Endothelial Lipase Modulates Paraoxonase 1 Content and Arylesterase Activity of HDL.
NMR spectroscopy
arylesterase activity
endothelial lipase
high-density lipoprotein
mass spectrometry
paraoxonase 1
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
13 Jan 2021
13 Jan 2021
Historique:
received:
18
12
2020
revised:
09
01
2021
accepted:
11
01
2021
entrez:
16
1
2021
pubmed:
17
1
2021
medline:
13
4
2021
Statut:
epublish
Résumé
Endothelial lipase (EL) is a strong modulator of the high-density lipoprotein (HDL) structure, composition, and function. Here, we examined the impact of EL on HDL paraoxonase 1 (PON1) content and arylesterase (AE) activity in vitro and in vivo. The incubation of HDL with EL-overexpressing HepG2 cells decreased HDL size, PON1 content, and AE activity. The EL modification of HDL did not diminish the capacity of HDL to associate with PON1 when EL-modified HDL was incubated with PON1-overexpressing cells. The overexpression of EL in mice significantly decreased HDL serum levels but unexpectedly increased HDL PON1 content and HDL AE activity. Enzymatically inactive EL had no effect on the PON1 content of HDL in mice. In healthy subjects, EL serum levels were not significantly correlated with HDL levels. However, HDL PON1 content was positively associated with EL serum levels. The EL-induced changes in the HDL-lipid composition were not linked to the HDL PON1 content. We conclude that primarily, the interaction of enzymatically active EL with HDL, rather than EL-induced alterations in HDL size and composition, causes PON1 displacement from HDL in vitro. In vivo, the EL-mediated reduction of HDL serum levels and the consequently increased PON1-to-HDL ratio in serum increase HDL PON1 content and AE activity in mice. In humans, additional mechanisms appear to underlie the association of EL serum levels and HDL PON1 content.
Identifiants
pubmed: 33450841
pii: ijms22020719
doi: 10.3390/ijms22020719
pmc: PMC7828365
pii:
doi:
Substances chimiques
Lipoproteins, HDL
0
Carboxylic Ester Hydrolases
EC 3.1.1.-
arylesterase
EC 3.1.1.2
Lipase
EC 3.1.1.3
Aryldialkylphosphatase
EC 3.1.8.1
PON1 protein, human
EC 3.1.8.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Austrian Science Fund FWF
ID : DOC 31
Pays : Austria
Organisme : Austrian Science Fund FWF
ID : W 1226
Pays : Austria
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