scholarly journals Laminar Shear Stress Inhibits Vascular Endothelial Cell Proliferation by Inducing Cyclin-Dependent Kinase Inhibitor p21 Sdi1/Cip1/Waf1

2000 ◽  
Vol 86 (2) ◽  
pp. 185-190 ◽  
Author(s):  
Shigeo Akimoto ◽  
Masako Mitsumata ◽  
Toshiyuki Sasaguri ◽  
Yoji Yoshida
Keyword(s):  
Cell Proliferation ◽  
Shear Stress ◽  
Kinase Inhibitor ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Proliferation ◽  
Vascular Endothelial ◽  
Cyclin Dependent Kinase ◽  
Laminar Shear Stress ◽  
Cyclin Dependent Kinase Inhibitor ◽  
Laminar Shear

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

scholarly journals Resveratrol promotes endothelial cell wound healing under laminar shear stress through an estrogen receptor-α-dependent pathway

2014 ◽  
Vol 306 (6) ◽  
pp. H797-H806 ◽  
Author(s):  
Arif Yurdagul ◽  
James J. Kleinedler ◽  
Marshall C. McInnis ◽  
Alok R. Khandelwal ◽  
Allyson L. Spence ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Wound Healing ◽  
Shear Stress ◽  
Estrogen Receptor ◽  
Endothelial Cell ◽  
Endothelial Cell Proliferation ◽  
Laminar Shear Stress ◽  
Endothelial Cell Growth ◽  
Laminar Shear

Restenosis is an adverse outcome of angioplasty, characterized by vascular smooth muscle cell (VSMC) hyperplasia. However, therapies targeting VSMC proliferation delay reendothelialization, increasing the risk of thrombosis. Resveratrol (RESV) inhibits restenosis and promotes reendothelialization after arterial injury, but in vitro studies assessing RESV-mediated effects on endothelial cell growth contradict these findings. We thus hypothesized that fluid shear stress, mimicking physiological blood flow, would recapitulate RESV-dependent endothelial cell wound healing. Since RESV is an estrogen receptor (ER) agonist, we tested whether RESV promotes reendothelialization through an ER-α-dependent mechanism. Mice fed a high-fat diet or a diet supplemented with RESV were subjected to carotid artery injury. At 7 days after injury, RESV significantly accelerated reendothelialization compared with vehicle. In vitro wound healing assays demonstrated that RESV exhibits cell-type selectivity, inhibiting VSMC, but not endothelial cell growth. Under laminar shear stress (LSS), RESV dramatically enhanced endothelial cell wound healing and increased both the activation of extracellular signal-regulated kinase (ERK) and endothelial cell proliferation. Under LSS, small interfering RNA against ER-α, but not endothelial nitric oxide synthase, abolished RESV-induced ERK activation, endothelial cell proliferation, and wound healing. Thus these studies suggest that the EC phenotype induced by LSS better models the prohealing effects of RESV and that RESV and LSS interact to promote an ER-α-dependent mitogenic effect in endothelial cells.

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.

scholarly journals Transactivation of Fetal Liver Kinase-1/Kinase-Insert Domain-Containing Receptor by Lysophosphatidylcholine Induces Vascular Endothelial Cell Proliferation

Endocrinology ◽  
2006 ◽  
Vol 147 (3) ◽  
pp. 1377-1385 ◽  
Author(s):  
Yoshiko Fujita ◽  
Masanori Yoshizumi ◽  
Yuki Izawa ◽  
Nermin Ali ◽  
Hideki Ohnishi ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Endothelial Cell ◽  
Fetal Liver ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Proliferation ◽  
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.

scholarly journals Des-γ-carboxyl Prothrombin-promoted Vascular Endothelial Cell Proliferation and Migration

2007 ◽  
Vol 282 (12) ◽  
pp. 8741-8748 ◽  
Author(s):  
Tatsuya Fujikawa ◽  
Hidenori Shiraha ◽  
Naoki Ueda ◽  
Nobuyuki Takaoka ◽  
Yutaka Nakanishi ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Endothelial Cell ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Proliferation ◽  
Vascular Endothelial ◽  
Cell Proliferation And Migration ◽  
And Migration ◽  
Proliferation And Migration
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