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(Received for publication, September 11, 1996, and in revised form, December 10, 1996)
From the Department of Medicine, Clinical Nutrition Research Unit
and Section of Gastroenterology, University of Chicago,
Chicago, Illinois 60637
Recent data indicate that sterol carrier
protein-2 (SCP-2) functions in the rapid movement of newly synthesized
cholesterol to the plasma membrane (Puglielli, L., Rigotti, A., Greco,
A. V., Santos, M. J., and Nervi, F. (1995) J. Biol.
Chem. 270, 18723-18726). In order to further characterize the
cellular function of SCP-2, we transfected McA-RH7777 rat hepatoma
cells with a pre-SCP-2 cDNA expression construct. In stable
transfectants, pre-SCP-2 processing resulted in an 8-fold increase in
peroxisomal levels of SCP-2. SCP-2 overexpression increased the rates
of newly synthesized cholesterol transfer to the plasma membrane and
plasma membrane cholesterol internalization by 4-fold. There was no
effect of SCP-2 overexpression on the microsomal levels of
acyl-CoA:cholesterol acyltransferase and neutral cholesterol ester (CE)
hydrolase; however, in the intact cell, CE synthesis and mass were
reduced by 50%. SCP-2 overexpression also reduced high density
lipoprotein-cholesterol secretion and apoA-I gene expression by 70%
and doubled the rate of plasma membrane desmosterol conversion to
cholesterol. We conclude that SCP-2 overexpression enhances the rate of
cholesterol cycling, which reduces the availability of cholesterol for
CE synthesis and alters the activity of a cellular cholesterol pool
involved in regulating apoA-I-mediated high density lipoprotein
cholesterol secretion. The net result of these changes in cholesterol
metabolism is a 46% increase in plasma membrane cholesterol content,
the implications of which are discussed.
Volume 272, Number 10,
Issue of March 7, 1997
pp. 6490-6498
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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