Ligand-binding domains in vitellogenin receptors and other LDL-receptor family members share a common ancestral ordering of cysteine-rich repeats

1998 ◽  
Vol 46 (4) ◽  
pp. 476-487 ◽  
Author(s):  
Thomas W. Sappington ◽  
Alexander S. Raikhel
Keyword(s):  
Ligand Binding ◽  
Family Members ◽  
Ldl Receptor ◽  
Binding Domains ◽  
Receptor Family

Interaction of beta2-Glycoprotein I with Members of the Low Density Lipoprotein Receptor Family.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 2646-2646
Author(s):  
Menno van Lummel ◽  
Maarten T.T. Pennings ◽  
Ronald H.W.M. Derksen ◽  
Erik Westein ◽  
Peter J. Lenting ◽  
...  
Keyword(s):  
Family Members ◽  
Ldl Receptor ◽  
Density Lipoprotein ◽  
Binding Kinetics ◽  
Binding Model ◽  
Glycoprotein I ◽  
Domain V ◽  
Kinetics Of ◽  
Site Binding ◽  
Receptor Family

Abstract The antiphospholipid syndrome (APS) is a non-inflammatory disease characterized by arterial and/or venous thrombosis and/or pregnancy morbidity in the presence of auto-antibodies that recognize beta2-glycoprotein I (beta2GPI) bound to cardiolipin. We have previously demonstrated that dimerization of beta2GPI by auto-antibodies induces platelet activation. This effect has been shown to be mediated by apoER2′. Here, we show that dimeric beta2GPI, and not plasma beta2GPI interacts with three different LDL-receptor family members; apolipoprotein E receptor 2′ (apoER2′), the low LDL-receptor related protein (LRP) and megalin. Interaction between dimeric beta2GPI and apoER2′ was best described with a one-site binding model (KD(app) 25 nM), whereas for LRP and megalin the interaction with dimeric beta2GPI was best described with a two-site binding model, representing a high- (3.1 nM) and a low-affinity site (192.1 and 241.2 nM, respectively). Binding kinetics of a dimeric beta2GPI mutant, that binds poorly to anionic phospholipids were similar to the binding kinetics of full length dimeric beta2GPI for all three LDL-receptor family members. Upon deletion of domain I or domain II of dimeric beta2GPI no changes in the binding kinetics were observed. Deletion of domain V however, significantly decreased the affinity for apoER2′, LRP and megalin. In conclusion, our data show that dimeric beta2GPI can interact with different LDL-receptor family members. This interaction is dependent on a recognition site in domain V of beta2GPI, which does not overlap with the phospholipid-binding site.

scholarly journals Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members

2007 ◽  
Vol 117 (1) ◽  
pp. 153-164 ◽  
Author(s):  
Jennifer M. MacArthur ◽  
Joseph R. Bishop ◽  
Kristin I. Stanford ◽  
Lianchun Wang ◽  
André Bensadoun ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Family Members ◽  
Ldl Receptor ◽  
Heparan Sulfate Proteoglycans ◽  
Receptor Family

scholarly journals Chicken oocyte growth is mediated by an eight ligand binding repeat member of the LDL receptor family.

1994 ◽  
Vol 13 (21) ◽  
pp. 5165-5175 ◽  
Author(s):  
H. Bujo ◽  
M. Hermann ◽  
M.O. Kaderli ◽  
L. Jacobsen ◽  
S. Sugawara ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Ldl Receptor ◽  
Oocyte Growth ◽  
Receptor Family

Trichosanthin Interacts with and Enters Cells via LDL Receptor Family Members

2000 ◽  
Vol 270 (2) ◽  
pp. 453-457 ◽  
Author(s):  
Wah-Lun Chan ◽  
Pang-Chui Shaw ◽  
Siu-Cheung Tam ◽  
Christian Jacobsen ◽  
Jørgen Gliemann ◽  
...  
Keyword(s):  
Family Members ◽  
Ldl Receptor ◽  
Receptor Family

scholarly journals Dissection of receptor folding and ligand-binding property with functional minireceptors of LDL receptor-related protein

2001 ◽  
Vol 114 (5) ◽  
pp. 899-908 ◽  
Author(s):  
L.M. Obermoeller-McCormick ◽  
Y. Li ◽  
H. Osaka ◽  
D.J. FitzGerald ◽  
A.L. Schwartz ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Ldl Receptor ◽  
Cell Surface Expression ◽  
Binding Property ◽  
Related Protein ◽  
Binding Properties ◽  
Binding Domains ◽  
Putative Ligand Binding

The LDL receptor-related protein (LRP) is a large, multifunctional endocytic receptor that binds and endocytoses a variety of structurally and functionally distinct ligands. LRP contains four putative ligand-binding domains. However, only domains II, III and IV, but not domain I, bind the receptor-associated protein (RAP), a molecular chaperone and universal antagonist for LRP. In order to dissect the function of RAP in LRP folding and to examine the ligand-binding properties of LRP, we generated LRP minireceptors that represent each of the four putative ligand-binding domains (termed mLRP1, mLRP2, mLRP3 and mLRP4, respectively). We found that proper folding and trafficking of mLRP2, mLRP3, mLRP4, but not mLRP1, is facilitated by coexpression of RAP. When these mLRPs were stably expressed in Chinese Hamster Ovary cells that lack the endogenous LRP, we found that each of these receptors was processed and traffics through the secretory pathway. Cell surface expression of these minireceptors was quantitatively examined by flow cytometric analyses. Using these minireceptor cell lines to map the ligand-binding domains, we found that although the majority of LRP ligands bind to both domain II and domain IV, Pseudomonas exotoxin A utilizes only domain IV for its binding to LRP. We conclude that while domains II and IV of LRP share many ligand-binding properties, each of the putative ligand-binding domains of LRP is unique in its contribution to ligand binding.

Sign in / Sign up

Export Citation Format

Share Document