<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>185(4)</volume><submitter>Winderlich M</submitter><pubmed_abstract>Vascular endothelial protein tyrosine phosphatase (VE-PTP) is an endothelial-specific receptor-type tyrosine phosphatase that associates with Tie-2 and VE-cadherin. VE-PTP gene disruption leads to embryonic lethality, vascular remodeling defects, and enlargement of vascular structures in extraembryonic tissues. We show here that antibodies against the extracellular part of VE-PTP mimic the effects of VE-PTP gene disruption exemplified by vessel enlargement in allantois explants. These effects require the presence of the angiopoietin receptor Tie-2. Analyzing the mechanism we found that anti-VE-PTP antibodies trigger endocytosis and selectively affect Tie-2-associated, but not VE-cadherin-associated VE-PTP. Dissociation of VE-PTP triggers the activation of Tie-2, leading to enhanced endothe</pubmed_abstract><journal>The Journal of cell biology</journal><pagination>657-71</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2711575</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>VE-PTP controls blood vessel development by balancing Tie-2 activity.</pubmed_title><pmcid>PMC2711575</pmcid><pubmed_authors>Winderlich M</pubmed_authors><pubmed_authors>Vestweber D</pubmed_authors><pubmed_authors>Cagna G</pubmed_authors><pubmed_authors>Keller L</pubmed_authors><pubmed_authors>Kamenyeva O</pubmed_authors><pubmed_authors>Kiefer F</pubmed_authors><pubmed_authors>Broermann A</pubmed_authors><pubmed_authors>Deutsch U</pubmed_authors><pubmed_authors>Nottebaum AF</pubmed_authors></additional><is_claimable>false</is_claimable><name>VE-PTP controls blood vessel development by balancing Tie-2 activity.</name><description>Vascular endothelial protein tyrosine phosphatase (VE-PTP) is an endothelial-specific receptor-type tyrosine phosphatase that associates with Tie-2 and VE-cadherin. VE-PTP gene disruption leads to embryonic lethality, vascular remodeling defects, and enlargement of vascular structures in extraembryonic tissues. We show here that antibodies against the extracellular part of VE-PTP mimic the effects of VE-PTP gene disruption exemplified by vessel enlargement in allantois explants. These effects require the presence of the angiopoietin receptor Tie-2. Analyzing the mechanism we found that anti-VE-PTP antibodies trigger endocytosis and selectively affect Tie-2-associated, but not VE-cadherin-associated VE-PTP. Dissociation of VE-PTP triggers the activation of Tie-2, leading to enhanced endothe</description><dates><release>2009-01-01T00:00:00Z</release><publication>2009 May</publication><modification>2025-04-22T15:15:27.418Z</modification><creation>2019-06-06T21:31:29Z</creation></dates><accession>S-EPMC2711575</accession><cross_references><pubmed>19451274</pubmed><doi>10.1083/jcb.200811159</doi></cross_references></HashMap>