scholarly journals Rac1 mediates laminar shear stress-induced vascular endothelial cell migration

2013 ◽  
Vol 7 (6) ◽  
pp. 472-478 ◽  
Author(s):  
Xianliang Huang ◽  
Yang Shen ◽  
Yi Zhang ◽  
Lin Wei ◽  
Yi Lai ◽  
...  
Keyword(s):  
Shear Stress ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial ◽  
Laminar Shear Stress ◽  
Laminar Shear

Autophagy Regulates Vascular Endothelial Cell eNOS and ET-1 Expression Induced by Laminar Shear Stress in an Ex Vivo Perfused System

2014 ◽  
Vol 42 (9) ◽  
pp. 1978-1988 ◽  
Author(s):  
Fengxia Guo ◽  
Xiaohong Li ◽  
Juan Peng ◽  
Yaling Tang ◽  
Qin Yang ◽  
...  
Keyword(s):  
Shear Stress ◽  
Endothelial Cell ◽  
Ex Vivo ◽  
Vascular Endothelial Cell ◽  
Vascular Endothelial ◽  
Laminar Shear Stress ◽  
Laminar Shear

CXCR1 and CXCR2 are novel mechano-sensors mediating laminar shear stress-induced endothelial cell migration

Cytokine ◽  
2011 ◽  
Vol 53 (1) ◽  
pp. 42-51 ◽  
Author(s):  
Ye Zeng ◽  
Hu-Rong Sun ◽  
Chang Yu ◽  
Yi Lai ◽  
Xiao-Jing Liu ◽  
...  
Keyword(s):  
Shear Stress ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Endothelial Cell Migration ◽  
Laminar Shear Stress ◽  
Laminar Shear

Laminar Shear Stress Promotes Vascular Endothelial Cell Autophagy Through Upregulation with Rab4

2016 ◽  
Vol 35 (3) ◽  
pp. 118-123 ◽  
Author(s):  
Pingbo Yao ◽  
Hong Zhao ◽  
Wenjuan Mo ◽  
Pingping He
Keyword(s):  
Shear Stress ◽  
Endothelial Cell ◽  
Vascular Endothelial Cell ◽  
Vascular Endothelial ◽  
Laminar Shear Stress ◽  
Laminar Shear

Wound Closure in Sheared Endothelial Cells is Enhanced by Modulation of Vascular Endothelial-Cadherin Expression and Localization

2002 ◽  
Vol 227 (11) ◽  
pp. 1006-1016 ◽  
Author(s):  
Maria Luiza C. Albuquerque ◽  
Annette S. Flozak
Keyword(s):  
Shear Stress ◽  
Endothelial Cell ◽  
Protein Expression ◽  
Wound Closure ◽  
Vascular Endothelial Cell ◽  
Vascular Endothelial ◽  
Laminar Shear Stress ◽  
Static Conditions ◽  
Laminar Shear ◽  
Cell Cell

We previously demonstrated that laminar shear stress enhances human coronary artery endothelial cell (HCAEC) wound closure via the mechanisms of cell spreading and migration. Because cell–cell junctional proteins such as vascular endothelial cell cadherin (VE–cadherin) are critical to cell–cell adhesion and motility, we tested the hypothesis that modulation of VE–cadherin expression under shear stress may be linked to this enhancement in wound closure. HCAEC monolayers were preconditioned to attain cellular alignment by shearing at 12 dynes/cm2 for 18 hr in a parallel-plate flow chamber. Subsequently, they were divided into the following three groups: (i) control; (ii) treated with anti-cadherin-5 antibody; or (iii) treated with the calcium chelating agent EGTA. Next, the monolayers were wounded with a metal spatula and resheared at 20 dynes/cm2 or left static. Time-lapse imaging was performed during the first 3 hr after imposition of these conditions, immunocytochemistry or Western blot analyses for VE–cadherin expression were performed on all wounded monolayers. Deconvolution microscopy, three-dimensional cell–cell junctional reconstruction images, and histogram analyses of interendothelial junction signal intensities were performed on cells at the wound edge of a monolayer. Under shear, HCAEC demonstrated increased VE–cadherin immunofluorescence and protein expression despite an enhancement in wound closure compared with static conditions. In separate experiments, application with anti-cadherin-5 antibody or treatment with EGTA attenuated VE–cadherin expression and further enhanced wound closure compared with control shear and all static conditions. In addition, the pattern of VE–cadherin localization with these treatments became more intracellular and nuclear in appearance. These findings of changes in this junctional adhesion protein expression and localization may further our understanding of laminar shear stress-induced endothelial repair in the coronary circulation.

Cyclic strain-mediated regulation of vascular endothelial cell migration and tube formation

2005 ◽  
Vol 329 (2) ◽  
pp. 573-582 ◽  
Author(s):  
Nicholas Von Offenberg Sweeney ◽  
Philip M. Cummins ◽  
Eoin J. Cotter ◽  
Paul A. Fitzpatrick ◽  
Yvonne A. Birney ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Vascular Endothelial Cell ◽  
Cyclic Strain ◽  
Tube Formation ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial

scholarly journals SENCR stabilizes vascular endothelial cell adherens junctions through interaction with CKAP4

2018 ◽  
Vol 116 (2) ◽  
pp. 546-555 ◽  
Author(s):  
Qing Lyu ◽  
Suowen Xu ◽  
Yuyan Lyu ◽  
Mihyun Choi ◽  
Christine K. Christie ◽  
...  
Keyword(s):  
Shear Stress ◽  
Endothelial Cell ◽  
Noncoding Rna ◽  
Rna Binding ◽  
Adherens Junctions ◽  
Vascular Endothelial Cell ◽  
Membrane Integrity ◽  
Laminar Shear Stress ◽  
Loss Of Function ◽  
Laminar Shear

SENCR is a human-specific, vascular cell-enriched long-noncoding RNA (lncRNA) that regulates vascular smooth muscle cell and endothelial cell (EC) phenotypes. The underlying mechanisms of action of SENCR in these and other cell types is unknown. Here, levels of SENCR RNA are shown to be elevated in several differentiated human EC lineages subjected to laminar shear stress. Increases in SENCR RNA are also observed in the laminar shear stress region of the adult aorta of humanized SENCR-expressing mice, but not in disturbed shear stress regions. SENCR loss-of-function studies disclose perturbations in EC membrane integrity resulting in increased EC permeability. Biotinylated RNA pull-down and mass spectrometry establish an abundant SENCR-binding protein, cytoskeletal-associated protein 4 (CKAP4); this ribonucleoprotein complex was further confirmed in an RNA immunoprecipitation experiment using an antibody to CKAP4. Structure–function studies demonstrate a noncanonical RNA-binding domain in CKAP4 that binds SENCR. Upon SENCR knockdown, increasing levels of CKAP4 protein are detected in the EC surface fraction. Furthermore, an interaction between CKAP4 and CDH5 is enhanced in SENCR-depleted EC. This heightened association appears to destabilize the CDH5/CTNND1 complex and augment CDH5 internalization, resulting in impaired adherens junctions. These findings support SENCR as a flow-responsive lncRNA that promotes EC adherens junction integrity through physical association with CKAP4, thereby stabilizing cell membrane-bound CDH5.

The Effect of Human Intraocular Fluid on Vascular Endothelial Cell Migration

Ophthalmology ◽  
1981 ◽  
Vol 88 (9) ◽  
pp. 986-991 ◽  
Author(s):  
Bert M. Glaser ◽  
Patricia A. D’Amore ◽  
Ronald G. Michels
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial ◽  
Intraocular Fluid

scholarly journals Progesterone enhances vascular endothelial cell migration via activation of focal adhesion kinase

2012 ◽  
Vol 16 (2) ◽  
pp. 296-305 ◽  
Author(s):  
Shuhui Zheng ◽  
Jinghe Huang ◽  
Kewen Zhou ◽  
Qiuling Xiang ◽  
Yaxing Zhang ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial

CYLD regulates angiogenesis by mediating vascular endothelial cell migration

Blood ◽  
2010 ◽  
Vol 115 (20) ◽  
pp. 4130-4137 ◽  
Author(s):  
Jinmin Gao ◽  
Lei Sun ◽  
Lihong Huo ◽  
Min Liu ◽  
Dengwen Li ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial Cell ◽  
Tube Formation ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial

Cylindromatosis (CYLD) is a deubiquitinase that was initially identified as a tumor suppressor and has recently been implicated in diverse normal physiologic processes. In this study, we have investigated the involvement of CYLD in angiogenesis, the formation of new blood vessels from preexisting ones. We find that knockdown of CYLD expression significantly impairs angiogenesis in vitro in both matrigel-based tube formation assay and collagen-based 3-dimensional capillary sprouting assay. Disruption of CYLD also remarkably inhibits angiogenic response in vivo, as evidenced by diminished blood vessel growth into the angioreactors implanted in mice. Mechanistic studies show that CYLD regulates angiogenesis by mediating the spreading and migration of vascular endothelial cells. Silencing of CYLD dramatically decreases microtubule dynamics in endothelial cells and inhibits endothelial cell migration by blocking the polarization process. Furthermore, we identify Rac1 activation as an important factor contributing to the action of CYLD in regulating endothelial cell migration and angiogenesis. Our findings thus uncover a previously unrecognized role for CYLD in the angiogenic process and provide a novel mechanism for Rac1 activation during endothelial cell migration and angiogenesis.

Alpha-Catulin Co-Localizes With Vimentin Intermediate Filaments and Functions in Pulmonary Vascular Endothelial Cell Migration via ROCK

2015 ◽  
Vol 231 (4) ◽  
pp. 934-943 ◽  
Author(s):  
Michael D. Bear ◽  
Tiegang Liu ◽  
Shereen Abualkhair ◽  
Maher A. Ghamloush ◽  
Nicholas S. Hill ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Intermediate Filaments ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial
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