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(Received for publication, January 29, 1997, and in revised form, March 10, 1997)
From the The class B, type I scavenger
receptor, SR-BI, was the first molecularly well defined cell surface
high density lipoprotein (HDL) receptor to be described. It mediates
transfer of lipid from HDL to cells via selective lipid uptake, a
mechanism distinct from receptor-mediated endocytosis via
clathrin-coated pits and vesicles. SR-BI is expressed most abundantly
in steroidogenic tissues (adrenal gland, ovary), where trophic hormones
coordinately regulate its expression with steroidogenesis, and in the
liver, where it may participate in reverse cholesterol transport. Here we have used immunochemical methods to study the structure and subcellular localization of murine SR-BI (mSR-BI) expressed either in
transfected Chinese hamster ovary cells or in murine adrenocortical Y1-BS1 cells. mSR-BI, an ~82-kDa glycoprotein, was initially
synthesized with multiple high mannose N-linked
oligosaccharide chains, and some, but not all, of these were processed
to complex forms during maturation of the protein in the Golgi
apparatus. Metabolic labeling with [3H]palmitate and
[3H]myristate demonstrated that mSR-BI was fatty
acylated, a property shared with CD36, another class B scavenger
receptor, and other proteins that concentrate in specialized,
cholesterol- and glycolipid-rich plasma membrane microdomains called
caveolae. OptiPrep density gradient fractionation of plasma membranes
established that mSR-BI copurified with caveolin-1, a constituent of
caveolae; and immunofluorescence microscopy demonstrated that mSR-BI
colocalized with caveolin-1 in punctate microdomains across the surface
of cells and on the edges of cells. Thus, mSR-BI colocalizes with
caveolae, and this raises the possibility that the unique properties of
these specialized cell surface domains may play a critical role in
SR-BI-mediated transfer of lipids between lipoproteins and cells.
Volume 272, Number 20,
Issue of May 16, 1997
pp. 13242-13249
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
,
,
,
and
Department of Biology, Massachusetts
Institute of Technology, Cambridge, Massachusetts 02139, the
§ Division of Health Sciences and Technology,
Harvard-Massachusetts Institute of Technology, Cambridge,
Massachusetts 02139, and the ** Department of Cell Biology and
Neuroscience, University of Texas Southwestern Medical Center,
Dallas, Texas 75235
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 F. Schroeder, A. M. Gallegos, B. P. Atshaves, S. M. Storey, A. L. McIntosh, A. D. Petrescu, H. Huang, O. Starodub, H. Chao, H. Yang, et al. Recent Advances in Membrane Microdomains: Rafts, Caveolae, and Intracellular Cholesterol Trafficking Experimental Biology and Medicine, November 1, 2001; 226(10): 873 - 890. [Abstract] [Full Text] [PDF]
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G. A. Graf, K. L. Roswell, and E. J. Smart 17{beta}-Estradiol promotes the up-regulation of SR-BII in HepG2 cells and in rat livers J. Lipid Res., September 1, 2001; 42(9): 1444 - 1449. [Abstract] [Full Text] [PDF]
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