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Journal of Lipid Research, Vol 35, 825-835, Copyright © 1994 by Lipid Research, Inc.
L Lagrost, A Athias, P Gambert and C Lallemant
In the present study, a sequential procedure was set up to separate
simultaneously cholesteryl ester transfer protein (CETP), phospholipid
transfer protein (PTP), and lecithin:cholesterol acyltransferase (LCAT)
from human plasma. Subsequently, phospholipid transfer activities of
purified lipid transfer proteins, deprived of LCAT activity, were compared
and potential interactions between the two proteins were studied.
Phospholipid transfer (PT) activity was determined by using three
independent assays that measured the transfer of radiolabeled
phosphatidylcholine ([14C]PC) either from phospholipid liposomes to high
density lipoproteins-3 (PTliposome-->HDL3), from high density
lipoproteins-3 to phospholipid liposomes (PTHDL3-->liposome), or from
HDL3 to low density lipoproteins (PTHDL3-->LDL). Comparative study of
CETP and PTP pointed out several differences in the ability of the two
proteins to transfer phospholipids. i) Whereas both CETP and PTP were able
to mediate phospholipid transfers from [14C]PC-HDL3 to LDL, only PTP
facilitated phospholipid transfers from [14C]PC-liposomes to HDL3. ii) As
PTP did not promote the transfer of phospholipids from [14C]PC- HDL3 to
liposomes, it was concluded that it functions as a phospholipid transfer
protein rather than a phospholipid exchange protein. This latter point was
confirmed by the ability of purified PTP to induce the net mass transfer of
phospholipids from PC-liposomes to HDL3. iii) While PTP presented no
intrinsic cholesteryl ester transfer activity, it was able to significantly
increase CETP-mediated cholesteryl ester transfers from HDL3 to LDL. iv)
CETP did not influence the PTliposome-- >HDL3 activity induced by PTP.
v) Oleic acid was able to significantly increase the cholesteryl ester
transfer activity of CETP, but not the PTliposome-->HDL3 activity of
PTP. vi) PTHDL3-->LDL activity of purified CETP was explained, for a
large part, by the copurification of nonesterified fatty acids. Taken
together, data of the present report suggest that phospholipid transfer
activity of CETP and PTP could occur through distinct processes. Since, in
human plasma, PTP is not only responsible for the major part of
phospholipid net mass transfer but is also able in vitro to modulate the
CETP-mediated transfer of cholesteryl esters between various plasma
lipoprotein fractions, it could play a determinant role in lipoprotein
remodeling in vivo.
ARTICLES
Comparative study of phospholipid transfer activities mediated by cholesteryl ester transfer protein and phospholipid transfer protein
Laboratoire de Biochimie des Lipoproteines, INSERM CJF 93-10, Faculte de Medecine, Dijon, France.
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