Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development

Bäumer, Sebastian; Keller, Linda; Holtmann, Astrid; Funke, Ruth; August, Benjamin; Gamp, Alexander; Wolburg, Hartwig; Wolburg-Buchholz, Karen; Deutsch, Urban; Vestweber, Dietmar (2006). Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development. Blood, 107(12), pp. 4754-62. Washington, D.C.: American Society of Hematology 10.1182/blood-2006-01-0141

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VE-PTP, a receptor-type phosphotyrosine phosphatase, associates with the tyrosine kinase receptor Tie-2 and VE-cadherin and enhances the adhesive function of the latter. Here, VE-PTP was found to be restricted to endothelial cells, with a preference for arterial endothelium. Mutant mice expressing a truncated, secreted form of VE-PTP lacking the cytoplasmic and transmembrane domains and the most membrane-proximal extracellular fibronectin type III repeat, showed severe vascular malformations causing lethality at 10 days of gestation. Although blood vessels were initially formed, the intraembryonic vascular system soon deteriorated. Blood vessels in the yolk sac developed into dramatically enlarged cavities. In explant cultures of mutant allantoides, endothelial cells were found next to vessel structures growing as cell layers. No signs for enhanced endothelial apoptosis or proliferation were observed. Thus, the activity of VE-PTP is not required for the initial formation of blood vessels, yet it is essential for their maintenance and remodeling.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Theodor Kocher Institute

UniBE Contributor:

Deutsch, Urban

ISSN:

0006-4971

ISBN:

16514057

Publisher:

American Society of Hematology

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:45

Last Modified:

05 Dec 2022 14:14

Publisher DOI:

10.1182/blood-2006-01-0141

PubMed ID:

16514057

Web of Science ID:

000238305400035

URI:

https://boris.unibe.ch/id/eprint/18590 (FactScience: 790)

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