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(Received for publication, February 26, 1996, and in revised form, September 13, 1996)
From the Laboratory of Biochemical Genetics and Metabolism, The
Rockefeller University, New York, New York 10021-6399
RAW 264 mouse macrophage cells were stably
transfected with human apolipoprotein E (apoE) expression
vectors. Clonal derivatives were characterized for expression of
the human apoE2, apoE3, and apoE4 isoforms. An apoE4-expressing clonal
cell line and a non-expressing clonal control cell line were loaded
overnight with either [3H]cholesterol or
[3H]choline. The cells were washed and incubated for
24 h in serum-free medium with or without the addition of
8-bromo-cyclic AMP (8-Br-cAMP). Only the apoE-secreting cells and only
in the presence of 8-Br-cAMP released large amounts of labeled
cholesterol or phosphatidylcholine into the medium. Mass analyses of
cellular free and esterified cholesterol confirmed the results of the
labeling studies; a decrease in cellular cholesterol content was
observed in the 8-Br-cAMP-treated apoE-secreting cells, concurrent with
an increase in cholesterol found in the medium. FPLC analysis of the
medium demonstrated that 8-Br-cAMP treatment of the apoE-secreting
cells led to an increased size fraction and amount of a peak of
secreted cholesterol which comigrated with apoE. The 8-Br-cAMP-mediated
increase in cholesterol efflux was also observed in non-apoE-secreting
cells incubated with exogenous apoE or apoAI, and the effect of apoE was saturable. The apoE2, apoE3, and apoE4 isoforms were equally efficient in promoting 8-Br-cAMP-dependent cholesterol
efflux. Reductive methylation of apoE abolished its ability to promote 8-Br-cAMP-dependent cholesterol efflux. Brefeldin A and
monensin, inhibitors of protein processing through the Golgi, both
blocked the 8-Br-cAMP stimulation of cholesterol efflux to exogenous
apoE. 8-Br-cAMP induced specific apoE and apoAI binding, but not apoE degradation, by the RAW cells. We present a model wherein cAMP induces
a membrane apolipoprotein receptor that does not lead to endocytosis
and degradation, but instead promotes the transfer of lipids to
apolipoproteins, which can then be released from the cell.
Volume 271, Number 48,
Issue of November 29, 1996
pp. 30647-30655
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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