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J. Biol. Chem., Vol. 266, Issue 9, 5486-5496, Mar, 1991
JR Jefferson, JP Slotte, G Nemecz, A Pastuszyn, TJ Scallen and F Schroeder
The potential role of liver fatty acid binding protein (L-FABP) in
modulating cellular sterol distribution was examined in mouse L-cell
fibroblasts transfected with cDNA encoding L-FABP. L-cells were chosen
because they contain only a small amount of endogenous FABP which does not
bind [3H]cholesterol, does not enhance intermembrane sterol transfer, and
whose content is unaltered by the expression of L-FABP. Transfected L-cells
expressed 0.34% of cytosolic protein as L-FABP. Transfection alone with low
expression of L-FABP (0.008% of cytosolic protein) had no effect on any of
the parameters tested. Three aspects of cellular sterol transfer were
examined. First, cellular sterol uptake, monitored by [3H]cholesterol and
the fluorescent sterol, delta- 5,7,9(11),22-ergostatetraen-3 beta-ol, was
increased 21.5 +/- 2.6% (p less than 0.001) in L-cells expressing L-FABP.
This increase was not accounted for by increased sterol esterification in
the cells expressing L-FABP. Inhibition of both cholesterol transfer and
esterification with 3-(decyldimethylsilyl)-N-[2-(4-methylphenyl)-1-
phenylethyl]propanamide from Sandoz abolished the L-FABP related
enhancement of both [3H]cholesterol uptake and esterification. Second,
plasma membrane transbilayer distribution of sterol, determined by
fluorescence methods indicated that the majority of sterol was in the inner
leaflet of the plasma membrane. In transfected cells expressing L- FABP,
twice as much sterol (28 +/- 4%) was present in the exofacial leaflet of
the plasma membrane as compared to that of control cells (15 +/- 2%).
Third, expression of L-FABP enhanced sterol transfer from the plasma
membrane to microsomes in intact cells. Treatment of [3H]cholesterol or
[3H]oleate-loaded cells with sphingomyelinase resulted in increased
formation of radiolabeled cholesterol ester, consistent with enhanced
microsomal esterification of plasma membrane derived cholesterol.
Concomitantly, plasma membrane [3H]cholesterol became less accessible to
oxidation by cholesterol oxidase. Sphingomyelinase-stimulated cholesterol
esterification was 21 +/- 3% greater in transfected cells. Concomitantly,
accessibility of plasma membrane [3H]cholesterol to cholesterol oxidase was
decreased 18 +/- 3% in cells expressing L-FABP. These differences are
consistent with the ability of L-FABP to influence sterol transport and
plasma membrane transbilayer sterol distribution in intact cells.
Intracellular sterol distribution in transfected mouse L-cell fibroblasts expressing rat liver fatty acid-binding protein
Department of Pharmacology and Cell Biophysics, University of Cincinnati Medical Center, Ohio 45267-0004.
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