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J. Biol. Chem., Vol. 276, Issue 29, 26898-26905, July 20, 2001
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From the § Lipid Research Laboratory, The Hanson Centre,
Adelaide, South Australia 5000, Australia, Phospholipid transfer protein (PLTP) remodels
high density lipoproteins (HDL) into large and small particles. It also
mediates the dissociation of lipid-poor or lipid-free apolipoprotein
A-I (apoA-I) from HDL. Remodeling is enhanced markedly in triglyceride (TG)-enriched HDL (Rye, K.-A., Jauhiainen, M., Barter, P. J., and
Ehnholm. C. (1998) J. Lipid. Res. 39, 613-622). This study defines the mechanism of the remodeling of HDL by PLTP and determines why it is enhanced in TG-enriched HDL. Homogeneous populations of
spherical reconstituted HDL (rHDL) containing apoA-I and either cholesteryl esters only (CE-rHDL; diameter 9.3 nm) or CE and TG in
their core (TG-rHDL; diameter 9.5 nm) were used. After 24 h of
incubation with PLTP, all of the TG-rHDL, but only a proportion of the
CE-rHDL, were converted into large (11.3-nm diameter) and small (7.7-nm
diameter) particles. Only small particles were formed during the first
6 h of incubation of CE-rHDL with PLTP. The large particles and
dissociated apoA-I were apparent after 12 h. In the case of
TG-rHDL, small particles appeared after 1 h of incubation, while
dissociated apoA-I and large particles were apparent at 3 h. The
composition of the large particles indicated that they were derived
from a fusion product. Spectroscopic studies indicated that the apoA-I
in TG-rHDL was less stable than the apoA-I in CE-rHDL. In conclusion,
these results show that (i) PLTP mediates rHDL fusion, (ii) the fusion
product rearranges by two independent processes into small and large
particles, and (iii) the more rapid remodeling of TG-rHDL by PLTP may
be due to the destabilization of apoA-I.
The Mechanism of the Remodeling of High Density Lipoproteins by
Phospholipid Transfer Protein*
§¶,§,
,§§
Department of
Medicine, The University of Adelaide, Royal Adelaide Hospital, Adelaide
5000, South Australia, Australia, The Scripps Research
Institute, La Jolla, California 92037, the ** Department of
Biochemistry, National Public Health Institute, Helsinki
FIN-00300, Finland, and the
Division of Cardiovascular Services, Royal
Adelaide Hospital,
Adelaide 5000, South Australia, Australia
*
This work was supported by the National Health and Medical
Research Council of Australia.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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