Submit Data |  Help |  Video Tutorials |  News |  Publications |  FTP Download |  REST API |  Citing RGD |  Contact   

Inhibition of the binding of low density lipoproteins to liver membrane receptors by rat serum phosphorylcholine binding protein.

Authors: Saxena, U  Nagpurkar, A  Mookerjea, S 
Citation: Saxena U, etal., Biochem Biophys Res Commun. 1986 Nov 26;141(1):151-7.
Pubmed: (View Article at PubMed) PMID:3800992

Rat serum phosphorylcholine binding protein (PCBP) is characterized by its Ca2+ dependent property to bind phosphorylcholine ligand. PCBP immobilized on sepharose has been shown to selectively bind human plasma apo B and E containing lipoproteins. The present report describes an inhibitory effect of PCBP on the binding of human 125I-LDL to LDL receptors on estradiol treated rat liver membranes. Pre-incubation of liver membranes with PCBP did not affect the binding of 125I-LDL to the membranes. Gel filtration analysis of the incubation products from the LDL-receptor assay showed a concentration dependent binding of 125I-PCBP to LDL. The inhibitory effect of PCBP is likely due to the formation of LDL-PCBP complex and not due to the binding of PCBP to the LDL receptor site.


Gene Ontology Annotations
Objects Annotated

Additional Information

CRRD Object Information
CRRD ID: 9586005
Created: 2014-09-24
Species: All species
Last Modified: 2014-09-24
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.