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J. Biol. Chem., Vol. 265, Issue 14, 7859-7863, May, 1990
A Steinmetz, R Barbaras, N Ghalim, V Clavey, JC Fruchart and G Ailhaud
Cholesterol efflux was studied in cultured mouse adipose cells after
preloading with low density lipoprotein cholesterol. Exposure to complexes
containing human apolipoprotein A-IV and L-alpha-
dimyristoylphosphatidylcholine (DMPC) as well as to human lipoprotein
particles containing apolipoprotein A-IV but not apolipoprotein A-I and
particles containing apolipoproteins A-IV and A-I showed that both
artificial and native apolipoprotein A-IV-containing particles were able to
promote cholesterol efflux at 37 degrees C as a function of time and
concentration. The half-maximal concentration was found to be 0.3 X 10(-6)
M for apolipoprotein A-IV.DMPC complexes. Binding experiments performed in
intact cells at 4 degrees C with labeled apolipoprotein A-IV.DMPC complexes
showed the existence of specific binding sites, with a Kd value of 0.32 x
10(-6) M and a maximal binding capacity of 223,000 sites/cell. By
cross-competition experiments with labeled and unlabeled complexes
containing apolipoprotein A-IV, A-I, or A-II, it appeared that all three
apolipoproteins bind to the same cell- surface recognition sites. It is
suggested that apolipoprotein A-IV, which is present in the interstitial
fluid surrounding adipose cells in vivo at concentrations similar to those
required in vitro for the promotion of cholesterol efflux, plays a critical
role in cholesterol removal from peripheral cells.
Human apolipoprotein A-IV binds to apolipoprotein A-I/A-II receptor sites and promotes cholesterol efflux from adipose cells
SERLIA, Institut Pasteur, Lille, France.
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