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Relevant bibliographies by topics / Desmosomal disruption

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Journal articles

Academic literature on the topic 'Desmosomal disruption'

Author: Grafiati

Published: 7 June 2025

Last updated: 2 August 2025

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Journal articles on the topic "Desmosomal disruption"

1

Garrod, David, and Tomomi E. Kimura. "Hyper-adhesion: a new concept in cell–cell adhesion." Biochemical Society Transactions 36, no. 2 (2008): 195–201. http://dx.doi.org/10.1042/bst0360195.

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We have developed a new concept of cell–cell adhesion termed ‘hyper-adhesion’, the very strong adhesion adopted by desmosomes. This uniquely desmosomal property accounts for their ability to provide the intercellular links in the desmosome–intermediate filament complex. These links are targeted by diseases, resulting in disruption of the complex with severe consequences. Hyper-adhesion is characteristic of desmosomes in tissues and is believed to result from a highly ordered arrangement of the extracellular domains of the desmosomal cadherins that locks their binding interaction so that it is

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2

Li, Jifen, and Glenn L. Radice. "A New Perspective on Intercalated Disc Organization: Implications for Heart Disease." Dermatology Research and Practice 2010 (2010): 1–5. http://dx.doi.org/10.1155/2010/207835.

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Adherens junctions and desmosomes are intercellular adhesive junctions and essential for the morphogenesis, differentiation, and maintenance of tissues that are subjected to high mechanical stress, including heart and skin. The different junction complexes are organized at the termini of the cardiomyocyte called the intercalated disc. Disruption of adhesive integrity via mutations in genes encoding desmosomal proteins causes an inherited heart disease, arrhythmogenic right ventricular cardiomyopathy (ARVC). Besides plakoglobin, which is shared by adherens junctions and desmosomes, other desmos

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3

Zen, Ke, Brian A. Babbin, Yuan Liu, John B. Whelan, Asma Nusrat, and Charles A. Parkos. "JAM-C Is a Component of Desmosomes and a Ligand for CD11b/CD18-mediated Neutrophil Transepithelial Migration." Molecular Biology of the Cell 15, no. 8 (2004): 3926–37. http://dx.doi.org/10.1091/mbc.e04-04-0317.

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Neutrophil (PMN) transepithelial migration is dependent on the leukocyte β2integrin CD11b/CD18, yet the identity of epithelial counterreceptors remain elusive. Recently, a JAM protein family member termed JAM-C was implicated in leukocyte adhesive interactions; however, its expression in epithelia and role in PMN-epithelial interactions are unknown. Here, we demonstrate that JAM-C is abundantly expressed basolaterally in intestinal epithelia and localizes to desmosomes but not tight junctions. Desmosomal localization of JAM-C was further confirmed by experiments aimed at selective disruption o

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4

Bogner, P., P. Skehan, S. Kenney, E. Sainz, M. A. Akeson, and S. J. Friedman. "Stabilization of intercellular contacts in MDCK cells during Ca2+ deprivation. Selective effects of monocarboxylic acids on desmosomes." Journal of Cell Science 103, no. 2 (1992): 463–73. http://dx.doi.org/10.1242/jcs.103.2.463.

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Short-chain monocarboxylic acids (MCAs) selectively protect desmosomal junctions of MDCK cells from disruption by chelating agents and low calcium medium. This effect occurs in the millimolar concentration range and increases inversely with carbon chain length (formate &gt; acetate = propionate &gt; butyrate &gt; isobutyrate &gt; isovalerate). The relative activity of MCAs does not correlate with their overall hydrophobicity or ability to chelate ions, or their effectiveness in lowering cytosolic pH. It exhibits chemical specificity and is dependent upon postconfluency culture

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5

Stappenbeck, T. S., and K. J. Green. "The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells." Journal of Cell Biology 116, no. 5 (1992): 1197–209. http://dx.doi.org/10.1083/jcb.116.5.1197.

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Specific interactions between desmoplakins I and II (DP I and II) and other desmosomal or cytoskeletal molecules have been difficult to determine in part because of the complexity and insolubility of the desmosome and its constituents. We have used a molecular genetic approach to investigate the role that DP I and II may play in the association of the desmosomal plaque with cytoplasmic intermediate filaments (IF). A series of mammalian expression vectors encoding specific predicted domains of DP I were transiently expressed in cultured cells that form (COS-7) and do not form (NIH-3T3) desmosom

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6

Allen, E., Q. C. Yu, and E. Fuchs. "Mice expressing a mutant desmosomal cadherin exhibit abnormalities in desmosomes, proliferation, and epidermal differentiation." Journal of Cell Biology 133, no. 6 (1996): 1367–82. http://dx.doi.org/10.1083/jcb.133.6.1367.

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Desmogleins are members of the cadherin superfamily which form the core of desmosomes. In vitro studies indicate that the cytoplasmic domain of desmogleins associates with plakoglobin; however, little is known about the role of this domain in desmosome recognition or assembly in vivo, or about the possible relation of desmoglein mutations to epidermal differentiation and disease. To address these questions we used transgenic mouse technology to produce an NH2-terminally truncated desmoglein (Pemphigus Vulgaris Antigen or Dsg3) in cells known to express its wild-type counterpart. Within 2 d, ne

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7

Jones, J. C., K. M. Yokoo, and R. D. Goldman. "Further analysis of pemphigus autoantibodies and their use in studies on the heterogeneity, structure, and function of desmosomes." Journal of Cell Biology 102, no. 3 (1986): 1109–17. http://dx.doi.org/10.1083/jcb.102.3.1109.

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Pemphigus is an autoimmune disease that causes blistering of human epidermis. We have recently shown that autoantibodies in the serum of three pemphigus patients bind to desmosomes (Jones, J. C. R., J. Arnn, L. A. Staehelin, and R. D. Goldman, 1984, Proc. Natl. Acad. Sci. USA., 81:2781-2785), and we suggested that pemphigus blisters form, at least in part, from a specific antibody-induced disruption of desmosomes in the epidermis. In this paper, experiments are described that extend our initial observations. 13 pemphigus serum samples, which include four known pemphigus vulgaris (Pv) and four

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8

de Bruin, Alain, Reto Caldelari, Lina Williamson, et al. "Plakoglobin-dependent disruption of the desmosomal plaque in pemphigus vulgaris." Experimental Dermatology 16, no. 6 (2007): 468–75. http://dx.doi.org/10.1111/j.1600-0625.2007.00557.x.

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9

Chavez, Miquella G., Christian A. Buhr, Whitney K. Petrie, Angela Wandinger-Ness, Donna F. Kusewitt, and Laurie G. Hudson. "Differential Downregulation of E-Cadherin and Desmoglein by Epidermal Growth Factor." Dermatology Research and Practice 2012 (2012): 1–14. http://dx.doi.org/10.1155/2012/309587.

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Modulation of cell : cell junctions is a key event in cutaneous wound repair. In this study we report that activation of the epidermal growth factor (EGF) receptor disrupts cel : cell adhesion, but with different kinetics and fates for the desmosomal cadherin desmoglein and for E-cadherin. Downregulation of desmoglein preceded that of E-cadherinin vivoand in an EGF-stimulatedin vitrowound reepithelialization model. Dual immunofluorescence staining revealed that neither E-cadherin nor desmoglein-2 internalized with the EGF receptor, or with one another. In response to EGF, desmoglein-2 entered

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10

Caldelari, Reto, Alain de Bruin, Dominique Baumann, et al. "A Central Role for the Armadillo Protein Plakoglobin in the Autoimmune Disease Pemphigus Vulgaris." Journal of Cell Biology 153, no. 4 (2001): 823–34. http://dx.doi.org/10.1083/jcb.153.4.823.

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In pemphigus vulgaris (PV), autoantibody binding to desmoglein (Dsg) 3 induces loss of intercellular adhesion in skin and mucous membranes. Two hypotheses are currently favored to explain the underlying molecular mechanisms: (a) disruption of adhesion through steric hindrance, and (b) interference of desmosomal cadherin-bound antibody with intracellular events, which we speculated to involve plakoglobin. To investigate the second hypothesis we established keratinocyte cultures from plakoglobin knockout (PG−/−) embryos and PG+/+ control mice. Although both cell types exhibited desmosomal cadher

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