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J Biol Chem, Vol. 273, Issue 24, 15241-15248, June 12, 1998
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From the Departments of The scavenger receptor class B, type I (SR-BI),
binds high density lipoprotein (HDL) and mediates selective uptake of
cholesteryl ester from HDL and HDL-dependent cholesterol
efflux from cells. We recently identified a new mRNA variant that
differs from the previously characterized form in that the encoded
C-terminal cytoplasmic domain is almost completely different. In the
present study, we demonstrate that the mRNAs for mouse SR-BI and
SR-BII (previously termed SR-BI.2) are the alternatively spliced
products of a single gene. The translation products predicted from
human, bovine, mouse, hamster, and rat cDNAs exhibit a high degree
of sequence similarity within the SR-BII C-terminal domain (62-67%
identity when compared with the human sequence), suggesting that this
variant is biologically important. SR-BII protein represents
approximately 12% of the total immunodetectable SR-BI/II protein in
mouse liver. Subcellular fractionation of transfected Chinese hamster
ovary cells showed that SR-BII, like SR-BI, is enriched in caveolae,
indicating that the altered cytoplasmic tail does not affect targeting
of the receptor. SR-BII mediated both selective cellular uptake of
cholesteryl ether from HDL as well as HDL-dependent
cholesterol efflux from cells, although with approximately 4-fold lower
efficiency than SR-BI. In vivo studies using adenoviral
vectors showed that SR-BII was relatively less efficient than SR-BI in
reducing plasma HDL cholesterol. These studies show that SR-BII, an HDL
receptor isoform containing a distinctly different cytoplasmic tail,
mediates selective lipid transfer between HDL and cells, but with a
lower efficiency than the previously characterized variant.
Internal Medicine and
§ Physiology, University of Kentucky Medical Center,
Lexington, Kentucky 40536 and the ¶ Veterans Affairs Medical
Center, Lexington, Kentucky 40511
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