J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.M700439-JLR200 on February 26, 2008

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Journal of Lipid Research, Vol. 49, 1246-1253, June 2008
Copyright © 2008 by American Society for Biochemistry and Molecular Biology

HDL subfraction distribution of paraoxonase-1 and its relevance to enzyme activity and resistance to oxidative stress

Xenia Moren*, Sara Deakin*, Ming-Lin Liu{dagger}, Marja-Riitta Taskinen§ and Richard W. James1,*

* Clinical Diabetes Unit, Department of Internal Medicine, University Hospital, Geneva, Switzerland
{dagger} Division of Endocrinology, Thomas Jefferson University, Philadelphia, PA
§ Department of Internal Medicine, Helsinki University Central Hospital, Helsinki, Finland

The study was supported by a grant from the Swiss National Research Foundation (R.W.J.), an Erityisvaltionosuus grant from Helsinki University Central Hospital (M.R.T.), and by a Beginning Grant-In-Aid, Grant 0765254U (M-L.L.), from the American Heart Association.

Published, JLR Papers in Press, February 26, 2008.

1 To whom correspondence should be addressed. e-mail: Richard.James{at}hcuge.ch

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.

Supplementary key words lipoprotein • atherosclerosis • ApoA-I • ApoA-II

Abbreviations: AAPH, 2,2'-azobis (2-amidinopropane) hydrochloride; apoA-II, apolipoprotein A-II; ARE, arylesterase; CHO, Chinese hamster ovary; PON1, paraoxonase-1


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