2007
DOI: 10.1042/bj20061048
|View full text |Cite
|
Sign up to set email alerts
|

Pathway of biogenesis of apolipoprotein E-containing HDL in vivo with the participation of ABCA1 and LCAT

Abstract: We have investigated the ability of apoE (apolipoprotein E) to participate in the biogenesis of HDL (high-density lipoprotein) particles in vivo using adenovirus-mediated gene transfer in apoA-I-/- (apolipoprotein A-I) or ABCA1-/- (ATP-binding cassette A1) mice. Infection of apoA-I-/- mice with 2x10(9) pfu (plaque-forming units) of an apoE4-expressing adenovirus increased both HDL and the triacylglycerol-rich VLDL (very-low-density lipoprotein)/IDL (intermediate-density lipoprotein)/LDL (low-density lipoprotei… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

3
74
1
9

Year Published

2009
2009
2016
2016

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 84 publications
(87 citation statements)
references
References 42 publications
3
74
1
9
Order By: Relevance
“…Lipid composition of HDL copper-deficient rats does not differ from that of copper adequate animals, unlike the ApoE fraction that shows a considerable enrichment [13,14]. Physiological concentrations of ApoE ensure the lipid homeostasis and its anti-atherogenic effects, while higher concentrations of ApoE are responsible for the spherical to discoidal transformation of HDL, which makes them unable to bind to the liver LDL receptors and slow down the retrograde transport of CL [15]. On the other hand, lecithin:cholesterol acyltransferase (LCAT) catalyzes the esterification of free CL in the HDL, contributing to the lipoprotein maturation and to the shape transition from the discoidal to the spherical form, but plasma LCAT activity in copper-deficient rats is considerably reduced [16].…”
Section: Discussionmentioning
confidence: 99%
“…Lipid composition of HDL copper-deficient rats does not differ from that of copper adequate animals, unlike the ApoE fraction that shows a considerable enrichment [13,14]. Physiological concentrations of ApoE ensure the lipid homeostasis and its anti-atherogenic effects, while higher concentrations of ApoE are responsible for the spherical to discoidal transformation of HDL, which makes them unable to bind to the liver LDL receptors and slow down the retrograde transport of CL [15]. On the other hand, lecithin:cholesterol acyltransferase (LCAT) catalyzes the esterification of free CL in the HDL, contributing to the lipoprotein maturation and to the shape transition from the discoidal to the spherical form, but plasma LCAT activity in copper-deficient rats is considerably reduced [16].…”
Section: Discussionmentioning
confidence: 99%
“…These functional interactions catalyze the transfer of phospholipids and subsequently cholesterol from intracellular membrane pools to lipidfree apoA-I or apoE leading to the formation of minimally lipidated particles which are gradually converted to discoidal particles ( 39,47,55,56 ). Subsequent esterifi cation of the cholesterol of the nascent pre-␤ and discoidal particles by LCAT generates the spherical HDL particles present in the plasma that can be visualized by EM ( 55,56 ). In the present study the ability of apoA-IV to promote de novo formation of HDL-A-IV particles was established by adenovirus mediated gene transfer in four different mouse models.…”
Section: Role Of Apoa-iv Abca1 and Lcat In The Biogenesis Of Hdl-a-ivmentioning
confidence: 99%
“…On the basis of studies using synthetic peptide mimics of apolipoproteins it appears that the key structural motif necessary for an apolipoprotein to function as a lipid acceptor is the presence amphipathic helices [201]. Studies in mice suggest that in addition to its role in clearing TG rich lipoproteins apoE participates in the biogenesis of apoE containing HDL particles with the participation of ABCA1 [202]. It is likely, however, that the concentration of lipid poor apolipoprotein in the extracellular fluid is more relevant for ABCA1 efflux (Figure 4).…”
Section: Abca1 and Hdl Assemblymentioning
confidence: 99%