Regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein E
Apolipoprotein E (apoE) enters the plasma as a component of discoidal HDL and is subsequently incorporated into spherical HDL, most of which contain apoE as the sole apolipoprotein. This study investigates the regulation, origins, and structure of spherical, apoE-containing HDLs and their remodeling...
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doaj-c09cb324b67b4ed1af5b36887c2674652021-04-27T04:44:39ZengElsevierJournal of Lipid Research0022-22752006-05-0147510251036Regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein EKerry-Anne Rye0Richard Bright1Maria Psaltis2Philip J. Barter3Lipid Research Group, The Heart Research Institute, Camperdown, Sydney, New South Wales, Australia 2050; Department of Medicine, University of Sydney, New South Wales, Australia 2006; Department of Medicine, University of Melbourne, Victoria, Australia 3010Lipid Research Group, The Heart Research Institute, Camperdown, Sydney, New South Wales, Australia 2050Lipid Research Group, The Heart Research Institute, Camperdown, Sydney, New South Wales, Australia 2050Lipid Research Group, The Heart Research Institute, Camperdown, Sydney, New South Wales, Australia 2050; Department of Medicine, University of Sydney, New South Wales, Australia 2006Apolipoprotein E (apoE) enters the plasma as a component of discoidal HDL and is subsequently incorporated into spherical HDL, most of which contain apoE as the sole apolipoprotein. This study investigates the regulation, origins, and structure of spherical, apoE-containing HDLs and their remodeling by cholesteryl ester transfer protein (CETP). When the ability of discoidal reconstituted high density lipoprotein (rHDL) containing apoE2 [(E2)rHDL], apoE3 [(E3)rHDL], or apoE4 [(E4)rHDL] as the sole apolipoprotein to act as substrates for LCAT were compared with that of discoidal rHDL containing apoA-I [(A-I)rHDL], the rate of cholesterol esterification was (A-I)rHDL >> (E2)rHDL ∼ (E3)rHDL > (E4)rHDL. LCAT also had a higher affinity for discoidal (A-I)rHDL than for the apoE-containing rHDL. When the discoidal rHDLs were incubated with LCAT and LDL, the resulting spherical (E2)rHDL, (E3)rHDL, and (E4)rHDL were larger than, and structurally distinct from, spherical (A-I)rHDL. Incubation of the apoE-containing spherical rHDL with CETP and Intralipid® generated large fusion products without the dissociation of apoE, whereas the spherical (A-I)rHDLs were remodeled into small particles with the formation of lipid-poor apoA-I. In conclusion, i) apoE activates LCAT less efficiently than apoA-I; ii) apoE-containing spherical rHDLs are structurally distinct from spherical (A-I)rHDL; and iii) the CETP-mediated remodeling of apoE-containing spherical rHDL differs from that of spherical (A-I)rHDL.http://www.sciencedirect.com/science/article/pii/S002222752033251Xcholesteryl ester transfer proteinapolipoprotein A-Ikinetics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Kerry-Anne Rye Richard Bright Maria Psaltis Philip J. Barter |
spellingShingle |
Kerry-Anne Rye Richard Bright Maria Psaltis Philip J. Barter Regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein E Journal of Lipid Research cholesteryl ester transfer protein apolipoprotein A-I kinetics |
author_facet |
Kerry-Anne Rye Richard Bright Maria Psaltis Philip J. Barter |
author_sort |
Kerry-Anne Rye |
title |
Regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein E |
title_short |
Regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein E |
title_full |
Regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein E |
title_fullStr |
Regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein E |
title_full_unstemmed |
Regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein E |
title_sort |
regulation of reconstituted high density lipoprotein structure and remodeling by apolipoprotein e |
publisher |
Elsevier |
series |
Journal of Lipid Research |
issn |
0022-2275 |
publishDate |
2006-05-01 |
description |
Apolipoprotein E (apoE) enters the plasma as a component of discoidal HDL and is subsequently incorporated into spherical HDL, most of which contain apoE as the sole apolipoprotein. This study investigates the regulation, origins, and structure of spherical, apoE-containing HDLs and their remodeling by cholesteryl ester transfer protein (CETP). When the ability of discoidal reconstituted high density lipoprotein (rHDL) containing apoE2 [(E2)rHDL], apoE3 [(E3)rHDL], or apoE4 [(E4)rHDL] as the sole apolipoprotein to act as substrates for LCAT were compared with that of discoidal rHDL containing apoA-I [(A-I)rHDL], the rate of cholesterol esterification was (A-I)rHDL >> (E2)rHDL ∼ (E3)rHDL > (E4)rHDL. LCAT also had a higher affinity for discoidal (A-I)rHDL than for the apoE-containing rHDL. When the discoidal rHDLs were incubated with LCAT and LDL, the resulting spherical (E2)rHDL, (E3)rHDL, and (E4)rHDL were larger than, and structurally distinct from, spherical (A-I)rHDL. Incubation of the apoE-containing spherical rHDL with CETP and Intralipid® generated large fusion products without the dissociation of apoE, whereas the spherical (A-I)rHDLs were remodeled into small particles with the formation of lipid-poor apoA-I. In conclusion, i) apoE activates LCAT less efficiently than apoA-I; ii) apoE-containing spherical rHDLs are structurally distinct from spherical (A-I)rHDL; and iii) the CETP-mediated remodeling of apoE-containing spherical rHDL differs from that of spherical (A-I)rHDL. |
topic |
cholesteryl ester transfer protein apolipoprotein A-I kinetics |
url |
http://www.sciencedirect.com/science/article/pii/S002222752033251X |
work_keys_str_mv |
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