scholarly journals Regulation of epithelial cell adhesion and repulsion: role of endocytic recycling

2008 ◽  
Vol 55 (1,2) ◽  
pp. 9-16 ◽  
Author(s):  
Noriyuki Nishimura ◽  
Takuya Sasaki
2001 ◽  
Vol 266 (2) ◽  
pp. 311-322 ◽  
Author(s):  
Mitsuo Shimizu ◽  
Kazunobu Minakuchi ◽  
Ayako Tsuda ◽  
Takachika Hiroi ◽  
Noboru Tanaka ◽  
...  

2012 ◽  
Vol 41 (6) ◽  
pp. 2150-2158 ◽  
Author(s):  
JUN SANG BAE ◽  
SANG JAE NOH ◽  
KYU YUN JANG ◽  
HO SUNG PARK ◽  
MYOUNG JA CHUNG ◽  
...  

1996 ◽  
Vol 133 (3) ◽  
pp. 695-708 ◽  
Author(s):  
G M Zinkl ◽  
A Zuk ◽  
P van der Bijl ◽  
G van Meer ◽  
K S Matlin

Epithelial cells polarize not only in response to cell-cell contacts, but also to contacts with a substratum composed of extracellular matrix molecules. To probe the role of specific matrix constituents in epithelial cell polarization, we investigated the effects of an adhesion-blocking mAb, 12B12, on initial polarization of MDCK cells. The 12B12 antibody, raised against whole MDCK cells, blocks adhesion to laminin by 65% but has no effect on adhesion of cells to collagen type I. Taking advantage of this antibody's function-blocking activity, as well as the fact that MDCK cells secrete laminin, the role of endogenous laminin in polarization was examined by plating cells on collagen-coated substrata in the presence of the antibody. Under these conditions, cell spreading was reduced 1.5h after plating, and cells were flatter and had fewer microvilli after 24 h. Even though lateral cell membranes were closely apposed, transepithelial resistance in the presence of the antibody was significantly reduced relative to controls. When the polarization of specific apical and basolateral markers was examined both biochemically and immunocytochemically in the presence of the antibody, we observed that the apical marker polarized at normal rates while basolateral markers did not. Surprisingly, the 12B12 antibody was not directed against any known cell adhesion protein but reacted specifically with Forssman antigen, a glycosphingolipid. These results suggest that glycolipids may play a significant role in cell adhesion via laminin and in epithelial cell polarization.


2011 ◽  
Vol 102 (8) ◽  
pp. 1493-1500 ◽  
Author(s):  
Tetsunari Hase ◽  
Mitsuo Sato ◽  
Kenya Yoshida ◽  
Luc Girard ◽  
Yoshihiro Takeyama ◽  
...  

1994 ◽  
Vol 2 (5) ◽  
pp. 417-428 ◽  
Author(s):  
Sergey V. Litvinov ◽  
Hellen A. M. Bakker ◽  
Maia M. Gourevitch ◽  
Markwin P. Velders ◽  
Sven O. Warnaar

2003 ◽  
Vol 163 (1) ◽  
pp. 165-176 ◽  
Author(s):  
Masaki Shigeta ◽  
Noriko Sanzen ◽  
Masayuki Ozawa ◽  
Jianguo Gu ◽  
Hitoshi Hasegawa ◽  
...  

CD151, a member of the tetraspanin family proteins, tightly associates with integrin α3β1 and localizes at basolateral surfaces of epithelial cells. We found that overexpression of CD151 in A431 cells accelerated intercellular adhesion, whereas treatment of cells with anti-CD151 mAb perturbed the integrity of cortical actin filaments and cell polarity. E-Cadherin puncta formation, indicative of filopodia-based adhesion zipper formation, as well as E-cadherin anchorage to detergent-insoluble cytoskeletal matrix, was enhanced in CD151-overexpressing cells. Levels of GTP-bound Cdc42 and Rac were also elevated in CD151-overexpressing cells, suggesting the role of CD151 in E-cadherin–mediated cell–cell adhesion as a modulator of actin cytoskeletal reorganization. Consistent with this possibility, engagement of CD151 by the substrate-adsorbed anti-CD151 mAb induced prominent Cdc42-dependent filopodial extension, which along with E-cadherin puncta formation, was strongly inhibited by calphostin C, a protein kinase C (PKC) inhibitor. Together, these results indicate that CD151 is involved in epithelial cell–cell adhesion as a modulator of PKC- and Cdc42-dependent actin cytoskeletal reorganization.


2019 ◽  
Vol 317 (5) ◽  
pp. G580-G591 ◽  
Author(s):  
Barun Das ◽  
Kevin Okamoto ◽  
John Rabalais ◽  
Philip A. Kozan ◽  
Ronald R. Marchelletta ◽  
...  

Congenital tufting enteropathy (CTE) is an autosomal recessive disease characterized by severe intestinal failure in infancy and mutations in the epithelial cell adhesion molecule ( EPCAM) gene. Previous studies of CTE in mice expressing mutant EpCAM show neonatal lethality. Hence, to study the cellular, molecular, and physiological alterations that result from EpCAM mutation, a tamoxifen-inducible mutant EpCAM enteroid model has been generated. The presence of mutant EpCAM in the model was confirmed at both mRNA and protein levels. Immunofluorescence microscopy demonstrated the reduced expression of mutant EpCAM. Mutant enteroids had reduced budding potential as well as significantly decreased mRNA expression for epithelial lineage markers ( Mucin 2, lysozyme, sucrase-isomaltase), proliferation marker Ki67, and secretory pathway transcription factors ( Atoh1, Hnf1b). Significantly decreased numbers of Paneth and goblet cells were confirmed by staining. These findings were correlated with intestinal tissue from CTE patients and the mutant mice model that had significantly fewer Paneth and goblet cells than in healthy counterparts. FITC-dextran studies demonstrated significantly impaired barrier function in monolayers derived from mutant enteroids compared with control monolayers. In conclusion, we have established an ex vivo CTE model. The role of EpCAM in the budding potential, differentiation, and barrier function of enteroids is noted. Our study establishes new facets of EpCAM biology that will aid in understanding the pathophysiology of CTE and role of EpCAM in health and disease. NEW & NOTEWORTHY Here, we develop a novel ex vivo enteroid model for congenital tufting enteropathy (CTE) based on epithelial cell adhesion molecule ( EPCAM) gene mutations found in patients. With this model we demonstrate the role of EpCAM in maintaining the functional homeostasis of the intestinal epithelium, including differentiation, proliferation, and barrier integrity. This study further establishes a new direction in EpCAM biology that will help in understanding the detailed pathophysiology of CTE and role of EpCAM.


2001 ◽  
Vol 276 (24) ◽  
pp. 21714-21723 ◽  
Author(s):  
Zhiyi Cao ◽  
Zheng Zhao ◽  
Royce Mohan ◽  
Joseph Alroy ◽  
Pamela Stanley ◽  
...  

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