scholarly journals Intracellular fate of LDL receptor family members depends on the cooperation between their ligand-binding and EGF domains

2005 ◽  
Vol 118 (6) ◽  
pp. 1309-1320 ◽  
Author(s):  
D. Van Hoof
Keyword(s):  
Ligand Binding ◽  
Family Members ◽  
Ldl Receptor ◽  
Intracellular Fate ◽  
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

β2-Glycoprotein I and LDL-receptor family members

2004 ◽  
Vol 114 (5-6) ◽  
pp. 455-459 ◽  
Author(s):  
Philip G. de Groot ◽  
Menno van Lummel ◽  
Maarten Pennings ◽  
Rolf Urbanus ◽  
H. Bas de Laat ◽  
...  
Keyword(s):  
Family Members ◽  
Ldl Receptor ◽  
Glycoprotein I ◽  
Receptor Family
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