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A more recent version of this article appeared on April 1, 2003

Papers In Press, published online ahead of print January 16, 2003
J. Lipid Res., doi:10.1194/jlr.M200432-JLR200
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Submitted on November 7, 2002
Revised on December 26, 2002
Accepted on January 3, 2003

Serum paraoxonase: effect of the apoproteins of HDL and the acute phase response

Veneracion G. Cabana, Catherine A. Reardon, Ning Feng, Sean-Xavier Neath, John R. Lukens, and Godfrey S. Getz

Pathology Dept., The University of Chicago, Chicago, IL 60637

Corresponding Author: vcabana{at}midway.uchicago.edu

Paraoxonase (PON), an HDL associated arylesterase, may have anti-atherogenic properties. Genetic variations of PON in human correlate with HDL cholesterol and apoA-I levels. Atherosclerosis occurs naturally in human and rabbit but not in mice. Using phenylacetate as a substrate, we compared variations in the levels and lipoprotein distribution of PON activity (henceforth referred to as PON AEase) in human, rabbit, and genetically modified mice. In humans and rabbits >95% of the PON AEase activity is HDL-associated. In mice, about 30% of PON AEase is lipid poor. In the absence of apoA-I in mice, total PON AEase is reduced, with >60% lipid poor. PON AEase level and distribution is restored in apoA-I-/- mice upon injection of adenovirus encoding human apoA-I and in transgenic animals expressing human apoA-I at a steady state level. Thus, while apoA-I is not required for the HDL association of PON AEase, induced variations in serum apoA-I level correlates with changes in HDL-associated but not with lipid poor PON AEase. PON AEase associates only with apoA-I or apoE containing HDL but not VLDL. In the absence of both apoA-I and apoE, PON AEase distributes exclusively to the lipid poor fraction. PON AEase is displaced from HDL during ultracentrifugal flotation and following incubation of serum with recombinant serum amyloid A. Variations in the PON distribution between HDL and the lipid poor fractions may have important consequences in its anti-oxidant activity and in atherogenesis.


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