scholarly journals Gi-mediated Cas Tyrosine Phosphorylation in Vascular Endothelial Cells Stimulated with Sphingosine 1-Phosphate

2000 ◽  
Vol 276 (7) ◽  
pp. 5274-5280 ◽  
Author(s):  
Tsukasa Ohmori ◽  
Yutaka Yatomi ◽  
Hirotaka Okamoto ◽  
Yoshie Miura ◽  
Ge Rile ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Tyrosine Phosphorylation ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Sphingosine 1 Phosphate

scholarly journals Identification of Fer Tyrosine Kinase Localized on Microtubules as a Platelet Endothelial Cell Adhesion Molecule-1 Phosphorylating Kinase in Vascular Endothelial Cells

2003 ◽  
Vol 14 (9) ◽  
pp. 3553-3564 ◽  
Author(s):  
Naoko Kogata ◽  
Michitaka Masuda ◽  
Yuji Kamioka ◽  
Akiko Yamagishi ◽  
Akira Endo ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Adhesion Molecule ◽  
Intracellular Signaling ◽  
Vascular Endothelial Cells ◽  
Expression Cloning ◽  
Vascular Endothelial ◽  
Cell Contacts ◽  
Cell Cell

Platelet endothelial adhesion molecule-1 (PECAM-1) is a part of intercellular junctions and triggers intracellular signaling cascades upon homophilic binding. The intracellular domain of PECAM-1 is tyrosine phosphorylated upon homophilic engagement. However, it remains unclear which tyrosine kinase phosphorylates PECAM-1. We sought to isolate tyrosine kinases responsible for PECAM-1 phosphorylation and identified Fer as a candidate, based on expression cloning. Fer kinase specifically phosphorylated PECAM-1 at the immunoreceptor tyrosine-based inhibitory motif. Notably, Fer induced tyrosine phosphorylation of SHP-2, which is known to bind to the immunoreceptor tyrosine-based inhibitory motif of PECAM-1, and Fer also induced tyrosine phosphorylation of Gab1 (Grb2-associated binder-1). Engagement-dependent PECAM-1 phosphorylation was inhibited by the overexpression of a kinase-inactive mutant of Fer, suggesting that Fer is responsible for the tyrosine phosphorylation upon PECAM-1 engagement. Furthermore, by using green fluorescent protein-tagged Fer and a time-lapse fluorescent microscope, we found that Fer localized at microtubules in polarized and motile vascular endothelial cells. Fer was dynamically associated with growing microtubules in the direction of cell-cell contacts, where p120catenin, which is known to associate with Fer, colocalized with PECAM-1. These results suggest that Fer localized on microtubules may play an important role in phosphorylation of PECAM-1, possibly through its association with p120catenin at nascent cell-cell contacts.

scholarly journals Mouse SPNS2 Functions as a Sphingosine-1-Phosphate Transporter in Vascular Endothelial Cells

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e38941 ◽  
Author(s):  
Yu Hisano ◽  
Naoki Kobayashi ◽  
Akihito Yamaguchi ◽  
Tsuyoshi Nishi
Keyword(s):  
Endothelial Cells ◽  
Vascular Endothelial Cells ◽  
Phosphate Transporter ◽  
Vascular Endothelial ◽  
Sphingosine 1 Phosphate

scholarly journals A Novel Sphingosine-1-Phosphate Receptor 1 Antagonist Prevents the Proliferation and Relaxation of Vascular Endothelial Cells by Sphingosine-1-Phosphate

2010 ◽  
Vol 33 (9) ◽  
pp. 1500-1505 ◽  
Author(s):  
Kiyoaki Yonesu ◽  
Tsuyoshi Nakamura ◽  
Yumiko Mizuno ◽  
Chie Suzuki ◽  
Takahiro Nagayama ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Vascular Endothelial Cells ◽  
Vascular Endothelial ◽  
Sphingosine 1 Phosphate

scholarly journals Lipopolysaccharide induces the rapid tyrosine phosphorylation of the mitogen-activated protein kinases erk-1 and p38 in cultured human vascular endothelial cells requiring the presence of soluble CD14

Blood ◽  
1996 ◽  
Vol 87 (7) ◽  
pp. 2805-2814 ◽  
Author(s):  
RR Schumann ◽  
D Pfeil ◽  
N Lamping ◽  
C Kirschning ◽  
G Scherzinger ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Tyrosine Phosphorylation ◽  
Kinase Inhibitors ◽  
Vascular Endothelial Cells ◽  
Mitogen Activated Protein Kinase ◽  
Vascular Endothelial ◽  
Protein Tyrosine Phosphorylation ◽  
Soluble Cd14 ◽  
Protein Tyrosine ◽  
Mitogen Activated Protein

Human vascular endothelial cells (HUVECs), which do not display the lipopolysaccharide (LPS) receptor CD14, were examined for protein tyrosine phosphorylation after LPS stimulation in the presence and absence of soluble CD14 (sCD14). By phosphotyrosine Western blotting and immunocomplex kinase assays we show that LPS was capable of inducing in these cells rapid protein tyrosine phosphorylation and kinase activation of two members of the mitogen-activated protein kinase (MAPK) family erk-1 and the newly discovered p38, requiring the presence of sCD14. LPS-induced tyrosine phosphorylation of MAPK was associated with increased transcript- and surface protein expression of intracellular adhesion molecule-1 by HUVECs. MAPK phosphorylation and activation was induced by LPS in concentrations as little as 30 ng/mL and as early as 15 minutes after stimulation. Furthermore, tyrosine kinase inhibitors such as Genistein partially inhibited this effect. These results show that LPS triggers similar signaling events in both CD14+ myelo-monocytic cells and cells lacking the putative LPS-receptor CD14, suggesting the presence of a common, yet unidentified element in LPS-signaling in both cell types.

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