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J Biol Chem, Vol. 273, Issue 28, 17391-17398, July 10, 1998
From the Lipid and Lipoprotein Research Group and the Department of
Medicine, University of Alberta, Edmonton,
Alberta T6G 2S2, Canada
Myeloperoxidase secreted by
phagocytes in the artery wall may be a catalyst for lipoprotein
oxidation. High density lipoprotein (HDL) oxidized by
peroxidase-generated tyrosyl radical has a markedly enhanced ability to
deplete cultured cells of cholesterol. We have investigated the
structural modifications in tyrosylated HDL responsible for this
effect. Spherical reconstituted HDL (rHDL) containing the whole
apolipoprotein (apo) fraction of tyrosylated HDL reproduced the ability
of intact tyrosylated HDL to enhance cholesterol efflux from
cholesterol-loaded human fibroblasts when reconstituted with the whole
lipid fraction of either HDL or tyrosylated HDL. Free apoAI or apoAII
showed no increased capacity to induce cholesterol efflux from
cholesterol-loaded fibroblasts following oxidation by tyrosyl radical,
either in their lipid-free forms or in rHDL. The product of oxidation
of a mixture of apoAI and apoAII (1:1 molar ratio) by tyrosyl radical,
however, reproduced the enhanced ability of tyrosylated HDL to induce
cholesterol efflux when reconstituted with the whole lipid fraction of
HDL. HDL containing only apoAI or apoAII showed no enhanced ability to
promote cholesterol efflux following oxidation by tyrosyl radical, whereas HDL containing both apoAI and apoAII did. rHDL containing apoAI-apoAIImonomer and apoAI-(apoAII)2
heterodimers showed a markedly increased ability to prevent the
accumulation of LDL-derived cholesterol mass by sterol-depleted
fibroblasts compared with other apolipoprotein species of tyrosylated
HDL. These results indicate a novel product of HDL oxidation,
apoAI-apoAII heterodimers, with a markedly enhanced capacity to deplete
cells of the regulatory pool of free cholesterol and total cholesterol
mass. The recent observation of tyrosyl radical-oxidized LDL in
vivo suggests that a similar modification of HDL would
significantly enhance its ability to deplete peripheral cells of
cholesterol in the first step of reverse cholesterol transport.
Enhanced Cholesterol Efflux by Tyrosyl Radical-oxidized High
Density Lipoprotein Is Mediated by Apolipoprotein AI-AII
Heterodimers
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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