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Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells.


ABSTRACT: Nogo isoforms (Nogo-A and -B) have been implicated in regulating neural and cardiovascular functions, such as cell spreading and chemotaxis. Unlike the loop domain (Nogo-66) found in all Nogo isoforms that can interact with a neural-specific Nogo-66 receptor, the receptor for the amino terminus of Nogo-B that mediates vascular function is unknown. Here, we identify a previously uncharacterized Nogo-B receptor specific for the amino terminus of Nogo-B and show that Nogo-B receptor localizes with the ligand Nogo-B during VEGF and wound healing angiogenesis in vivo, mediates chemotaxis in a heterologous expression system and chemotaxis, and 3D tube formation in native endothelial cells. Thus, identification of this receptor may lead to the discovery of agonists or antagonists of this pathway to regulate vascular remodeling and angiogenesis.

SUBMITTER: Miao RQ 

PROVIDER: S-EPMC1544163 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature

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Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells.

Miao Robert Qing RQ   Gao Yuan Y   Harrison Kenneth D KD   Prendergast Jay J   Acevedo Lisette M LM   Yu Jun J   Hu Fenghua F   Strittmatter Stephen M SM   Sessa William C WC  

Proceedings of the National Academy of Sciences of the United States of America 20060711 29


Nogo isoforms (Nogo-A and -B) have been implicated in regulating neural and cardiovascular functions, such as cell spreading and chemotaxis. Unlike the loop domain (Nogo-66) found in all Nogo isoforms that can interact with a neural-specific Nogo-66 receptor, the receptor for the amino terminus of Nogo-B that mediates vascular function is unknown. Here, we identify a previously uncharacterized Nogo-B receptor specific for the amino terminus of Nogo-B and show that Nogo-B receptor localizes with  ...[more]

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