SR-B1 belongs to the CD36 scavenger receptor family and serves as a receptor for several ligands including phospholipids, cholesterol ester, lipoproteins, phosphatidylserine, and caveolae localized HDL. It is expressed in endothelial cells, macrophages, and dendritic cells. It facilitates the flux of both free and esterified cholesterol between the cell surface and extracellular donors and acceptors (HDL and to a lesser extent, apoB-containing lipoproteins and modified lipoproteins). Thus SR-B1 plays an important role in meditating the uptake of HDL-derived cholesterol and cholesterol ester in both liver and steroidogenic tissues. It also appears to be involved in the phagocytosis of apoptotic cells, uptake of lipid soluble vitamins (vitamin E and carotenoids), as well as pathogen recognition, and the anti-inflammatory response. SR-BI has also been involved in the capture and cross-presentation of antigens from viruses, bacteria and parasites.
Liu’s group used the SR-B1 antibody in their knockout mice studies aimed at understanding the effects of sphingomyelin synthase (SMS2) deficiency on atherosclerosis1. The SR-B1 antibody was used in flow cytometry and immunoblotting experiments to demonstrate that oxidized (but not native) HDL acquires anti-thrombotic activity2. Additional flow studies with the SR-B1 antibody were done in Zhou’s lab, where they investigated the role of the receptor of advanced glycation end products (RAGE) in podocyte apoptosis3. Use of the SR-B1 antibody allowed them to follow up their previous work in podocyte signaling to demonstrate that the interaction of RAGE interacts with advanced oxidation protein products (AOPPs) contributes to chronic kidney disease progression. The SR-B1 antibody enabled Molina-Jimenez’s group to validate a novel matrigel-based three-dimensional hepatocyte cell culture system as a model cell line-based polarized system capable of robust infection and virion production4.
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