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Title

HDL subfraction distribution of paraoxonase-1 and its relevance to enzyme activity and resistance to oxidative stress
Authors
Moren, Xenia
Deakin, Sara Patricia
Liu, Ming-Lin
Taskinen, Marja-Riitta
James, Richard William
Published in Journal of Lipid Research. 2008, vol. 49, no. 6, p. 1246-53
Abstract The subfraction distribution of HDL-associated peptides has implications for their functions and the impact of pathological modifications to lipoprotein metabolism on these functions. We have analyzed the subfraction distribution of paraoxonase-1 (PON1) and the consequences for enzyme activity and stability. HDL subfractions were defined by the presence (LpA-I,A-II) or absence (LpA-I) of apolipoprotein A-II (apoA-II). PON1 was present in both subfractions, although increased concentrations of HDL were associated with significantly increased PON1 in LpA-I. ApoA-II did not modify the capacity of native human HDL or reconstituted HDL to promote PON1 secretion from cells or to stabilize enzyme activity, nor did apoA-II decrease PON1 activity when added to rabbit serum normally devoid of the apolipoprotein. LpA-I,A-II particles isolated from human serum or reconstituted HDL (LpA-I,A-II) showed a significantly greater capacity than HDL(LpA-I) to stabilize secreted PON1 and purified recombinant PON1 added to such particles. PON1 associated with apoA-II-containing particles showed greater resistance to inactivation arising from oxidation. ApoA-I, apoA-II, and LpA-I,A-II, but not LpA-I, were independent determinants of serum PON1 concentration and activity in multivariate analyses. PON1 is at least equally distributed between LpA-I and LpA-II,A-II HDL particles. This dichotomous distribution has implications for PON1 activity and stability that may impact on the physiological role of the enzyme.
Keywords Animals — Aryldialkylphosphatase/metabolism — CHO Cells — Chromatography, Liquid — Cricetinae — Cricetulus — Enzyme Stability — Lipoproteins, HDL/blood/metabolism — Oxidative Stress
Identifiers
PMID: 18314464
Full text
Article (Author postprint) (225 Kb) - document accessible for UNIGE members only Limited access to UNIGE
Other version: http://www.jlr.org/cgi/content/full/49/6/1246
Structures
Faculté de médecine / Section de médecine clinique / Département de médecine interne des spécialités
Research group Lipoprotéines sériques (598)
Citation
(ISO format) 		MOREN, Xenia et al. HDL subfraction distribution of paraoxonase-1 and its relevance to enzyme activity and resistance to oxidative stress. In: Journal of Lipid Research, 2008, vol. 49, n° 6, p. 1246-53. https://archive-ouverte.unige.ch/unige:905

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Deposited on : 2009-02-24

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