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ProteomicsVE-PTP inhibition stabilizes endothelial junctions by activating FGD5
Inhibition of VE-PTP, an endothelial receptor type tyrosine phosphatase, triggers phosphorylation of the tyrosine kinase receptor Tie-2, which leads to the suppression of inflammation-induced vascular permeability. Analyzing the underlying mechanism, we show here that inhibition of VE-PTP and activa...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2019-05-04 | PXD010959 | Pride
Junctions Phosphatase Transmigration Signalling Ve-ptp Lc-msms Fgd5 Shotgun proteomics Inflammation Ptprb Tyrosine kinase receptor Adhesion Phosphorylation Endothelium 
GenomicsSoluble VE-cadherin disrupts endothelial barrier function via VE-PTP/RhoA signalling
Soluble VE-cadherin disrupts endothelial barrier function via VE-PTP/RhoA signalling
PRJNA865806 | ENA
TranscriptomicsSoluble VE-cadherin disrupts endothelial barrier function via VE-PTP/RhoA signalling
We generated recombinant human sVE-cadherin (extracellular domains EC1-5) which was applied to human dermal microvascular endothelial cells (HDMEC) to investigate it`s role in endothelial barrier function. In other experiments we observed that sVE-cadherin disrupted endothelial barrier function by d...
ORGANISM(S): Homo sapiens 
2025-10-01 | GSE210502 | GEO
UnknownVE-PTP stabilizes VE-cadherin junctions and the endothelial barrier via a phosphatase-independent mechanism.
Not available
S-EPMC6504901 | biostudies-literature
UnknownVE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts.
Not available
S-EPMC126293 | biostudies-literature
UnknownVE-PTP inhibition stabilizes endothelial junctions by activating FGD5.
Not available
S-EPMC6607018 | biostudies-literature
UnknownVE-PTP controls blood vessel development by balancing Tie-2 activity.
Not available
S-EPMC2711575 | biostudies-literature
UnknownInterfering with VE-PTP stabilizes endothelial junctions in vivo via Tie-2 in the absence of VE-cadherin.
Not available
S-EPMC4689167 | biostudies-literature
UnknownVE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF.
Not available
S-EPMC2585844 | biostudies-literature
ProteomicsVascular endothelial protein tyrosine phosphatase: Identification of novel cell junction-related substrates and a ternary receptor complex with EPHB4 and TIE2
Vascular endothelial protein tyrosine phosphatase (VE-PTP, PTPRB) is a receptor type phosphatase that is crucial for the regulation of endothelial junctions and blood vessel development. VE-PTP regulates vascular integrity by dephosphorylating substrates which are key players in endothelial junction...
ORGANISM(S): Mus musculus (Mouse) 
2019-08-20 | PXD011940 | Pride
Lc-msms Mouse Tyrosine phosphatase Endothelial cells Substrate trapping 
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