scholarly journals Microcystin-leucine arginine blocks vasculogenesis and angiogenesis through impairing cytoskeleton and impeding endothelial cell migration by downregulating integrin-mediated Rho/ROCK signaling pathway

2021 ◽  
Author(s):  
Qilong Wang ◽  
Guoliang Chen ◽  
Qian Zhang ◽  
Mingxing Wang ◽  
Guixue Wang ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Signaling Pathway ◽  
Endothelial Cell Migration ◽  
Vasculogenesis And Angiogenesis

scholarly journals CRIF1 deficiency suppresses endothelial cell migration via upregulation of RhoGDI2

PLoS ONE ◽  
2021 ◽  
Vol 16 (8) ◽  
pp. e0256646
Author(s):  
Harsha Nagar ◽  
Seonhee Kim ◽  
Ikjun Lee ◽  
Su-Jeong Choi ◽  
Shuyu Piao ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Signaling Pathway ◽  
Umbilical Vein ◽  
Vascular Endothelial Cell ◽  
Cellular Migration ◽  
Endothelial Cell Migration ◽  
Migration And Invasion ◽  
Mitochondrial Functions

Rho GDP-dissociation inhibitor (RhoGDI), a downregulator of Rho family GTPases, prevents nucleotide exchange and membrane association. It is responsible for the activation of Rho GTPases, which regulate a variety of cellular processes, such as migration. Although RhoGDI2 has been identified as a tumor suppressor gene involved in cellular migration and invasion, little is known about its role in vascular endothelial cell (EC) migration. CR6-interacting factor 1 (CRIF1) is a CR6/GADD45-interacting protein with important mitochondrial functions and regulation of cell growth. We examined the expression of RhoGDI2 in CRIF1-deficient human umbilical vein endothelial cells (HUVECs) and its role in cell migration. Expression of RhoGDI2 was found to be considerably higher in CRIF1-deficient HUVECs along with suppression of cell migration. Moreover, the phosphorylation levels of Akt and CREB were decreased in CRIF1-silenced cells. The Akt-CREB signaling pathway was implicated in the changes in endothelial cell migration caused by CRIF1 downregulation. In addition to RhoGDI2, we identified another factor that promotes migration and invasion of ECs. Adrenomedullin2 (ADM2) is an autocrine/paracrine factor that regulates vascular tone and other vascular functions. Endogenous ADM2 levels were elevated in CRIF1-silenced HUVECs with no effect on cell migration. However, siRNA-mediated depletion of RhoGDI2 or exogenous ADM2 administration significantly restored cell migration via the Akt-CREB signaling pathway. In conclusion, RhoGDI2 and ADM2 play important roles in the migration of CRIF1-deficient endothelial cells.

scholarly journals Dihydroartemisinin inhibits endothelial cell migration via the TGF‑β1/ALK5/SMAD2 signaling pathway

2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Ling Guo ◽  
Xiaoqing Wen ◽  
Yinglong Hou ◽  
Rong Sun ◽  
Liang Zhang ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Signaling Pathway ◽  
Endothelial Cell Migration ◽  
Tgf Β1

scholarly journals Oroxylin a Attenuates Limb Ischemia by Promoting Angiogenesis via Modulation of Endothelial Cell Migration

2021 ◽  
Vol 12 ◽  
Author(s):  
Lusha Zhang ◽  
Lu Chen ◽  
Chunxiao Li ◽  
Hong Shi ◽  
Qianyi Wang ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Migration ◽  
Endothelial Cell ◽  
Growth Factor ◽  
Signaling Pathway ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Endothelial Cell Migration ◽  
Oroxylin A ◽  
Fibroblast Growth Factor Basic

Oroxylin A (OA) has been shown to simultaneously increase coronary flow and provide a strong anti-inflammatory effect. In this study, we described the angiogenic properties of OA. OA treatment accelerated perfusion recovery, reduced tissue injury, and promoted angiogenesis after hindlimb ischemia (HLI). In addition, OA regulated the secretion of multiple cytokines, including vascular endothelial growth factor A (VEGFA), angiopoietin-2 (ANG-2), fibroblast growth factor-basic (FGF-2), and platelet derived growth factor BB (PDGF-BB). Specifically, those multiple cytokines were involved in cell migration, cell population proliferation, and angiogenesis. These effects were observed at 3, 7, and 14 days after HLI. In skeletal muscle cells, OA promoted the release of VEGFA and ANG-2. After OA treatment, the conditioned medium derived from skeletal muscle cells was found to significantly induce endothelial cell (EC) proliferation. OA also induced EC migration by activating the Ras homolog gene family member A (RhoA)/Rho-associated coiled-coil kinase 2 (ROCK-II) signaling pathway and the T-box20 (TBX20)/prokineticin 2 (PROK2) signaling pathway. In addition, OA was able to downregulate the number of macrophages and neutrophils, along with the secretion of interleukin-1β, at 3 days after HLI. These results expanded current knowledge about the beneficial effects of OA in angiogenesis and blood flow recovery. This research could open new directions for the development of novel therapeutic intervention for patients with peripheral artery disease (PAD).

scholarly journals 16-kDa Prolactin Inhibits Endothelial Cell Migration by Down-Regulating the Ras-Tiam1-Rac1-Pak1 Signaling Pathway

2007 ◽  
Vol 67 (22) ◽  
pp. 11045-11053 ◽  
Author(s):  
Sok-Hyong Lee ◽  
Jeannette Kunz ◽  
Sue-Hwa Lin ◽  
Li-yuan Yu-Lee
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Signaling Pathway ◽  
Endothelial Cell Migration

scholarly journals SAT-735 Effects of Androgen Receptor Activation on Angiogenesis

2020 ◽  
Vol 4 (Supplement_1) ◽  
Author(s):  
Yen-Nien Huo
Keyword(s):  
Cell Migration ◽  
Androgen Receptor ◽  
Endothelial Cell ◽  
Signaling Pathway ◽  
Receptor Activation ◽  
Endothelial Cell Migration ◽  
Endothelial Cell Proliferation ◽  
Pre Treatment ◽  
And Migration ◽  
Proliferation And Migration

Abstract The effect of androgen on angiogenesis has been documented. However, its molecular mechanisms underlying has not been well illustrated. Here, we conducted both in vitro migration assay and proliferation assay to investigate whether androgen receptor activation have any impacts on the angiogenesis. Treatment with an androgen receptor (AR) agonist, metribolone (R1881) at a range of concentrations (0.05-5 nM) or dihydrotestosterone (DHT) at a range of concentrations (0.5-2 nM) caused concentration-dependent inhibition of proliferation and migration in human umbilical venous endothelial cells (HUVEC). Blockade of the AR activity by pre-treatment with HF (5 nM), an AR antagonist, or knockdown of AR expression using the lenti-virus shRNA technique abolished the R1881-induced proliferation and migration inhibition in HUVEC, suggesting that AR receptor activation can inhibit endothelial cell proliferation and migration. To further delineate the signaling pathway involved in the AR activation-induced proliferation inhibition, our data indicate that R1881 inhibited proliferation in vascular endothelial cells through activating the AR/cSrc/AKT/p38/ERK/NFκB signaling pathway, which in turn up-regulated the expression of p53, p21 and p27 protein, and finally reduced endothelial cell proliferation. To investigate signaling pathway involved in the AR activation-induced migration inhibition, our data showed that R1881 can reduce the membrane translocation of RhoA and Rac-1, suggesting that inhibition of the RhoA and Rac-1 activity might be involved in the R1881-inhibited endothelial cell migration. Over-expression of RhoA prevented the R1881-inhibited endothelial cell migration and this effect was abolished by pre-treatment with Y27623, a ROCK inhibitor, confirming that inhibiting RhoA activity participated in the R1881-inhibited endothelial cell migration. Using the zebrafish and Matrigel angiogenesis models, we also demonstrated that R1881 inhibited angiogenesis through the AR-mediated pathway in vivo.

Cellular repressor of E1A-stimulated genes regulates vascular endothelial cell migration by The ILK/AKT/mTOR/VEGF165 signaling pathway

2011 ◽  
Vol 317 (20) ◽  
pp. 2904-2913 ◽  
Author(s):  
Huimin Zhang ◽  
Yaling Han ◽  
Jie Tao ◽  
Shaowei Liu ◽  
Chenghui Yan ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Signaling Pathway ◽  
Vascular Endothelial Cell ◽  
Endothelial Cell Migration ◽  
Vascular Endothelial
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