scholarly journals Restoration of E-cadherin Cell-Cell Junctions Requires Both Expression of E-cadherin and Suppression of ERK MAP Kinase Activation in Ras-Transformed Breast Epithelial Cells

Neoplasia ◽  
2008 ◽  
Vol 10 (12) ◽  
pp. 1444-1458 ◽  
Author(s):  
Quanwen Li ◽  
Raymond R. Mattingly
Keyword(s):  
Epithelial Cells ◽  
Map Kinase ◽  
Cell Junctions ◽  
Breast Epithelial Cells ◽  
Kinase Activation ◽  
Breast Epithelial ◽  
E Cadherin ◽  
Cell Cell

scholarly journals Tumorigenic epithelial clusters are less sensitive to moderate osmotic stresses due to low amounts of junctional E-cadherin

2020 ◽  
Author(s):  
Danahe Mohammed ◽  
Park Young Chan ◽  
Jeffrey J. Fredberg ◽  
David A. Weitz
Keyword(s):  
Breast Cancer ◽  
Cell Migration ◽  
Epithelial Cells ◽  
Osmotic Stress ◽  
Metastatic Breast ◽  
Tumorigenic Cells ◽  
Breast Epithelial ◽  
The Impact ◽  
E Cadherin ◽  
Cell Cell

AbstractThe migration of tumorigenic epithelial cells is a critical step for metastatic breast cancer progression. Although the role of the extracellular matrix in breast cancer cell migration has been extensively described, the effect of osmotic stress on the migration of tumor breast epithelial cohorts remains unclear. Most of our understanding on the effect of osmotic stresses on cell migration comes from studies at the level of the single cell in isolation and does not take into account cell-cell interactions. Here, we study the impact of moderate osmotic stress on the migration of epithelial clusters composed of either non-tumorigenic or tumorigenic epithelial cells. We observe a decrease in migration distance and speed for non-tumorigenic epithelial cells but not for tumorigenic ones. To explain these differences, we investigate how osmotic stress impacts the mechanical properties of cell clusters and affects cell volumes. After application of osmotic stress renal epithelial cells become stiffer whereas non-tumorigenic and tumorigenic breast epithelial cells do not. In addition, tumorigenic cells are shown to be less sensitive to osmotic stress than non-tumorigenic cells, and this difference is associated with lower levels of E-cadherin expression. Using EGTA treatments, we confirm that the establishment of cell-cell adhesive interactions is a key component of the behavior of epithelial clusters in response to osmotic stress. This study provides evidence on the low sensitivity of tumorigenic epithelial clusters to moderate osmotic stress and highlights the importance of cadherin-based junctions in response to osmotic stress.

scholarly journals A role for a micron-scale supramolecular myosin array in adherens junction cytoskeletal assembly

2021 ◽  
Author(s):  
Hui-Chia Yu-Kemp ◽  
Rachel A. Szymanski ◽  
Nicole C. Gadda ◽  
Madeline L. Lillich ◽  
Mark Peifer
Keyword(s):  
Epithelial Cells ◽  
Cell Shape ◽  
Shape Change ◽  
Cell Junctions ◽  
Actin Assembly ◽  
Cell Shape Change ◽  
Micrometer Scale ◽  
Assembly Pathways ◽  
E Cadherin ◽  
Cell Cell

AbstractEpithelial cells assemble specialized actomyosin structures at E-Cadherin-based cell-cell junctions, and the force exerted drives cell shape change during morphogenesis. The mechanisms used to build this supramolecular actomyosin structure remain unclear. We used ZO-knockdown MDCK cells, which assemble a robust, polarized and highly organized actomyosin cytoskeleton at the zonula adherens, and combined genetic and pharmacological approaches with super-resolution microscopy to define molecular machines required. To our surprise, inhibiting individual actin assembly pathways (Arp2/3, formins or Ena/VASP) did not prevent or delay assembly of this polarized actomyosin structure. Instead, as junctions matured, micrometer-scale supramolecular myosin arrays assembled, with aligned stacks of myosin filaments adjacent to the apical membrane, while associated actin filaments remained disorganized. This suggested these myosin arrays might bundle actin at mature junctions. Consistent with this, inhibiting ROCK or myosin ATPase disrupted myosin localization/organization, and prevented actin bundling and polarization. These results suggest a novel mechanism by which myosin self-assembly helps drive actin organization to facilitate cell shape change.SummaryWe explored mechanisms epithelial cells use to assemble supramolecular actomyosin structures at E-Cadherin-based cell-cell junctions. Our data suggest individual actin assembly pathways are not essential. Instead, microscopy and pharmacological inhibition suggest micrometer-scale supramolecular myosin arrays help bundle actin at mature junctions.

scholarly journals Inhibition of PTP1B disrupts cell–cell adhesion and induces anoikis in breast epithelial cells

2017 ◽  
Vol 8 (5) ◽  
pp. e2769-e2769 ◽  
Author(s):  
Bylgja Hilmarsdottir ◽  
Eirikur Briem ◽  
Skarphedinn Halldorsson ◽  
Jennifer Kricker ◽  
Sævar Ingthorsson ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Breast Epithelial Cells ◽  
Breast Epithelial ◽  
Cell Cell

scholarly journals Loss of Tpm4.1 leads to disruption of cell-cell adhesions and invasive behavior in breast epithelial cells via increased Rac1 signaling

Oncotarget ◽  
2017 ◽  
Vol 8 (20) ◽  
pp. 33544-33559 ◽  
Author(s):  
SukYeong Jeong ◽  
SunYoung Lim ◽  
Galina Schevzov ◽  
Peter W. Gunning ◽  
David M. Helfman
Keyword(s):  
Epithelial Cells ◽  
Breast Epithelial Cells ◽  
Invasive Behavior ◽  
Breast Epithelial ◽  
Cell Adhesions ◽  
Cell Cell
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