scholarly journals E‐cadherin is downregulated in benign prostatic hyperplasia and required for tight junction formation and permeability barrier in the prostatic epithelial cell monolayer

The Prostate ◽  
2019 ◽  
Vol 79 (11) ◽  
pp. 1226-1237 ◽  
Author(s):  
Feng Li ◽  
Laura E. Pascal ◽  
Donna B. Stolz ◽  
Ke Wang ◽  
Yibin Zhou ◽  
...  
Keyword(s):  
Benign Prostatic Hyperplasia ◽  
Epithelial Cell ◽  
Tight Junction ◽  
Cell Monolayer ◽  
Prostatic Hyperplasia ◽  
Permeability Barrier ◽  
Tight Junction Formation ◽  
Junction Formation ◽  
Prostatic Epithelial Cell ◽  
E Cadherin

scholarly journals Shank2 Binds to aPKC and Controls Tight Junction Formation with Rap1 Signaling during Establishment of Epithelial Cell Polarity

Cell Reports ◽  
2020 ◽  
Vol 31 (1) ◽  
pp. 107407
Author(s):  
Kazunori Sasaki ◽  
Noriko Kojitani ◽  
Hiroko Hirose ◽  
Yohei Yoshihama ◽  
Hidefumi Suzuki ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Tight Junction ◽  
Cell Polarity ◽  
Epithelial Cell Polarity ◽  
Tight Junction Formation ◽  
Junction Formation

scholarly journals PALS1 Regulates E-Cadherin Trafficking in Mammalian Epithelial Cells

2007 ◽  
Vol 18 (3) ◽  
pp. 874-885 ◽  
Author(s):  
Qian Wang ◽  
Xiao-Wei Chen ◽  
Ben Margolis
Keyword(s):  
Tight Junction ◽  
Adherens Junction ◽  
Cell Periphery ◽  
Madin Darby Canine Kidney ◽  
Tight Junction Formation ◽  
Junction Protein ◽  
Evolutionarily Conserved ◽  
Junction Formation ◽  
Darby Canine Kidney ◽  
E Cadherin

Protein Associated with Lin Seven 1 (PALS1) is an evolutionarily conserved scaffold protein that targets to the tight junction in mammalian epithelia. Prior work in our laboratory demonstrated that the knockdown of PALS1 in Madin Darby canine kidney cells leads to tight junction and polarity defects. We have created new PALS1 stable knockdown cell lines with more profound reduction of PALS1 expression, and a more severe defect in tight junction formation was observed. Unexpectedly, we also observed a severe adherens junction defect, and both defects were corrected when PALS1 wild type and certain PALS1 mutants were expressed in the knockdown cells. We found that the adherens junction structural component E-cadherin was not effectively delivered to the cell surface in the PALS1 knockdown cells, and E-cadherin puncta accumulated in the cell periphery. The exocyst complex was also found to be mislocalized in PALS1 knockdown cells, potentially explaining why E-cadherin trafficking is disrupted. Our results suggest a broad and evolutionarily conserved role for the tight junction protein PALS1 in the biogenesis of adherens junction.

scholarly journals Claudins and JAM-A coordinately regulate tight junction formation and epithelial polarity

2019 ◽  
Vol 218 (10) ◽  
pp. 3372-3396 ◽  
Author(s):  
Tetsuhisa Otani ◽  
Thanh Phuong Nguyen ◽  
Shinsaku Tokuda ◽  
Kei Sugihara ◽  
Taichi Sugawara ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Tight Junction ◽  
Genome Editing ◽  
Epithelial Barrier ◽  
Permeability Barrier ◽  
Epithelial Polarity ◽  
Tight Junction Formation ◽  
Barrier Formation ◽  
Junction Formation ◽  
Epithelial Barriers

Tight junctions (TJs) establish the epithelial barrier and are thought to form a membrane fence to regulate epithelial polarity, although the roles of TJs in epithelial polarity remain controversial. Claudins constitute TJ strands in conjunction with the cytoplasmic scaffolds ZO-1 and ZO-2 and play pivotal roles in epithelial barrier formation. However, how claudins and other TJ membrane proteins cooperate to organize TJs remains unclear. Here, we systematically knocked out TJ components by genome editing and show that while ZO-1/ZO-2–deficient cells lacked TJ structures and epithelial barriers, claudin-deficient cells lacked TJ strands and an electrolyte permeability barrier but formed membrane appositions and a macromolecule permeability barrier. Moreover, epithelial polarity was disorganized in ZO-1/ZO-2–deficient cells, but not in claudin-deficient cells. Simultaneous deletion of claudins and a TJ membrane protein JAM-A resulted in a loss of membrane appositions and a macromolecule permeability barrier and in sporadic epithelial polarity defects. These results demonstrate that claudins and JAM-A coordinately regulate TJ formation and epithelial polarity.

A spectroscopic method for assessing confluence of epithelial cell cultures

1991 ◽  
Vol 261 (6) ◽  
pp. C1196-C1203 ◽  
Author(s):  
B. Jovov ◽  
N. K. Wills ◽  
S. A. Lewis
Keyword(s):  
Epithelial Cell ◽  
Tight Junction ◽  
Culture Media ◽  
Spectroscopic Method ◽  
Isosbestic Point ◽  
Epithelial Cell Line ◽  
Phenol Red ◽  
Renal Epithelial Cell ◽  
Tight Junction Formation ◽  
Junction Formation

We describe a convenient nonelectrophysiological technique for assessing cell proliferation and subsequent tight junction formation for epithelial monolayers grown on permeable supports. The method involves the use of phenol red (PR), a standard pH indicator in most cell culture media. In addition, we report a systematic error in a commercially available system for measuring transepithelial electrical properties. Briefly, the flux of PR across the epithelium was measured from the serosal solution into the mucosal solution. The mucosal solution was first replaced with a PR-free solution and then collected at timed intervals. The PR concentration was measured using a spectrophotometer set at the isosbestic point for PR (479 nm). PR flux was then calculated and used as an index of the permeability of the epithelium to PR. This method was tested using the renal epithelial cell line A6. After cell seeding, PR flux decreased in two phases: an initial large decrease, associated with cell growth and monolayer confluence, and a second decrease associated with tight junction formation [assessed by measuring transepithelial conductance (Gt)]. In addition to monitoring tight junction formation, PR flux measurements were also used to estimate the net movement of solution by the epithelial cells between the mucosal and serosal compartments. For convenience, Gt was initially measured in culture dishes using a commercially available “chopstick” electrode system. However, the chopstick system yielded Gt values that were on average 51% lower than values for the same preparations when measured in standard Ussing-type chambers. The discrepancy was due to a nonuniform current field produced by the chopstick electrodes.

scholarly journals The MAGUK Protein MPP7 Binds to the Polarity Protein hDlg1 and Facilitates Epithelial Tight Junction Formation

2007 ◽  
Vol 18 (5) ◽  
pp. 1744-1755 ◽  
Author(s):  
Volker M. Stucke ◽  
Evy Timmerman ◽  
Joel Vandekerckhove ◽  
Kris Gevaert ◽  
Alan Hall
Keyword(s):  
Epithelial Cell ◽  
Tight Junction ◽  
Tight Junctions ◽  
Cell Polarity ◽  
Functional Organization ◽  
Epithelial Cell Polarity ◽  
Tight Junction Formation ◽  
Evolutionarily Conserved ◽  
Junction Formation ◽  
Epithelial Tight Junction

Three groups of evolutionarily conserved proteins have been implicated in the establishment of epithelial cell polarity: the apically-localized proteins of the Par (Par3-Par6-aPKC-Cdc42) and Crumbs groups (Crb3-PALS1-PATJ) and the basolaterally localized proteins of the Dlg group (Dlg1-Scribble-Lgl). During epithelial morphogenesis, these proteins participate in a complex network of interdependent interactions that define the position and functional organization of adherens junctions and tight junctions. However, the biochemical pathways through which they control polarity are poorly understood. In this study, we identify an interaction between endogenous hDlg1 and MPP7, a previously uncharacterized MAGUK-p55 subfamily member. We find that MPP7 targets to the lateral surface of epithelial cells via its L27N domain, through an interaction with hDlg1. Loss of either hDlg1 or MPP7 from epithelial Caco-2 cells results in a significant defect in the assembly and maintenance of functional tight junctions. We conclude that the formation of a complex between hDlg1 and MPP7 promotes epithelial cell polarity and tight junction formation.

LXA4 stimulates ZO-1 expression and transepithelial electrical resistance in human airway epithelial (16HBE14o-) cells

2009 ◽  
Vol 296 (1) ◽  
pp. L101-L108 ◽  
Author(s):  
Yael Grumbach ◽  
Nga Vu Thi Quynh ◽  
Raphaël Chiron ◽  
Valérie Urbach
Keyword(s):  
Plasma Membrane ◽  
Tight Junction ◽  
Electrical Resistance ◽  
Cell Monolayer ◽  
Transepithelial Electrical Resistance ◽  
Biologically Active ◽  
Airway Epithelial ◽  
Tight Junction Formation ◽  
Junction Formation ◽  
Human Airways

Lipoxin A4 (LXA4) is a biologically active eicosanoid produced in human airways that displays anti-inflammatory properties. In cystic fibrosis and severe asthma, LXA4 production has been reported to be decreased, and, in such diseases, one of the consequences of airway inflammation is disruption of the tight junctions. In the present study, we investigated the possible role of LXA4 on tight junction formation, using transepithelial electrical resistance (TER) measurements, Western blotting, and immunofluorescence. We observed that exposure to LXA4 (100 nM) for 2 days significantly increased zonula occludens-1 (ZO-1), claudin-1, and occludin expression at the plasma membrane of confluent human bronchial epithelial 16HBE14o- cells. LXA4 (100 nM) stimulated the daily increase of the 16HBE14o- cell monolayer TER, and this effect was inhibited by boc-2 (LXA4 receptor antagonist). LXA4 also had a rapid effect on ZO-1 immunofluorescence at the plasma membrane and increased TER within 10 min. In conclusion, our experiments provide evidence that LXA4 plays certainly a new role for the regulation of tight junction formation and stimulation of the localization and expression of ZO-1 at the plasma membrane through a mechanism involving the LXA4 receptor.

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