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J. Lipid Res.
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A more recent version of this article appeared on March 1, 2004

Papers In Press, published online ahead of print December 1, 2003
J. Lipid Res., doi:10.1194/jlr.M300370-JLR200
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Submitted on September 3, 2003
Revised on November 5, 2003
Accepted on November 20, 2003

Dimerization of the scavenger receptor class B type I: formation, function and localization in diverse cells and tissues

Eve Reaven, Yuan Cortez, Susan Leers-Sucheta, Ann Nomoto, and Salman Azhar

GRECC, VA Palo Alto Health Care System, Palo Alto, CA 94304

Corresponding Author: eve.reaven{at}med.va.gov

This study has examined the dimeric and higher order oligomeric forms of Scavenger Receptor Class B-type I (SR-BI), and its alternatively spliced form, SR-BII, in a diverse group of cells and tissues: i.e., normal and hormonally altered tissues of mice and rats, tissues of transgenic animals, and genetically altered steroidogenic and non-steroidogenic cells overexpressing the SR-B proteins. Using both biochemical and morphological techniques, we have seen that dimeric and oligomeric forms of SR-BI expression are strongly associated with both functional and morphological expression of the selective HDL cholesteryl ester uptake pathway. Rats and mice show some species differences in expression of SR-BII dimeric forms. In a separate study, co-transfection of HEK293 cells with cMyc and V5 epitope tagged SR-BI permitted co-precipitation and quantitative co-immunocytochemical measurements at the electron microscope level, suggesting that much of the newly expressed SR-BI protein dimerizes in stimulated cells, and that the SR-BI dimers are localized to the cell surface and specifically to microvillar or double membraned intracellular channels. These combined data suggest that SR-BI self-association represents an integral step in the selective cholesteryl ester uptake process.


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