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

Abstract:

:This study has examined the dimeric/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 as well as tissues of transgenic animals and genetically altered steroidogenic and nonsteroidogenic cells overexpressing the SR-B proteins. Using both biochemical and morphological techniques, we have seen that these dimeric and higher order 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; this difference does not extend to the use of SR-B cDNA types for transfection purposes. In a separate study, cotransfection of HEK293 cells with cMyc and V5 epitope-tagged SR-BI permitted coprecipitation and quantitative coimmunocytochemical measurements at the electron microscope level, suggesting that much of the newly expressed SR-BI protein in stimulated cells dimerizes 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.

journal_name

J Lipid Res

authors

Reaven E,Cortez Y,Leers-Sucheta S,Nomoto A,Azhar S

doi

10.1194/jlr.M300370-JLR200

keywords:

subject

Has Abstract

pub_date

2004-03-01 00:00:00

pages

513-28

issue

3

eissn

0022-2275

issn

1539-7262

pii

M300370-JLR200

journal_volume

45

pub_type

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