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 Members of the syndecan family of heparan sulfate proteoglycans are expressed in distinct cell-, tissue-, and development-specific patterns.

1994 ◽  
Vol 5 (7) ◽  
pp. 797-805 ◽  
Author(s):  
C W Kim ◽  
O A Goldberger ◽  
R L Gallo ◽  
M Bernfield
Keyword(s):  
Heparan Sulfate ◽  
Family Member ◽  
Cultured Cells ◽  
Family Members ◽  
Cell Types ◽  
Heparan Sulfate Proteoglycans ◽  
Mrna Levels ◽  
Cell Tissue ◽  
Mouse Tissues ◽  
The Individual

The syndecans are a gene family of four transmembrane heparan sulfate proteoglycans that bind, via their HS chains, diverse components of the cellular microenvironment. To evaluate the expression of the individual syndecans, we prepared cDNA probes to compare mRNA levels in various adult mouse tissues and cultured mouse cells representing various epithelial, fibroblastic, endothelial, and neural cell types and B cells at various stages of differentiation. We also prepared antibody probes to assess whether the extracellular domains of the individual syndecans are shed into the conditioned media of cultured cells. Our results show that all cells and tissues studied, except B-stem cells, express at least one syndecan family member; most cells and tissues express multiple syndecans. However, each syndecan family member is expressed selectively in cell-, tissue-, and development-specific patterns. The extracellular domain of all syndecan family members is shed as an intact proteoglycan. Thus, most, if not all, cells acquire a distinctive repertoire of the four syndecan family members as they differentiate, resulting in selective patterns of expression that likely reflect distinct functions.

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 P4770PCSK9-induced LDL receptor degradation depends on heparan sulfate proteoglycans

2018 ◽  
Vol 39 (suppl_1) ◽  
Author(s):  
S Glerup Pedersen ◽  
J Vilstrup ◽  
P Madsen ◽  
C Gustafsen
Keyword(s):  
Heparan Sulfate ◽  
Ldl Receptor ◽  
Heparan Sulfate Proteoglycans
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