Lipids in Health and Disease
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 ResearchLipoprotein binding preference of CD36 is altered by filipin treatmentJianshe Zhang1  , Wuying Chu1  and Ian Crandall2 1
Department of Bioengineering and Environmental Science, Changsha University, Changsha, Hunan, PR China 2
Department of Medicine, University of Toronto, Toronto, M5S 1A8, Canada  author email corresponding author email
Lipids in Health and Disease 2008,
7:23doi:10.1186/1476-511X-7-23 Abstract
The class B scavenger receptor CD36 binds multiple ligands, including oxidized and native lipoprotein species. CD36 and the related receptor SR-B1 have been localized to caveolae, domains that participate in cell signaling, transcytosis, and regulation of cellular cholesterol homeostasis. Previous work has indicated that the ligand preference of CD36 may depend on the cell type in which it is expressed. To determine if the presence or absence of caveolae is the determining factor for lipoprotein preference, we treated CHO-CD36 and C32 cells with filipin. Filipin treatment rapidly increased the binding capacity of CD36 for the native lipoproteins HDL and LDL, but did not affect the binding capacity of CD36 for oxidized LDL. Filipin treatment affected the distribution of caveolin and CD36 suggesting that the presence caveolae may modulate the ligand preference of CD36. However, its molecular mechanism how CD36 and caveolin interaction in regulating lipoprotein transport remains to be further studied. | 
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