H2O2and Genistein Differentially Modulate Protein Tyrosine Phosphorylation, Endothelial Morphology, and Monolayer Barrier Function

1998 ◽  
Vol 249 (2) ◽  
pp. 461-466 ◽  
Author(s):  
José M. Carbajal ◽  
Richard C. Schaeffer
Keyword(s):  
Tyrosine Phosphorylation ◽  
Barrier Function ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine ◽  
Monolayer Barrier Function

Tyrosine phosphorylation of paxillin/pp125FAK and microvascular endothelial barrier function

1998 ◽  
Vol 275 (1) ◽  
pp. H84-H93 ◽  
Author(s):  
Yuan Yuan ◽  
F. Y. Meng ◽  
Q. Huang ◽  
James Hawker ◽  
H. Mac Wu
Keyword(s):  
Endothelial Cells ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Barrier Function ◽  
Tyrosine Phosphatase ◽  
Endothelial Barrier ◽  
Protein Tyrosine Phosphorylation ◽  
Endothelial Barrier Function ◽  
Adhesion Proteins ◽  
Protein Tyrosine

The transendothelial movement of solutes is a dynamic process controlled by a complex interaction between the cytoskeleton and adhesion proteins. The aim of this study was to examine whether protein tyrosine phosphorylation is involved in the regulation of endothelial barrier function. The apparent permeability coefficient of albumin ( P a) was measured in isolated and perfused coronary venules. Tyrosine phosphatase inhibitors, including phenylarsine oxide and sodium orthovanadate, dose and time dependently increased basal P a. Western blot analysis of cultured coronary venular endothelial cells revealed that inhibition of tyrosine phosphatase induced an increase in phosphotyrosine content in a number of proteins, including bands at 65–70 and 120–130 kDa, which were identified as paxillin and focal adhesion kinase (pp125FAK), respectively. The time course and dose responsiveness of protein tyrosine phosphorylation were tightly correlated with those of increases in P a. Furthermore, stimulation of endothelial cells with histamine or phorbol myristate acetate (PMA) enhanced tyrosine phosphorylation of paxillin and pp125FAK, which was blocked by the tyrosine kinase inhibitor damnacanthal. Correspondingly, the increases in venular permeability elicited by histamine and PMA were abolished in damnacanthal-treated venules. Taken together, the data suggest a possible involvement of protein tyrosine phosphorylation in the control of endothelial barrier function. Paxillin and its associated focal adhesion proteins may play a specific role in agonist-induced hyperpermeability responses in the endothelium of exchange vessels.

Tyrosine phosphorylation and the small GTPase rac cross-talk in regulation of endothelial barrier function

2005 ◽  
Vol 94 (09) ◽  
pp. 620-629 ◽  
Author(s):  
Jochen Seebach ◽  
Hans-Jürgen Mädler ◽  
Beata Wojciak-Stothard ◽  
Hans-Joachim Schnittler
Keyword(s):  
Tyrosine Phosphorylation ◽  
Barrier Function ◽  
Rho Gtpase ◽  
Small Gtpase ◽  
Cell Junctions ◽  
Endothelial Barrier ◽  
Protein Tyrosine Phosphorylation ◽  
Endothelial Barrier Function ◽  
Protein Tyrosine ◽  
Junctional Proteins

SummaryEndothelial barrier function depends on the integrity of intercellular adherens junctions controlled by the association of VEcadherin/ catenin complex with cortical actin filaments. Both tyrosine phosphorylation/dephosphorylation of junctional proteins and actin reorganization mediated by rho-GTPases regulate barrier function but the relationship between these regulatory mechanisms is unclear. Here we studied the effects of factors increasing protein tyrosine phosphorylation, pervanadate (PV) and VEGF, on distribution of VE-cadherin, F-actin polymerization and transendothelial electrical resistance (TER) in human umbilical vein endothelial cells (HUVECs). Changes in protein tyrosine phosphorylation of cytoplasmic and junctional proteins, as well as the activity of rho-GTPase rac1, were also measured. We report for the first time that PV and VEGF induced a rapid transient increase in endothelial barrier function accompanied by rac1 activation, a differentiated tyrosine phosphorylation of theVE-cadherin/catenin complex, recruitment of actin filament to cell junctions and ruffle formation. A sustained decrease in endothelial barrier function was observed at later times of PV and VEGF treatment. Expression of dominant negative rac1, N17rac1 abolished the barrier-enhancing effects of PV andVEGF, while the sustained decrease in barrier function was unaffected. These observations bring into focus early shortterm effects of protein tyrosine phosphorylation in cells, often overshadowed by more pronounced and long-lasting later effects and may play an important role in the regulation of endothelial barrier function.

Role of Ca2+ in diperoxovanadate-induced cytoskeletal remodeling and endothelial cell barrier function

2003 ◽  
Vol 285 (5) ◽  
pp. L1006-L1017 ◽  
Author(s):  
Peter V. Usatyuk ◽  
Victor P. Fomin ◽  
Shu Shi ◽  
Joe G. N. Garcia ◽  
Kane Schaphorst ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endothelial Cell ◽  
Tyrosine Phosphorylation ◽  
Barrier Function ◽  
Endothelial Barrier ◽  
Protein Tyrosine Phosphorylation ◽  
Endothelial Barrier Function ◽  
Protein Tyrosine ◽  
Cytoskeletal Remodeling

Diperoxovanadate (DPV), a potent inhibitor of protein tyrosine phosphatases and activator of tyrosine kinases, alters endothelial barrier function via signaling pathways that are incompletely understood. One potential pathway is Src kinase-mediated tyrosine phosphorylation of proteins such as cortactin that regulate endothelial cell (EC) cytoskeleton assembly. As DPV modulates endothelial cell signaling via protein tyrosine phosphorylation, we determined the role of DPV-induced intracellular free calcium concentration ([Ca2+]i) in activation of Src kinase, cytoskeletal remodeling, and barrier function in bovine pulmonary artery endothelial cells (BPAECs). DPV in a dose- and time-dependent fashion increased [Ca2+]i, which was partially blocked by the calcium channel blockers nifedipine and Gd3+. Treatment of cells with thapsigargin released Ca2+ from the endoplasmic reticulum, and subsequent addition of DPV caused no further change in [Ca2+]i. These data suggest that DPV-induced [Ca2+]i includes Ca release from the endoplasmic reticulum and Ca influx through store-operated calcium entry. Furthermore, DPV induced an increase in protein tyrosine phosphorylation, phosphorylation of Src and cortactin, actin remodeling, and altered transendothelial electrical resistance in BPAECs. These DPV-mediated effects were significantly attenuated by BAPTA (25 μM), a chelator of [Ca2+]i. Immunofluorescence studies reveal that the DPV-mediated colocalization of cortactin with peripheral actin was also prevented by BAPTA. Chelation of extracellular Ca2+ by EGTA had marginal effects on DPV-induced phosphorylation of Src and cortactin; actin stress fibers formation, however, affected EC barrier function. These data suggest that DPV-induced changes in [Ca2+]i regulate endothelial barrier function using signaling pathways that involve Src and cytoskeleton remodeling.

scholarly journals Angiotensin II-induced protein tyrosine phosphorylation in neonatal rat cardiac fibroblasts.

1994 ◽  
Vol 269 (30) ◽  
pp. 19626-19632
Author(s):  
W. Schorb ◽  
T.C. Peeler ◽  
N.N. Madigan ◽  
K.M. Conrad ◽  
K.M. Baker
Keyword(s):  
Angiotensin Ii ◽  
Tyrosine Phosphorylation ◽  
Cardiac Fibroblasts ◽  
Neonatal Rat ◽  
Protein Tyrosine Phosphorylation ◽  
Protein Tyrosine
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