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Epiplakin

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https://www.readbyqxmd.com/read/27206504/effects-of-epiplakin-knockdown-in-cultured-corneal-epithelial-cells
#1
Masahide Kokado, Yuka Okada, Takeshi Miyamoto, Osamu Yamanaka, Shizuya Saika
BACKGROUND: To investigate effects of knockdown of epiplakin gene expression on the homeostasis of cultured corneal epithelial cell line. We previously reported acceleration of corneal epithelial wound healing in an epiplakin-null mouse. METHODS: Gene expression of epiplakin was knockdowned by employing siRNA transfection in SV40-immortalized human corneal epithelial cell line. Protein expression of E-cadherin, keratin 6 and vimentin was examined by western blotting...
2016: BMC Research Notes
https://www.readbyqxmd.com/read/26802236/epiplakin-is-a-paraneoplastic-pemphigus-autoantigen-and-related-to-bronchiolitis-obliterans-in-japanese-patients
#2
COMPARATIVE STUDY
Atsunari Tsuchisaka, Sanae Numata, Kwesi Teye, Yohei Natsuaki, Tamihiro Kawakami, Yoshito Takeda, Wenqing Wang, Kazushi Ishikawa, Mizuki Goto, Hiroshi Koga, Ryosuke Sogame, Norito Ishii, Shinzo Takamori, Tomoaki Hoshino, Oliver Brandt, Hendri H Pas, Sakuhei Fujiwara, Takashi Hashimoto
All plakin family proteins are known to be autoantigens in paraneoplastic pemphigus (PNP). In this study, we first examined whether PNP sera also react with epiplakin, another plakin protein, by various immunological methods using 48 Japanese PNP sera. Immunofluorescence confirmed that cultured keratinocytes expressed epiplakin. Epiplakin was detected by 72.9% of PNP sera by immunoprecipitation-immunoblotting with KU-8 cell extract, but not by immunoblotting of either normal human epidermal extract or KU-8 cell extract...
February 2016: Journal of Investigative Dermatology
https://www.readbyqxmd.com/read/26778563/functional-and-genetic-analysis-of-epiplakin-in-epithelial-cells
#3
REVIEW
Sandra Szabo, Karl L Wögenstein, Peter Fuchs
Epiplakin is a large member (>700 kDa) of the plakin protein family and exclusively expressed in epithelial cell types. Compared to other plakin proteins epiplakin exhibits an unusual structure as it consists entirely of a variable number of consecutive plakin repeat domains (13 in humans, 16 in mice). The only binding partners of epiplakin identified so far are keratins of simple as well as of stratified epithelia. Epiplakin-deficient mice show no obvious spontaneous phenotype. However, ex vivo studies using epiplakin-deficient primary cells indicated protective functions of epiplakin in response to stress...
2016: Methods in Enzymology
https://www.readbyqxmd.com/read/26480281/epiplakin-is-a-paraneoplastic-pemphigus-autoantigen-and-related-to-bronchiolitis-obliterans-in-japanese-patients
#4
Atsunari Tsuchisaka, Sanae Numata, Kwesi Teye, Yohei Natsuaki, Tamihiro Kawakami, Yoshito Takeda, Wenqing Wang, Kazushi Ishikawa, Mizuki Goto, Hiroshi Koga, Ryosuke Sogame, Norito Ishii, Shinzo Takamori, Tomoaki Hoshino, Oliver Brandt, Hendri H Pas, Sakuhei Fujiwara, Takashi Hashimoto
All plakin family proteins are known to be autoantigens in paraneoplastic pemphigus (PNP). In this study, we first examined whether PNP sera also react with epiplakin, another plakin protein, by various immunological methods using 48 Japanese PNP sera. Immunofluorescence confirmed that cultured keratinocytes expressed epiplakin. Epiplakin was detected by 72.9% of PNP sera by immunoprecipitation-immunoblotting with KU-8 cell extract, but not by immunoblotting of either normal human epidermal extract or KU-8 cell extract...
October 19, 2015: Journal of Investigative Dermatology
https://www.readbyqxmd.com/read/25617501/epiplakin-attenuates-experimental-mouse-liver-injury-by-chaperoning-keratin-reorganization
#5
Sandra Szabo, Karl L Wögenstein, Christoph H Österreicher, Nurdan Guldiken, Yu Chen, Carina Doler, Gerhard Wiche, Peter Boor, Johannes Haybaeck, Pavel Strnad, Peter Fuchs
BACKGROUND & AIMS: Epiplakin is a member of the plakin protein family and exclusively expressed in epithelial tissues where it binds to keratins. Epiplakin-deficient (Eppk1(-/-)) mice displayed no obvious spontaneous phenotype, but their keratinocytes showed a faster keratin network breakdown in response to stress. The role of epiplakin in the stressed liver remained to be elucidated. METHODS: Wild-type (WT) and Eppk1(-/-) mice were subjected to common bile duct ligation (CBDL) or fed with a 3,5-diethoxycarbonyl-1,4-dihydrocollidine (DDC)-containing diet...
June 2015: Journal of Hepatology
https://www.readbyqxmd.com/read/25232867/epiplakin-deficiency-aggravates-murine-caerulein-induced-acute-pancreatitis-and-favors-the-formation-of-acinar-keratin-granules
#6
Karl L Wögenstein, Sandra Szabo, Mariia Lunova, Gerhard Wiche, Johannes Haybaeck, Pavel Strnad, Peter Boor, Martin Wagner, Peter Fuchs
Epiplakin, a member of the plakin protein family, is exclusively expressed in epithelial tissues and was shown to bind to keratins. Epiplakin-deficient (EPPK-/-) mice showed no obvious spontaneous phenotype, however, EPPK-/- keratinocytes displayed faster keratin network breakdown in response to stress. The role of epiplakin in pancreas, a tissue with abundant keratin expression, was not yet known. We analyzed epiplakin's expression in healthy and inflamed pancreatic tissue and compared wild-type and EPPK-/- mice during caerulein-induced acute pancreatitis...
2014: PloS One
https://www.readbyqxmd.com/read/24769843/asymmetric-synthesis-of-3-3-5-5-tetrasubstituted-1-2-dioxolanes-total-synthesis-of-epiplakinic-acid-f
#7
Xiang-Yin Tian, Jian-Wei Han, Qiong Zhao, Henry N C Wong
The first enantioselective total synthesis of epiplakinic acid F (1) was achieved through a pivotal step involving a radical-mediated asymmetric peroxidation of vinylcyclopropanes with molecular oxygen to construct highly substituted 1,2-dioxolanes. Subsequent conversions of the chiral 1,2-dioxolanes led to total synthesis of epiplakinic acid F (1) and the confirmation of its absolute configuration. The enantiomer of epiplakinic acid F methyl ester (2) was also prepared.
June 14, 2014: Organic & Biomolecular Chemistry
https://www.readbyqxmd.com/read/24352042/plakins-a-versatile-family-of-cytolinkers-roles-in-skin-integrity-and-in-human-diseases
#8
REVIEW
Jamal-Eddine Bouameur, Bertrand Favre, Luca Borradori
The plakin family consists of giant proteins involved in the cross-linking and organization of the cytoskeleton and adhesion complexes. They further modulate several fundamental biological processes, such as cell adhesion, migration, and polarization or signaling pathways. Inherited and acquired defects of plakins in humans and in animal models potentially lead to dramatic manifestations in the skin, striated muscles, and/or nervous system. These observations unequivocally demonstrate the key role of plakins in the maintenance of tissue integrity...
April 2014: Journal of Investigative Dermatology
https://www.readbyqxmd.com/read/23599337/increased-fragility-impaired-differentiation-and-acceleration-of-migration-of-corneal-epithelium-of-epiplakin-null-mice
#9
Masahide Kokado, Yuka Okada, Mizuki Goto, Kazushi Ishikawa, Takeshi Miyamoto, Osamu Yamanaka, Sakuhei Fujiwara, Shizuya Saika
PURPOSE: To investigate the effects of gene ablation of epiplakin on the homeostasis of corneal epithelium in mice. METHODS: Light and transmission electron microscopic histology, immunohistochemistry, and real-time RT-PCR were carried out to evaluate the effects of the loss of epiplakin on structure and gene expression of cell-cell adhesion-related components in mice. Integrity against mechanical intervention and wound-healing response of corneal epithelium were also tested...
May 2013: Investigative Ophthalmology & Visual Science
https://www.readbyqxmd.com/read/23398049/epiplakin-modifies-the-motility-of-the-hela-cells-and-accumulates-at-the-outer-surfaces-of-3-d-cell-clusters
#10
Hiromitsu Shimada, Akiko Nambu-Niibori, Masayo Wilson-Morifuji, Souhei Mizuguchi, Norie Araki, Hideaki Sumiyoshi, Mitsuru Sato, Yoshihiro Mezaki, Haruki Senoo, Kazushi Ishikawa, Yutaka Hatano, Osamu Okamoto, Sakuhei Fujiwara
Elimination of epiplakin (EPPK) by gene targeting in mice results in acceleration of keratinocyte migration during wound healing, suggesting that epithelial cellular EPPK may be important for the regulation of cellular motility. To study the function of EPPK, we developed EPPK knock-down (KD) and EPPK-overexpressing HeLa cells and analyzed cellular phenotypes and motility by fluorescence/differential interference contrast time-lapse microscopy and immunolocalization of actin and vimentin. Cellular motility of EPPK-KD cells was significantly elevated, but that of EPPK-overexpressing cells was obviously depressed...
April 2013: Journal of Dermatology
https://www.readbyqxmd.com/read/20926261/epiplakin-accelerates-the-lateral-organization-of-keratin-filaments-during-wound-healing
#11
Kazushi Ishikawa, Hideaki Sumiyoshi, Noritaka Matsuo, Naoko Takeo, Mizuki Goto, Osamu Okamoto, Shuji Tatsukawa, Hirokazu Kitamura, Yoshihisa Fujikura, Hidekatsu Yoshioka, Sakuhei Fujiwara
BACKGROUND: Epiplakin (EPPK) belongs to the plakin family of cytolinker proteins and, resembling other members of the plakin family such as BPAG1 (an autoantigen of bullous pemphigoid) and plectin, EPPK has plakin repeat domains (PRDs) that bind to intermediate filaments. Elimination of EPPK by gene targeting in mice resulted in the acceleration of keratinocyte migration during wound healing. EPPK is expressed in proliferating keratinocytes at wound edges and, in view of its putative function in binding to keratin, we postulated that the keratin network in EPPK-null (EPPK(-/-)) mice might be disrupted during wound healing...
November 2010: Journal of Dermatological Science
https://www.readbyqxmd.com/read/20923180/bioactive-cycloperoxides-isolated-from-the-puerto-rican-sponge-plakortis-halichondrioides
#12
Carlos Jiménez-Romero, Idelisse Ortiz, Jan Vicente, Brunilda Vera, Abimael D Rodríguez, Sangkil Nam, Richard Jove
Two new five-membered-ring polyketide endoperoxides, epiplakinic acid F methyl ester (1) and epiplakinidioic acid (3), and a peroxide-lactone, plakortolide J (2), were isolated from the Puerto Rican sponge Plakortis halichondrioides, along with two previously reported cyclic peroxides, 4 and 5. The structures of the new metabolites were determined by spectroscopic and chemical analyses. The absolute stereostructures of 1, 2, and 5 were determined by degradation reactions followed by application of Kishi's method for the assignment of absolute configuration of alcohols...
October 22, 2010: Journal of Natural Products
https://www.readbyqxmd.com/read/18285451/stress-induced-recruitment-of-epiplakin-to-keratin-networks-increases-their-resistance-to-hyperphosphorylation-induced-disruption
#13
Daniel Spazierer, Julia Raberger, Karin Gross, Peter Fuchs, Gerhard Wiche
Epiplakin is a large (>725 kDa) cytoskeletal protein exclusively expressed in epithelial tissues. It has a unique structure, consisting entirely of plakin repeat domains (PRDs), one of the hallmarks of spectraplakin protein family members. Previous studies, including the phenotypic analyses of knockout mice, failed to reveal the biological function of epiplakin. Using in vitro binding assays, we show here that all but one of the 16 PRDs of mouse epiplakin bind to keratins of basal keratinocytes. Nevertheless, in primary keratinocyte cell cultures, epiplakin only partially colocalized with keratin intermediate filament networks...
March 15, 2008: Journal of Cell Science
https://www.readbyqxmd.com/read/17499243/plakins-in-development-and-disease
#14
REVIEW
Arnoud Sonnenberg, Ronald K H Liem
Plakins are large multi-domain molecules that have various functions to link cytoskeletal elements together and to connect them to junctional complexes. Plakins were first identified in epithelial cells where they were found to connect the intermediate filaments to desmosomes and hemidesmosomes [Ruhrberg, C., and Watt, F.M. (1997). The plakin family: versatile organizers of cytoskeletal architecture. Curr Opin Genet Dev 7, 392-397.]. They were subsequently found to be important for the integrity of muscle cells...
June 10, 2007: Experimental Cell Research
https://www.readbyqxmd.com/read/17244023/identification-of-markers-for-nipple-epidermis-changes-in-expression-during-pregnancy-and-lactation
#15
Jennifer Eastwood, Carlos Offutt, Keshav Menon, Mitchell Keel, Petra Hrncirova, Milos V Novotny, Randy Arnold, John Foley
In vertebrates, specific regions of skin crucial for interaction with and manipulation of elements in the environment are characterized by specialized epidermis. Regions of specialized epidermis show distinct patterns of cellular differentiation and express specific keratins that provide an increased ability to withstand mechanical strain. The nipple, which must endure the mechanical strain of nursing, is a type of specialized epidermis. The entire ventral skin of the keratin 14 promoter driven PTHrP mouse provides a model for nipple development...
January 2007: Differentiation; Research in Biological Diversity
https://www.readbyqxmd.com/read/16923132/interactions-between-epiplakin-and-intermediate-filaments
#16
Wenqing Wang, Hideaki Sumiyoshi, Hidekatsu Yoshioka, Sakuhei Fujiwara
Epiplakin, a cytoskeletal linker protein, was originally identified as an autoantigen in a serum specimen obtained from a patient with subepidermal blistering disease. To examine the binding ability of epiplakin with intermediate filaments (IF), we performed slot-blot assays using fusion proteins that included various domains and subdomains of epiplakin. At least two of the 4.6 copies in the B domains of epiplakin were necessary for the binding of fusion proteins to keratin. The repeated structures of linker domains also played an important role in the binding of epiplakin to keratin in these assays while also increasing the repeated structure in the linker domain of epiplakin which is involved in the increased binding to IF...
August 2006: Journal of Dermatology
https://www.readbyqxmd.com/read/16382147/epiplakin-is-dispensable-for-skin-barrier-function-and-for-integrity-of-keratin-network-cytoarchitecture-in-simple-and-stratified-epithelia
#17
Daniel Spazierer, Peter Fuchs, Siegfried Reipert, Irmgard Fischer, Matthias Schmuth, Hans Lassmann, Gerhard Wiche
Epiplakin, a giant epithelial protein of >700 kDa, belongs to the plakin family of cytolinker proteins. It represents an atypical family member, however, as it consists entirely of plakin repeat domains but lacks any of the other domains commonly shared by plakins. Hence, its putative function as a cytolinker protein remains to be shown. To investigate epiplakin's biological role, we generated epiplakin-deficient mice by gene targeting in embryonic stem cells. Epiplakin-deficient mice were viable and fertile, without developing any discernible phenotype...
January 2006: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/16382146/elimination-of-epiplakin-by-gene-targeting-results-in-acceleration-of-keratinocyte-migration-in-mice
#18
Mizuki Goto, Hideaki Sumiyoshi, Takao Sakai, Reinhard Fässler, Shihoka Ohashi, Eijiro Adachi, Hidekatsu Yoshioka, Sakuhei Fujiwara
Epiplakin (EPPK) was originally identified as a human epidermal autoantigen. To identify the function of epiplakin, we generated epiplakin "knockout" mice. These mice developed normally, with apparently normal epidermis and hair. Electron microscopy after immunostaining revealed the presence of EPPK adjacent to keratin filaments in wild-type mice, suggesting that epiplakin might associate with keratin. The appearance and localization of keratin bundles in intact epidermal keratinocytes of EPPK-/- mice were similar to those in wild-type mice...
January 2006: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/15671067/characterization-of-human-epiplakin-rnai-mediated-epiplakin-depletion-leads-to-the-disruption-of-keratin-and-vimentin-if-networks
#19
Shyh-Ing Jang, Alexandr Kalinin, Kaoruko Takahashi, Lyuben N Marekov, Peter M Steinert
Epiplakin is a member of the plakin family with multiple copies of the plakin repeat domain (PRD). We studied the subcellular distribution and interactions of human epiplakin by immunostaining, overlay assays and RNAi knockdown. Epiplakin decorated the keratin intermediate filaments (IF) network and partially that of vimentin. In the binding assays, the repeat unit (PRD plus linker) showed strong binding and preferentially associated with assembled IF over keratin monomers. Epiplakin knockdown revealed disruption of IF networks in simple epithelial but not in epidermal cells...
February 15, 2005: Journal of Cell Science
https://www.readbyqxmd.com/read/12853460/trichohyalin-mechanically-strengthens-the-hair-follicle-multiple-cross-bridging-roles-in-the-inner-root-shealth
#20
Peter M Steinert, David A D Parry, Lyuben N Marekov
Trichohyalin is expressed in specialized epithelia that are unusually mechanically strong, such as the inner root sheath cells of the hair follicle. We have previously shown that trichohyalin is sequentially subjected to post-synthetic modifications by peptidylarginine deaminases, which convert many of its arginines to citrullines, and by transglutaminases, which introduce intra- and interprotein chain cross-links. Here we have characterized in detail the proteins to which it becomes cross-linked in vivo in the inner root sheath of the mouse hair follicle...
October 17, 2003: Journal of Biological Chemistry
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