Glybatomaq312317b: A hyper-ligand playing a role in angiogenesis, controlling endothelial cell motility and invasion

2018 ◽  
Vol 06 ◽  
Author(s):  
Grigoriadis Ioannis
Keyword(s):  
Endothelial Cell ◽  
Cell Motility

scholarly journals Angiomotin Regulates Endothelial Cell-Cell Junctions and Cell Motility

2005 ◽  
Vol 280 (41) ◽  
pp. 34859-34869 ◽  
Author(s):  
Anders Bratt ◽  
Olivier Birot ◽  
Indranil Sinha ◽  
Niina Veitonmäki ◽  
Karin Aase ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Motility ◽  
Cell Junctions ◽  
Cell Cell

scholarly journals SHP-2 phosphatase activity is required for PECAM-1-dependent cell motility

2010 ◽  
Vol 299 (4) ◽  
pp. C854-C865 ◽  
Author(s):  
Jing-Xu Zhu ◽  
Gaoyuan Cao ◽  
James T. Williams ◽  
Horace M. DeLisser
Keyword(s):  
Endothelial Cell ◽  
Cell Motility ◽  
Phosphatase Activity ◽  
Tyrosine Phosphorylation ◽  
Mapk Pathway ◽  
Tube Formation ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Catalytically Active ◽  
Dependent Cell

Platelet endothelial cell adhesion molecule-1 (PECAM-1) has been implicated in endothelial cell motility during angiogenesis. Although there is evidence that SHP-2 plays a role in PECAM-1-dependent cell motility, the molecular basis of the activity of SHP-2 in this process has not been defined. To investigate the requirement of SHP-2 in PECAM-1-dependent cell motility, studies were done in which various constructs of SHP-2 were expressed in cell transfectants expressing PECAM-1. We observed that the levels of PECAM-1 tyrosine phosphorylation and SHP-2 association with PECAM-1 were significantly increased in cells expressing a phosphatase-inactive SHP-2 mutant, suggesting that the level of PECAM-1 tyrosine phosphorylation, and thus SHP-2 binding are regulated in part by bound, catalytically active SHP-2. We subsequently found that expression of PECAM-1 stimulated wound-induced migration and the formation of filopodia (a morphological feature of motile cells). These activities were associated with increased mitogen-activated protein kinase (MAPK) activation and the dephosphorylation of paxillin (an event implicated in the activation of MAPK). The phosphatase-inactive SHP-2 mutant, however, suppressed these PECAM-1-dependent phenomena, whereas the activity of PECAM-1 expressing cells was not altered by expression of wild-type SHP-2 or SHP-2 in which the scaffold/adaptor function had been disabled. Pharmacological inhibition of SHP-2 phosphatase activity also suppressed PECAM-1-dependent motility. Furthermore, PECAM-1 expression also stimulates tube formation, but none of the SHP-2 constructs affected this process. These findings therefore suggest a model for the involvement of SHP-2 in PECAM-1-dependent motility in which SHP-2, recruited by its interaction with PECAM-1, targets paxillin to ultimately activate the MAPK pathway and downstream events required for cell motility.

Sphingosine‐1‐Phosphate‐Mediated Endothelial Cell Motility Is Regulated by S1P1 Receptor, Lipid Phosphate Phosphatase‐1 and Sphingosine Kinase 1

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Irina Gorshkova ◽  
Evgeny Berdyshev ◽  
Bahman Saatian ◽  
Yutong Zhao ◽  
Srikanth Pendyala ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Motility ◽  
Sphingosine Kinase ◽  
Sphingosine Kinase 1 ◽  
S1p1 Receptor ◽  
Sphingosine 1 Phosphate ◽  
Lipid Phosphate

Membrane microviscosity regulates endothelial cell motility

2002 ◽  
Vol 4 (11) ◽  
pp. 894-900 ◽  
Author(s):  
Prabar K. Ghosh ◽  
Amit Vasanji ◽  
Gurunathan Murugesan ◽  
Steven J. Eppell ◽  
Linda M. Graham ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Motility ◽  
Membrane Microviscosity

scholarly journals HIV-1 Tat Interacts with a Kaposi’s Sarcoma-Associated Herpesvirus Reactivation-Upregulated Antiangiogenic Long Noncoding RNA, LINC00313, and Antagonizes Its Function

2019 ◽  
Vol 94 (3) ◽  
Author(s):  
Wan-Shan Yang ◽  
Ting-Yu Lin ◽  
Lung Chang ◽  
Wayne W. Yeh ◽  
Shih-Ching Huang ◽  
...  
Keyword(s):  
Cell Migration ◽  
Endothelial Cell ◽  
Cell Motility ◽  
Long Noncoding Rna ◽  
Noncoding Rna ◽  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Hiv Tat ◽  
Lytic Reactivation ◽  
Hiv 1

ABSTRACT Kaposi’s sarcoma-associated herpesvirus (KSHV) is the causative agent of Kaposi’s sarcoma (KS), an AIDS-defining cancer with abnormal angiogenesis. The high incidence of KS in human immunodeficiency virus (HIV)-infected AIDS patients has been ascribed to an interaction between HIV type 1 (HIV-1) and KSHV, focusing on secretory proteins. The HIV-1 secreted protein HIV Tat has been found to synergize with KSHV lytic proteins to induce angiogenesis. However, the impact and underlying mechanisms of HIV Tat in KSHV-infected endothelial cells undergoing viral lytic reactivation remain unclear. Here, we identified LINC00313 as a novel KSHV reactivation-activated long noncoding RNA (lncRNA) that interacts with HIV Tat. We found that LINC00313 overexpression inhibits cell migration, invasion, and tube formation, and this suppressive effect was relieved by HIV Tat. In addition, LINC00313 bound to polycomb repressive complex 2 (PRC2) complex components, and this interaction was disrupted by HIV Tat, suggesting that LINC00313 may mediate transcription repression through recruitment of PRC2 and that HIV Tat alleviates repression through disruption of this association. This notion was further supported by bioinformatics analysis of transcriptome profiles in LINC00313 overexpression combined with HIV Tat treatment. Ingenuity Pathway Analysis (IPA) showed that LINC00313 overexpression negatively regulates cell movement and migration pathways, and enrichment of these pathways was absent in the presence of HIV Tat. Collectively, our results illustrate that an angiogenic repressive lncRNA, LINC00313, which is upregulated during KSHV reactivation, interacts with HIV Tat to promote endothelial cell motility. These results demonstrate that an lncRNA serves as a novel connector in HIV-KSHV interactions. IMPORTANCE KS is a prevalent tumor associated with infections with two distinct viruses, KSHV and HIV. Since KSHV and HIV infect distinct cell types, the virus-virus interaction associated with KS formation has focused on secretory factors. HIV Tat is a well-known RNA binding protein secreted by HIV. Here, we revealed LINC00313, an lncRNA upregulated during KSHV lytic reactivation, as a novel HIV Tat-interacting lncRNA that potentially mediates HIV-KSHV interactions. We found that LINC00313 can repress endothelial cell angiogenesis-related properties potentially by interacting with chromatin remodeling complex PRC2 and downregulation of cell migration-regulating genes. An interaction between HIV Tat and LINC00313 contributed to the dissociation of PRC2 from LINC00313 and the disinhibition of LINC00313-induced repression of cell motility. Given that lncRNAs are emerging as key players in tissue physiology and disease progression, including cancer, the mechanism identified in this study may help decipher the mechanisms underlying KS pathogenesis induced by HIV and KSHV coinfection.

scholarly journals The tight junctions protein Claudin-5 limits endothelial cell motility

2020 ◽  
pp. jcs.248237
Author(s):  
Zhenguo Yang ◽  
Shuilong Wu ◽  
Federica Fontana ◽  
Yanyu Li ◽  
Wei Xiao ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Cell Motility ◽  
Dorsal Aorta ◽  
Aortic Endothelial Cells ◽  
Differential Adhesion ◽  
Adhesive Forces

Steinberg's differential adhesion hypothesis suggests that adhesive mechanisms are important for sorting of cells and tissues during morphogenesis (Steinberg, 2007). During zebrafish vasculogenesis, endothelial cells sort into arterial and venous vessel beds but it is unknown whether this involves adhesive mechanisms. Claudins are tight junction proteins regulating the permeability of epithelial and endothelial tissue barriers. Previously, the roles of Claudins during organ development have exclusively been related to their canonical functions in determining paracellular permeability. Here, we use atomic force microscopy to quantify Claudin-5-dependent adhesion and find that this strongly contributes to the adhesive forces between arterial endothelial cells. Based on genetic manipulations, we reveal a non-canonical role of Claudin-5a during zebrafish vasculogenesis, which involves the regulation of adhesive forces between adjacent dorsal aortic endothelial cells. In vitro and in vivo studies demonstrate that loss of Claudin-5 results in increased motility of dorsal aorta endothelial cells and in a failure of the dorsal aorta to lumenize. Our findings uncover a novel role of Claudin-5 in limiting arterial endothelial cell motility, which goes beyond its traditional sealing function during embryonic development.

scholarly journals EP2, a receptor for PGE2, regulates tumor angiogenesis through direct effects on endothelial cell motility and survival

Oncogene ◽  
2006 ◽  
Vol 25 (53) ◽  
pp. 7019-7028 ◽  
Author(s):  
M Kamiyama ◽  
A Pozzi ◽  
L Yang ◽  
L M DeBusk ◽  
R M Breyer ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Motility ◽  
Tumor Angiogenesis ◽  
Direct Effects

scholarly journals Rat Aortic Endothelial Cell Motility Dependence on Flow Rate

2005 ◽  
Vol 11 (S02) ◽  
Author(s):  
P J Bernal ◽  
J M Karlsson ◽  
S C Watkins ◽  
C J Baty
Keyword(s):  
Endothelial Cell ◽  
Cell Motility ◽  
Flow Rate ◽  
Aortic Endothelial Cell ◽  
Aortic Endothelial
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