scholarly journals Modeling of Aniridia-Related Keratopathy by CRISPR/Cas9 Genome Editing of Human Limbal Epithelial Cells and Rescue by Recombinant PAX6 Protein

Stem Cells ◽  
2018 ◽  
Vol 36 (9) ◽  
pp. 1421-1429 ◽  
Author(s):  
Lauriane N. Roux ◽  
Isabelle Petit ◽  
Romain Domart ◽  
Jean-Paul Concordet ◽  
Jieqiong Qu ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Genome Editing ◽  
Pax6 Protein

scholarly journals Efficient genome editing of differentiated renal epithelial cells

2016 ◽  
Vol 469 (2) ◽  
pp. 303-311 ◽  
Author(s):  
Alexis Hofherr ◽  
Tilman Busch ◽  
Nora Huber ◽  
Andreas Nold ◽  
Albert Bohn ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Genome Editing ◽  
Renal Epithelial Cells

scholarly journals Angulin-1 seals tricellular contacts independently of tricellulin and claudins

2021 ◽  
Vol 220 (9) ◽  
Author(s):  
Taichi Sugawara ◽  
Kyoko Furuse ◽  
Tetsuhisa Otani ◽  
Tomohiko Wakayama ◽  
Mikio Furuse
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Genome Editing ◽  
Tight Junctions ◽  
Barrier Function ◽  
Intercellular Space ◽  
Epithelial Barrier ◽  
Epithelial Barrier Function ◽  
C Terminus ◽  
Membrane Contact

Tricellular tight junctions (tTJs) are specialized tight junctions (TJs) that seal the intercellular space at tricellular contacts (TCs), where the vertices of three epithelial cells meet. Tricellulin and angulin family membrane proteins are known constituents of tTJs, but the molecular mechanism of tTJ formation remains elusive. Here, we investigated the roles of angulin-1 and tricellulin in tTJ formation in MDCK II cells by genome editing. Angulin-1–deficient cells lost the plasma membrane contact at TCs with impaired epithelial barrier function. The C terminus of angulin-1 bound to the TJ scaffold protein ZO-1, and disruption of their interaction influenced the localization of claudins at TCs, but not the tricellular sealing. Strikingly, the plasma membrane contact at TCs was formed in tricellulin- or claudin-deficient cells. These findings demonstrate that angulin-1 is responsible for the plasma membrane seal at TCs independently of tricellulin and claudins.

scholarly journals Angulin-1 seals tricellular contacts independently of tricellulin and claudins

2020 ◽  
Author(s):  
Taichi Sugawara ◽  
Kyoko Furuse ◽  
Tetsuhisa Otani ◽  
Mikio Furuse
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Genome Editing ◽  
Tight Junctions ◽  
Molecular Mechanism ◽  
Barrier Function ◽  
Intercellular Space ◽  
Epithelial Barrier ◽  
Epithelial Barrier Function ◽  
Membrane Contact

AbstractTricellular tight junctions (tTJs) are specialized tight junctions (TJs) that seal the intercellular space at tricellular contacts (TCs), where the vertices of three epithelial cells meet. Tricellulin and angulin family membrane proteins are known constituents of tTJs, but the molecular mechanism of tTJ formation remains elusive. Here, we investigated the roles of angulin-1 and tricellulin in tTJ formation in MDCK II cells by genome editing. Angulin-1-deficient cells lost the plasma membrane contact at TCs with impaired epithelial barrier function. The COOH-terminus of angulin-1 bound to the TJ scaffold protein ZO-1 and disruption of their interaction influenced the localization of claudins at TCs, but not the tricellular sealing. Strikingly, the plasma membrane contact at TCs was formed in tricellulin- or claudin-deficient cells. These findings demonstrate that angulin-1 is responsible for the plasma membrane seal at TCs independently of tricellulin and claudins.

Electron Microscopic Study of the Epithelium of the Seminal Vesicle of Aging Rats

1974 ◽  
Vol 32 ◽  
pp. 138-139
Author(s):  
V. F. Allison ◽  
G. C. Fink ◽  
G. W. Cearley
Keyword(s):  
Cell Growth ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Seminal Vesicle ◽  
Seminal Vesicles ◽  
Epithelial Layer ◽  
Epithelial Hyperplasia ◽  
Electron Microscopic ◽  
Aging Rats ◽  
Pseudostratified Epithelium

It is well known that epithelial hyperplasia (benign hypertrophy) is common in the aging prostate of dogs and man. In contrast, little evidence is available for abnormal epithelial cell growth in seminal vesicles of aging animals. Recently, enlarged seminal vesicles were reported in senescent mice, however, that enlargement resulted from increased storage of secretion in the lumen and occurred concomitant to epithelial hypoplasia in that species.The present study is concerned with electron microscopic observations of changes occurring in the pseudostratified epithelium of the seminal vescles of aging rats. Special attention is given to certain non-epithelial cells which have entered the epithelial layer.

The Ultrastructure of Monkey Gingival Epithelium

1967 ◽  
Vol 25 ◽  
pp. 16-17
Author(s):  
C.N. Sun
Keyword(s):  
Epithelial Cells ◽  
Macaca Nemestrina ◽  
Stratum Granulosum ◽  
Solution Ph ◽  
Gingival Epithelial Cells ◽  
Stratum Spinosum ◽  
Cell Layers ◽  
Gingival Epithelium ◽  
The Individual ◽  
Different Thickness

The present study demonstrates the ultrastructure of the gingival epithelium of the pig tail monkey (Macaca nemestrina). Specimens were taken from lingual and facial gingival surfaces and fixed in Dalton's chrome osmium solution (pH 7.6) for 1 hr, dehydrated, and then embedded in Epon 812.Tonofibrils are variable in number and structure according to the different region or location of the gingival epithelial cells, the main orientation of which is parallel to the long axis of the cells. The cytoplasm of the basal epithelial cells contains a great number of tonofilaments and numerous mitochondria. The basement membrane is 300 to 400 A thick. In the cells of stratum spinosum, the tonofibrils are densely packed and increased in number (fig. 1 and 3). They seem to take on a somewhat concentric arrangement around the nucleus. The filaments may occur scattered as thin fibrils in the cytoplasm or they may be arranged in bundles of different thickness. The filaments have a diameter about 50 A. In the stratum granulosum, the cells gradually become flatted, the tonofibrils are usually thin, and the individual tonofilaments are clearly distinguishable (fig. 2). The mitochondria and endoplasmic reticulum are seldom seen in these superficial cell layers.

Ultrastructural Changes Associated with Alcoholic Hyalin in Hepatocytes and Biliary Epithelial Cells

1971 ◽  
Vol 29 ◽  
pp. 572-573
Author(s):  
Odell T. Minick ◽  
Hidejiro Yokoo ◽  
Fawzia Batti
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Liver Biopsy ◽  
Alcoholic Hepatitis ◽  
Ultrastructural Changes ◽  
Main Mass ◽  
Biliary Epithelial Cells ◽  
Biopsy Specimens ◽  
Alcoholic Hyalin

To learn more of the nature and origin of alcoholic hyalin (AH), 15 liver biopsy specimens from patients with alcoholic hepatitis were studied in detail.AH was found not only in hepatocytes but also in ductular cells (Figs. 1 and 2), although in the latter location only rarely. The bulk of AH consisted of a randomly oriented network of closely packed filaments measuring about 150 Å in width. Bundles of filaments smaller in diameter (40-90 Å) were observed along the periphery of the main mass (Fig. 1), often surrounding it in a rim-like fashion. Fine filaments were also found close to the nucleus in both hepatocytes and biliary epithelial cells, the latter even though characteristic AH was not present (Figs. 3 and 4). Dispersed among the larger filaments were glycogen, RNA particles and profiles of endoplasmic reticulum. Dilated cisternae of endoplasmic reticulum were often conspicuous around the periphery of the AH mass. A limiting membrane was not observed.

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