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(Received for publication, October 18, 1996, and in revised form, December 17, 1996)
From the Burnsides Research Laboratory, Department of Food Science
and Human Nutrition, University of Illinois,
Urbana, Illinois 61801
Phospholipid transfer protein (PLTP) purified
from human plasma was found to enhance the transfer of cholesterol from
single bilayer vesicles containing phosphatidylcholine and cholesterol to high density lipoprotein-3. The rate of cholesterol transfer was
greatly influenced by the cholesterol content of the donor vesicles.
The maximal rate was observed with the vesicles containing 20-25
mol % cholesterol. This was in contrast to a progressive decline in
the rate of phosphatidylcholine transfer with an increase in the
cholesterol content. To determine the binding of cholesterol and
phosphatidylcholine to PLTP, the mixtures of PLTP and the vesicles
containing 3H-labeled phosphatidylcholine and
14C-labeled cholesterol were incubated and subjected to
sucrose density gradient centrifugation. Determination of the label
profiles showed that cholesterol as well as phosphatidylcholine were
transferred from the vesicles to PLTP. The reversible nature of the
binding was shown by the transfer of labeled cholesterol and
phosphatidylcholine bound to PLTP to the acceptor vesicles or low
density lipoprotein. Isothermal equilibrium binding of PLTP for
cholesterol and phosphatidylcholine showed that PLTP possessed a
considerably higher affinity and binding capacity for
phosphatidylcholine than for cholesterol. The phosphatidylcholine
binding affinity and capacity were greater when PLTP was incubated with
phosphatidylcholine vesicles without cholesterol. A possible importance
of PLTP-mediated cholesterol transfer in the circulation was
described.
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