Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 276, Issue 29, Pages 26898-26905Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M010708200
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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.
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