parameter the activation of PKB/Akt and p44/42 was monitored by Western blotting. Likewise desomosomal contacts were manipulated by depletion or addition of calcium. Moreover, desmoglein 3 and desmocollin 3 were blocked by either specific antibodies or siRNA. RESULTS: It was found that the omission of calcium from the medium, a necessary cofactor for desmosomal cadherins, inhibited stretch mediated activation of PKB/Akt and p44/42. The relevance of desmosomes in this context was further substantiated by experiments using a desmoglein 3 blocking antibody (AK23) and siRNA against desmocollin 3. Moreover, disruption of the keratin filament by sodium orthovanadate also abrogates PKB/Akt and p44/42 activation in response to stretch. Likewise, KEB-7 keratinocytes harbouring a mutation in the keratin 14 gene and genetically modified keratinocytes devoid of any keratin show an altered signalling after stretch indicating the relevance of the keratin filament in this context. CONCLUSION: Besides their important role in cell architecture our results identify desmosomes and keratins as mechanosensing structures.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180225
[Lr] Last revision date:180225
[St] Status:In-Process

  8 / 5907 MEDLINE  
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[PMID]: 29253567
[Au] Autor:Vishal SS; Tilwani S; Dalal SN
[Ad] Address:KS215, Advanced Centre for Treatment Research and Education in Cancer (ACTREC), Tata Memorial Centre, Kharghar Node, Navi Mumbai 410210, India; Homi Bhabha National Institute, Training School Complex, Anushakti Nagar, Mumbai 400085, India.
[Ti] Title:Plakoglobin localization to the cell border restores desmosome function in cells lacking 14-3-3γ.
[So] Source:Biochem Biophys Res Commun;495(2):1998-2003, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Desmosomes are cell-cell adhesion junctions that anchor intermediate filaments. Loss of 14-3-3γ in HCT116 cells led to defects in desmosome assembly due to a decrease in the transport of Plakoglobin (PG) to the cell border thus disrupting desmosome formation. Desmosome formation in cells lacking 14-3-3γ was restored by artificially localizing PG to the cell border by fusing it to EGFP-f (PG-EGFP-f). These results suggest that a major role of 14-3-3γ in desmosome assembly is to transport PG to the cell border leading to the initiation of desmosome formation.
[Mh] MeSH terms primary: 14-3-3 Proteins/metabolism
Cell Membrane/metabolism
Colorectal Neoplasms/metabolism
Desmosomes/metabolism
Subcellular Fractions/metabolism
[Mh] MeSH terms secundary: Cell Line, Tumor
Humans
gamma Catenin/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (14-3-3 Proteins); 0 (JUP protein, human); 0 (gamma Catenin)
[Em] Entry month:1802
[Cu] Class update date: 180214
[Lr] Last revision date:180214
[Js] Journal subset:IM
[Da] Date of entry for processing:171219
[St] Status:MEDLINE

  9 / 5907 MEDLINE  
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[PMID]: 29416987
[Au] Autor:Sumitomo T; Mori Y; Nakamura Y; Honda-Ogawa M; Nakagawa S; Yamaguchi M; Matsue H; Terao Y; Nakata M; Kawabata S
[Ad] Address:Department of Oral and Molecular Microbiology, Osaka University Graduate School of Dentistry, Osaka, Japan.
[Ti] Title:Streptococcal Cysteine Protease-Mediated Cleavage of Desmogleins Is Involved in the Pathogenesis of Cutaneous Infection.
[So] Source:Front Cell Infect Microbiol;8:10, 2018.
[Is] ISSN:2235-2988
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:is responsible for a wide variety of cutaneous infections ranging from superficial impetigo to fulminant invasive necrotizing fasciitis. Dysfunction of desmosomes is associated with the pathogenesis of cutaneous diseases. We identified streptococcal pyrogenic exotoxin B (SpeB) as a proteolytic factor that cleaves the extracellular domains of desmoglein 1 and 3. In an epicutaneous infection model, lesional skin infected with an deletion mutant were significantly smaller as compared to those caused by the wild-type strain. Furthermore, immunohistological analysis indicated cleavage of desmogleins that developed around the invasion site of the wild-type strain. In contrast, the mutant was preferentially found on the epidermis surface layer. Taken together, our findings provide evidence that SpeB-mediated degradation of desmosomes has a pathogenic role in development of cutaneous infection.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180213
[Lr] Last revision date:180213
[St] Status:In-Data-Review
[do] DOI:10.3389/fcimb.2018.00010

  10 / 5907 MEDLINE  
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[PMID]: 29212005
[Au] Autor:Bartle EI; Urner TM; Raju SS; Mattheyses AL
[Ad] Address:Department of Cell Biology, Emory University, Atlanta, Georgia.
[Ti] Title:Desmoglein 3 Order and Dynamics in Desmosomes Determined by Fluorescence Polarization Microscopy.
[So] Source:Biophys J;113(11):2519-2529, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] Country of publication:United States
[La] Language:eng
[Ab] 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 dependent, and reduction of extracellular Ca leads to a loss of adhesion measured by dispase fragmentation assay (λ = 15.1 min). Live cell imaging revealed Dsg3 order decreased more rapidly (λ = 5.5 min), indicating that cadherin order is not required for adhesion. Our results suggest that rapid disordering of cadherins can communicate a change in extracellular Ca concentration to the cell, leading to a downstream loss of adhesion. Fluorescence polarization is an effective bridge between protein structure and complex dynamics and the approach presented here is broadly applicable to studying order in macromolecular structures.
[Mh] MeSH terms primary: Desmoglein 3/metabolism
Desmosomes/metabolism
[Mh] MeSH terms secundary: Cell Survival
Desmoglein 3/chemistry
Humans
Keratinocytes/cytology
Microscopy, Fluorescence
Microscopy, Polarization
Models, Molecular
Protein Conformation
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Desmoglein 3)
[Em] Entry month:1801
[Cu] Class update date: 180210
[Lr] Last revision date:180210
[Js] Journal subset:IM
[Da] Date of entry for processing:171207
[St] Status:MEDLINE


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