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J. Biol. Chem., Vol. 266, Issue 34, 22866-22871, 12, 1991
LA Bottalico, RE Wager, LB Agellon, RK Assoian and I Tabas
The macrophage scavenger receptor, a 220-kDa trimeric membrane
glycoprotein, mediates the internalization of modified forms of low density
lipoprotein (LDL) such as acetyl-LDL and oxidized-LDL and thus is likely to
play a key role in atheroma macrophage foam cell formation. In addition,
recent evidence suggests that the scavenger receptor may be an important
macrophage binding site for lipopolysaccharide involved in
lipopolysaccharide scavenging by macrophages. However, little is known
about the regulation of this important receptor. We now report that the
induction of scavenger receptor activity (as measured by acetyl-LDL
stimulation of intracellular cholesterol esterification) seen in phorbol
ester- differentiated THP-1 human macrophages was completely suppressed to
the level seen in undifferentiated THP-1 monocytes by picomolar
concentrations of transforming growth factor-beta 1 (TGF-beta 1). 125I-
Acetyl-LDL degradation was inhibited in a dose-dependent manner by TGF-
beta 1, with maximal inhibition (approximately 70%) occurring at 24 pM
TGF-beta 1. Scatchard analysis revealed that TGF-beta 1 treatment resulted
in a approximately 2-fold decrease in receptor number, and Northern blot
analysis of RNA isolated from differentiated THP-1 macrophages demonstrated
approximately 2-fold less scavenger receptor mRNA in TGF-beta 1-treated
cells compared with that in macrophages not treated with TGF-beta 1. Since
TGF-beta 1 is thought to be present in both atherosclerotic and
inflammatory lesions, the above findings may have physiological relevance
regarding the regulation of atheroma foam cell formation and/or the
regulation of lipopolysaccharide clearance by macrophages.
Transforming growth factor-beta 1 inhibits scavenger receptor activity in THP-1 human macrophages
Department of Medicine, Columbia University College of Physicians and Surgeons, New York, New York 10032.
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