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Papers In Press, published online ahead of print March 1, 2003
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Department of Chemistry, University of Ioannina, Ioannina 45110
Corresponding Author: atselep{at}cc.uoi.gr
Human plasma Platelet Activating Factor Acetylhydrolase (PAF-AH) is an enzyme associated mainly with the apolipoprotein B-containing lipoproteins and primarily with LDL. A small proportion of enzymatic activity is also associated with HDL. Plasma paraoxonase 1 (PON1) is an esterase exclusively associated with HDL. The effect of fenofibrate on PAF-AH and PON1 activities in patients with dyslipidemias of type IIA, IIB and IV was studied. Fenofibrate reduced plasma PAF-AH activity in all patient groups. In type IIA patients it was mainly due to a fall in enzyme activity associated with the dense LDL subspecies, whereas in types IIB and IV patients, this reduction was due to the decrease in PAF-AH activity associated with both the VLDL+IDL and dense LDL subspecies. Drug therapy in type IIB and type IV patients significantly increased the HDL-associated PAF-AH activity due to the induction in enzyme activity associated with the HDL3c subfraction. Fenofibrate did not affect serum PON1 activities towards paraoxon and phenylacetate in either patient group. The fenofibrate-induced elevation of HDL-associated PAF-AH activity in dyslipidemic patients of type IIB and type IV as well as the reduction in enzyme activity associated with atherogenic apoB-containing lipoproteins in all patient groups, may represent a new and important anti-atherogenic effect of this potent lipid-modulating agent.
Revised on February 21, 2003
Accepted on February 24, 2003
Fenofibrate induces HDL-associated PAF-acetylhydrolase but attenuates enzyme activity associated with apoB-containing lipoproteins
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