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Correspondence to:
Philippe Moulin
High density lipoprotein (HDL)-associated paraoxonase (PON) seems to play a major role in the protection of low density lipoprotein (LDL) against peroxidation by HDL, and the partly purified enzyme exerts a dose-dependent protective effect. A common polymorphism of the human gene (192 Q
In summary, these results suggest that the protein bearing both paraoxonase and arylesterase activities also possesses a third thermostable property, closely associated with paraoxon hydrolysis activity and unaffected by PON genetic variability.—Cao, H., A. Girard-Globa, F. Berthezene, and P. Moulin. Paraoxonase protection of LDL against peroxidation is independent of its esterase activity towards paraoxon and is unaffected by the Q
Supplementary key words:
paraoxonase, HDL, LDL, peroxidation, atherosclerosis
Copyright © 1999 by Lipid Research, Inc.
Original Article
Paraoxonase protection of LDL against peroxidation is independent of its esterase activity towards paraoxon and is unaffected by the Q
Huibi Caoa,
Anik Girard-Globaa,b,
Francois Berthezenec, and
Philippe Moulina,c
R genetic polymorphism
a Laboratoire de Métabolisme des Lipides, Université Lyon 1, Hôpital de l'Antiquaille, F-69005 Lyon
b CNRS-UPRESA 5014, Université Lyon 1, Faculté de Médecine et de Pharmacie, F-69007 Lyon
c Department of Endocrinology and Metabolic Diseases, Hôpital de l'Antiquaille, F-69005 Lyon, France
R) modulates paraoxonase activity but purified enzyme from either genotype is equally effective against LDL peroxidation. The inhibition of Cu2+-induced LDL peroxidation by HDL was monitored by lipid peroxide assay and change in LDL electrophoretic mobility. We show that HDL from type 2 diabetic patients with the QQ or RR genotype (n = 12 for each) reduce, to the same extent, both peroxide production (by 60.6 ± 20.0 and 63.9 ± 23.5%) and relative change in mobility (61.3 ± 21.8 and 61.4 ± 26.5%) despite a 6-fold difference in paraoxonase activity (47.4 ± 4.4 vs. 299.7 ± 23.7 U/l, P < 0.0001). Protection was, however, related to paraoxonase activity, but with a different efficiency in each group corresponding to a better protection per unit of enzyme in the QQ genotype group. Inactivation of PON activity by heating (56°C, 10 min) or by EDTA was totally without effect on protection, which remained correlated with the paraoxonase activity measured prior to inactivation. R genetic polymorphism. J. Lipid Res. 1999. 40: 133–139. 
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