Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells. Proc Natl Acad Sci U S A 2006 Jul 18;103(29):10997-1002
Date
07/13/2006Pubmed ID
16835300Pubmed Central ID
PMC1544163DOI
10.1073/pnas.0602427103Scopus ID
2-s2.0-33746622474 (requires institutional sign-in at Scopus site) 135 CitationsAbstract
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.
Author List
Miao RQ, Gao Y, Harrison KD, Prendergast J, Acevedo LM, Yu J, Hu F, Strittmatter SM, Sessa WCMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Cell Shape
Cells, Cultured
Chemotaxis
Cricetinae
Endothelial Cells
Humans
Mice
Molecular Sequence Data
Myelin Proteins
Nogo Proteins
Protein Binding
Protein Isoforms
Receptors, Cell Surface
