The effects of mechanical stretch on keratinocyte cell-cell adhesion

2017 ◽  
Vol 2017.29 (0) ◽  
pp. 1A15
Author(s):  
Katie R. Ryan ◽  
Akihisa Koyama ◽  
Katsuko S. Furukawa ◽  
Takashi Ushida
Keyword(s):  
Cell Adhesion ◽  
Mechanical Stretch ◽  
Keratinocyte Cell ◽  
Cell Cell

scholarly journals A role for the E-cadherin cell-cell adhesion molecule during tumor progression of mouse epidermal carcinogenesis.

1991 ◽  
Vol 115 (2) ◽  
pp. 517-533 ◽  
Author(s):  
P Navarro ◽  
M Gómez ◽  
A Pizarro ◽  
C Gamallo ◽  
M Quintanilla ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Lines ◽  
Spindle Cell ◽  
Inverse Correlation ◽  
Malignant Cell ◽  
Mouse Tumors ◽  
Keratinocyte Cell ◽  
Well Differentiated ◽  
E Cadherin ◽  
Cell Cell

The expression of the cell-cell adhesion molecules E- and P-cadherin has been analyzed in seven mouse epidermal keratinocyte cell lines representative of different stages of epidermal carcinogenesis. An inverse correlation between the amount of E-cadherin protein and tumorigenicity of the cell lines has been found, together with a complete absence of E-cadherin protein and mRNA expression in three carcinoma cell lines (the epithelioid HaCa4 and the fibroblastoid CarB and CarC cells). A similar result has been detected in tumors induced in nude mice by the cell lines, where induction of E-cadherin expression takes place in moderately differentiated squamous cell carcinomas induced by HaCa4 cells, although at much lower levels than in well-differentiated tumors induced by the epithelial PDV or PDVC57 cell lines. Complete absence of E-cadherin expression has been observed in spindle cell carcinomas induced by CarB or CarC cells. P-cadherin protein was detected in all cell lines that exhibit an epithelial (MCA3D, AT5, PDV, and PDVC57) or epithelioid (HaCa4) morphology, as well as in nude mouse tumors, independent of their tumorigenic capabilities. However, complete absence of P-cadherin was observed in the fibroblast-like cells (CarB and CarC) and in spindle cell carcinomas. The introduction of an exogenous E-cadherin cDNA into HaCa4 cells, or reactivation of the endogenous E-cadherin gene, leads to a partial suppression of the tumorigenicity of this highly malignant cell line. These results suggest a role for E-cadherin in the progression to malignancy of mouse epidermal carcinogenesis. They also suggest that the loss of both E- and P-cadherin could be associated to the final stage of carcinogenesis, the development of spindle cell carcinomas.

scholarly journals BRAF Modulates Stretch-Induced Intercellular Gap Formation through Localized Actin Reorganization

2021 ◽  
Vol 22 (16) ◽  
pp. 8989
Author(s):  
Anna Hollósi ◽  
Katalin Pászty ◽  
Miklós Kellermayer ◽  
Guillaume Charras ◽  
Andrea Varga
Keyword(s):  
Cell Adhesion ◽  
Barrier Function ◽  
Mechanical Stretch ◽  
Fiber Formation ◽  
Cell Junctions ◽  
Induced Response ◽  
Gap Formation ◽  
External Forces ◽  
Actin Cables ◽  
Cell Cell

Mechanical forces acting on cell–cell adhesion modulate the barrier function of endothelial cells. The actively remodeled actin cytoskeleton impinges on cell–cell adhesion to counteract external forces. We applied stress on endothelial monolayers by mechanical stretch to uncover the role of BRAF in the stress-induced response. Control cells responded to external forces by organizing and stabilizing actin cables in the stretched cell junctions. This was accompanied by an increase in intercellular gap formation, which was prevented in BRAF knockdown monolayers. In the absence of BRAF, there was excess stress fiber formation due to the enhanced reorganization of actin fibers. Our findings suggest that stretch-induced intercellular gap formation, leading to a decrease in barrier function of blood vessels, can be reverted by BRAF RNAi. This is important when the endothelium experiences changes in external stresses caused by high blood pressure, leading to edema, or by immune or cancer cells in inflammation or metastasis.

scholarly journals Mechanical stability of αT-catenin and its activation by force for vinculin binding

2019 ◽  
Vol 30 (16) ◽  
pp. 1930-1937 ◽  
Author(s):  
Si Ming Pang ◽  
Shimin Le ◽  
Adam V. Kwiatkowski ◽  
Jie Yan
Keyword(s):  
Cell Adhesion ◽  
Binding Site ◽  
Connexin 43 ◽  
Mechanical Stability ◽  
Critical Factor ◽  
Mechanical Stretch ◽  
Cell Junction ◽  
Unique Cell ◽  
Actomyosin Contraction ◽  
Cell Cell

αT (Testes)-catenin, a critical factor regulating cell–cell adhesion in the heart, directly couples the cadherin-catenin complex to the actin cytoskeleton at the intercalated disk (ICD), a unique cell–cell junction that couples cardiomyocytes. Loss of αT-catenin in mice reduces plakophilin2 and connexin 43 recruitment to the ICD. Since αT-catenin is subjected to mechanical stretch during actomyosin contraction in cardiomyocytes, its activity could be regulated by mechanical force. To provide insight in how force regulates αT-catenin function, we investigated the mechanical stability of the putative, force-sensing middle (M) domain of αT-catenin and determined how force impacts vinculin binding to αT-catenin. We show that 1) physiological levels of force, <15 pN, are sufficient to unfold the three M domains; 2) the M1 domain that harbors the vinculin-binding site is unfolded at ∼6 pN; and 3) unfolding of the M1 domain is necessary for high-affinity vinculin binding. In addition, we quantified the binding kinetics and affinity of vinculin to the mechanically exposed binding site in M1 and observed that αT-catenin binds vinculin with low nanomolar affinity. These results provide important new insights into the mechanosensing properties of αT-catenin and how αT-catenin regulates cell–cell adhesion at the cardiomyocyte ICD.

Tyrosine phosphorylation and SRC family kinases control keratinocyte cell-cell adhesion

1998 ◽  
Vol 16 ◽  
pp. S9 ◽  
Author(s):  
Enzo Calautti ◽  
Sara Cabodi ◽  
Nancy Kedersha ◽  
G.Paolo Dotto
Keyword(s):  
Cell Adhesion ◽  
Tyrosine Phosphorylation ◽  
Src Family Kinases ◽  
Keratinocyte Cell ◽  
Cell Cell

scholarly journals Stabilization of Plakoglobin and Enhanced Keratinocyte Cell-Cell Adhesion by IntracellularO-Glycosylation

2006 ◽  
Vol 281 (18) ◽  
pp. 12786-12791 ◽  
Author(s):  
Peiqi Hu ◽  
Paula Berkowitz ◽  
Victoria J. Madden ◽  
David S. Rubenstein
Keyword(s):  
Cell Adhesion ◽  
Keratinocyte Cell ◽  
Cell Cell

scholarly journals Cancer-associated fibroblasts regulate keratinocyte cell–cell adhesion via TGF-β-dependent pathways in genotype-specific oral cancer

2016 ◽  
Vol 38 (1) ◽  
pp. 76-85 ◽  
Author(s):  
N. Cirillo ◽  
Y. Hassona ◽  
A. Celentano ◽  
K.P. Lim ◽  
S. Manchella ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Oral Cancer ◽  
Cancer Associated Fibroblasts ◽  
Keratinocyte Cell ◽  
Cell Cell

scholarly journals Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell–cell adhesion

2002 ◽  
Vol 156 (1) ◽  
pp. 137-148 ◽  
Author(s):  
Enzo Calautti ◽  
Maddalena Grossi ◽  
Cristina Mammucari ◽  
Yumi Aoyama ◽  
Maria Pirro ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Kinase Activation ◽  
Positive Effects ◽  
Fyn Kinase ◽  
Keratinocyte Cell ◽  
Downstream Mediator ◽  
Cell Cell ◽  
Fyn Tyrosine Kinase

The Rho GTPase and Fyn tyrosine kinase have been implicated previously in positive control of keratinocyte cell–cell adhesion. Here, we show that Rho and Fyn operate along the same signaling pathway. Endogenous Rho activity increases in differentiating keratinocytes and is required for both Fyn kinase activation and increased tyrosine phosphorylation of β- and γ-catenin, which is associated with the establishment of keratinocyte cell–cell adhesion. Conversely, expression of constitutive active Rho is sufficient to promote cell–cell adhesion through a tyrosine kinase- and Fyn-dependent mechanism, trigger Fyn kinase activation, and induce tyrosine phosphorylation of β- and γ-catenin and p120ctn. The positive effects of activated Rho on cell–cell adhesion are not induced by an activated Rho mutant with defective binding to the serine/threonine PRK2/PKN kinases. Endogenous PRK2 kinase activity increases with keratinocyte differentiation, and, like activated Rho, increased PRK2 activity promotes keratinocyte cell–cell adhesion and induces tyrosine phosphorylation of β- and γ-catenin and Fyn kinase activation. Thus, these findings reveal a novel role of Fyn as a downstream mediator of Rho in control of keratinocyte cell–cell adhesion and implicate the PRK2 kinase, a direct Rho effector, as a link between Rho and Fyn activation.

622: Von Hippel-Lindau Inactivation Downregulates the Cell-Cell Adhesion Molecule E Cadherin in Renal Cancer Cells

2005 ◽  
Vol 173 (4S) ◽  
pp. 170-170
Author(s):  
Maxine G. Tran ◽  
Miguel A. Esteban ◽  
Peter D. Hill ◽  
Ashish Chandra ◽  
Tim S. O'Brien ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cancer Cells ◽  
Renal Cancer ◽  
Adhesion Molecule ◽  
Cell Adhesion Molecule ◽  
Von Hippel Lindau ◽  
E Cadherin ◽  
Cell Cell
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