Signal Transduction Pathways in Endothelial Cells

2015 ◽  
pp. 99-116
Author(s):  
Una S. Ryan ◽  
Marilyn K. Glassberg ◽  
Anthony Johns
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Signal Transduction Pathways

Heterogeneity of the signal transduction pathways for VEGF-induced MAPKs activation in human vascular endothelial cells

2001 ◽  
Vol 188 (2) ◽  
pp. 201-210 ◽  
Author(s):  
Rei Yashima ◽  
Mayumi Abe ◽  
Katsuhiro Tanaka ◽  
Hikaru Ueno ◽  
Kenya Shitara ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Vascular Endothelial Cells ◽  
Signal Transduction Pathways ◽  
Vascular Endothelial

Time dependent phosphorylation in eNOS linked signal transduction pathways in endothelial cells reveals feedback mechanisms

Nitric Oxide ◽  
2014 ◽  
Vol 42 ◽  
pp. 103
Author(s):  
Carol Chrestensen ◽  
Tasia Nabors ◽  
Katy Helms ◽  
Jonathan McMurry ◽  
Megan Mickanen ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Time Dependent ◽  
Signal Transduction Pathways ◽  
Feedback Mechanisms

scholarly journals Characterization of Signal Transduction Pathways in Human Bone Marrow Endothelial Cells

Blood ◽  
1997 ◽  
Vol 90 (6) ◽  
pp. 2253-2259 ◽  
Author(s):  
Zhong-Ying Liu ◽  
Ramesh K. Ganju ◽  
Jian-Feng Wang ◽  
Karin Schweitzer ◽  
Babette Weksler ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Bone Marrow ◽  
Endothelial Cells ◽  
Growth Factors ◽  
Growth Factor ◽  
T Antigen ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Signal Transduction Pathways ◽  
Stimulation Of

Human bone marrow endothelial cells immortalized with the T antigen of SV40 (TrHBMEC) have previously been characterized by us with regard to their properties that are similar to primary marrow endothelial cells and their utility as a model system. We now report that TrHBMEC express a recently discovered signal transduction molecule termed RAFTK (related adhesion focal tyrosine kinase), also called Pyk2 or CAK-β. RAFTK, the second member of the focal adhesion kinase (FAK) family, is known to be activated in response to calcium flux in neuronal cells and integrin stimulation in megakaryocytes and B cells. We have studied the effects of cytokines on RAFTK activation in TrHBMEC. Treatment of TrHBMEC with the vascular endothelial growth factor (VEGF ), as well as the VEGF-related protein (VRP), the recently identified ligand for the FLT-4 receptor, resulted in enhanced tyrosine phosphorylation of RAFTK. Similar changes in RAFTK phosphorylation were observed upon stimulation of TrHBMEC with basic fibroblast growth factor (bFGF ) or oncostatin M (OSM). Stimulation of these cells with growth factors also resulted in an increase in RAFTK activity and the c-Jun NH2 -terminal kinase (JNK). RAFTK coimmunoprecipitated with the cytoskeletal protein paxillin through its C-terminal proline-rich domain in TrHBMEC. These results suggest that, in marrow endothelium, activation of RAFTK by VEGF, VRP, OSM, and bFGF represents a new element in the signal transduction pathways used by these growth factors and likely acts to coordinate signaling from their surface receptors to the cytoskeleton, thereby modulating cell growth and function.

scholarly journals A Unique Autophosphorylation Site on Tie2/Tek Mediates Dok-R Phosphotyrosine Binding Domain Binding and Function

2003 ◽  
Vol 23 (8) ◽  
pp. 2658-2668 ◽  
Author(s):  
Nina Jones ◽  
Stephen H. Chen ◽  
Celina Sturk ◽  
Zubin Master ◽  
Jennifer Tran ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Endothelial Cells ◽  
Cell Migration ◽  
Binding Domain ◽  
Signal Transduction Pathways ◽  
Pleckstrin Homology Domain ◽  
Dependent Manner ◽  
Tyrosine Residue ◽  
Phosphotyrosine Binding Domain ◽  
Autophosphorylation Site

ABSTRACT Tie2/Tek is an endothelial cell receptor tyrosine kinase that induces signal transduction pathways involved in cell migration upon angiopoietin-1 (Ang1) stimulation. To address the importance of the various tyrosine residues of Tie2 in signal transduction, we generated a series of Tie2 mutants and examined their signaling properties. Using this approach in conjunction with a phosphorylation state-specific antibody, we identified tyrosine residue 1106 on Tie2 as an Ang1-dependent autophosphorylation site that mediates binding and phosphorylation of the downstream-of-kinase-related (Dok-R) docking protein. This tyrosine residue is contained within a unique interaction motif for the phosphotyrosine binding domain of Dok-R, and the pleckstrin homology domain of Dok-R further contributes to Tie2 binding in a phosphatidylinositol 3′-kinase-dependent manner. Introduction of a Tie2 mutant lacking tyrosine residue 1106 into endothelial cells interferes with Dok-R phosphorylation in response to Ang1. Furthermore, this mutant is unable to restore the migration potential of endothelial cells derived from mice lacking Tie2. Together, these findings demonstrate that tyrosine residue 1106 on Tie2 is critical for coupling downstream cell migration signal transduction pathways with Ang1 stimulation in endothelial cells.

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