VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.

<h4>Objective</h4>ApoE is an abundant component of chylomicron, VLDL, IDL, and HDL. It binds to multiple types of lipids and is implicated in cholesterol and triglyceride homeostasis. Oxidation of ApoE plays a crucial role in the genesis of atherosclerosis. It is proposed that heme-conta...

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Autores principales:	Youfeng Yang, Zehong Cao, Ling Tian, W Timothy Garvey, Guangjie Cheng
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/895833b63d5543c3906fef42e59d62df
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spelling	oai:doaj.org-article:895833b63d5543c3906fef42e59d62df2021-11-18T07:56:04ZVPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.1932-620310.1371/journal.pone.0057571https://doaj.org/article/895833b63d5543c3906fef42e59d62df2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23451244/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Objective</h4>ApoE is an abundant component of chylomicron, VLDL, IDL, and HDL. It binds to multiple types of lipids and is implicated in cholesterol and triglyceride homeostasis. Oxidation of ApoE plays a crucial role in the genesis of atherosclerosis. It is proposed that heme-containing peroxidases (hPx) are major mediators of lipoprotein oxidization. Vascular peroxidase 1 (VPO1) is a recently-discovered hPx, which is expressed in cardiovascular system, lung, liver etc. and secreted into plasma. Its plasma concentration is three orders of magnitude of that of myeloperoxidase. If VPO1 mediates ApoE oxidation and affects the lipid metabolism remains to be elucidated.<h4>Methods</h4>Recombinant ApoE and VPO1 were expressed and purified from stably-expressing cell lines deriving from HEK293 cells. ApoE oxidation was carried out by VPO1 in the presence of H2O2 and chloride. ApoE oxidation was verified by a variety of approaches including immunoblot and amino acid analyses. To evaluate the functional changes in VPO1-oxidized ApoE, lipid emulsion particle binding assays were employed.<h4>Results</h4>Oxidized ApoE binds weaker to lipid emulsion particles, which mimic the large lipid complexes in vivo. In lipid efflux assay, oxidized ApoE showed reduced capability in efflux of lipids from foam cells. Mice administrated with oxidized ApoE via blood exhibited weaker clearance ability of plasma lipids.<h4>Conclusions</h4>Our data suggest that VPO1 is a new mediator regulating lipid homeostasis, implying a role in genesis and development of atherosclerosis.Youfeng YangZehong CaoLing TianW Timothy GarveyGuangjie ChengPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 2, p e57571 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Youfeng Yang Zehong Cao Ling Tian W Timothy Garvey Guangjie Cheng VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.
description	<h4>Objective</h4>ApoE is an abundant component of chylomicron, VLDL, IDL, and HDL. It binds to multiple types of lipids and is implicated in cholesterol and triglyceride homeostasis. Oxidation of ApoE plays a crucial role in the genesis of atherosclerosis. It is proposed that heme-containing peroxidases (hPx) are major mediators of lipoprotein oxidization. Vascular peroxidase 1 (VPO1) is a recently-discovered hPx, which is expressed in cardiovascular system, lung, liver etc. and secreted into plasma. Its plasma concentration is three orders of magnitude of that of myeloperoxidase. If VPO1 mediates ApoE oxidation and affects the lipid metabolism remains to be elucidated.<h4>Methods</h4>Recombinant ApoE and VPO1 were expressed and purified from stably-expressing cell lines deriving from HEK293 cells. ApoE oxidation was carried out by VPO1 in the presence of H2O2 and chloride. ApoE oxidation was verified by a variety of approaches including immunoblot and amino acid analyses. To evaluate the functional changes in VPO1-oxidized ApoE, lipid emulsion particle binding assays were employed.<h4>Results</h4>Oxidized ApoE binds weaker to lipid emulsion particles, which mimic the large lipid complexes in vivo. In lipid efflux assay, oxidized ApoE showed reduced capability in efflux of lipids from foam cells. Mice administrated with oxidized ApoE via blood exhibited weaker clearance ability of plasma lipids.<h4>Conclusions</h4>Our data suggest that VPO1 is a new mediator regulating lipid homeostasis, implying a role in genesis and development of atherosclerosis.
format	article
author	Youfeng Yang Zehong Cao Ling Tian W Timothy Garvey Guangjie Cheng
author_facet	Youfeng Yang Zehong Cao Ling Tian W Timothy Garvey Guangjie Cheng
author_sort	Youfeng Yang
title	VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.
title_short	VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.
title_full	VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.
title_fullStr	VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.
title_full_unstemmed	VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.
title_sort	vpo1 mediates apoe oxidation and impairs the clearance of plasma lipids.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/895833b63d5543c3906fef42e59d62df
work_keys_str_mv	AT youfengyang vpo1mediatesapoeoxidationandimpairstheclearanceofplasmalipids AT zehongcao vpo1mediatesapoeoxidationandimpairstheclearanceofplasmalipids AT lingtian vpo1mediatesapoeoxidationandimpairstheclearanceofplasmalipids AT wtimothygarvey vpo1mediatesapoeoxidationandimpairstheclearanceofplasmalipids AT guangjiecheng vpo1mediatesapoeoxidationandimpairstheclearanceofplasmalipids
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VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids.

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