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

被引:130
作者
Miao, Robert Qing
Gao, Yuan
Harrison, Kenneth D.
Prendergast, Jay
Acevedo, Lisette M.
Yu, Jun
Hu, Fenghua
Strittmatter, Stephen M.
Sessa, William C. [1 ]
机构
[1] Yale Univ, Sch Med, Dept Pharmacol & Vasc Cell Signaling, New Haven, CT 06536 USA
[2] Yale Univ, Sch Med, Therapeut Program, New Haven, CT 06536 USA
[3] Yale Univ, Sch Med, Boyer Ctr Mol Med, Dept Neurol, New Haven, CT 06536 USA
关键词
migration; angiogenesis; reticulon; vascular remodeling; expression cloning;
D O I
10.1073/pnas.0602427103
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 specificforthe 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.
引用
收藏
页码:10997 / 11002
页数:6
相关论文
共 15 条
[11]   Genomic structure and functional characterisation of the promoters of human and mouse nogo/rtn4 [J].
Oertle, T ;
Huber, C ;
van der Putten, H ;
Schwab, ME .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 325 (02) :299-323
[12]   Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP [J].
Rotblat, B ;
Niv, H ;
André, S ;
Kaltner, H ;
Gabius, HJ ;
Kloog, Y .
CANCER RESEARCH, 2004, 64 (09) :3112-3118
[13]   The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI [J].
Scheffzek, K ;
Stephan, I ;
Jensen, ON ;
Illenberger, D ;
Gierschik, P .
NATURE STRUCTURAL BIOLOGY, 2000, 7 (02) :122-126
[14]   A class of membrane proteins shaping the tubular endoplasmic reticulum [J].
Voeltz, GK ;
Prinz, WA ;
Shibata, Y ;
Rist, JM ;
Rapoport, TA .
CELL, 2006, 124 (03) :573-586
[15]   Photoreceptor cGMP phosphodiesterase δ subunit (PDEδ) functions as a prenyl-binding protein [J].
Zhang, HB ;
Liu, XH ;
Zhang, K ;
Chen, CK ;
Frederick, JM ;
Prestwich, GD ;
Baehr, W .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (01) :407-413