Atorvastatin preferentially reduces LDL-associated platelet-activating factor acetylhydrolase activity in dyslipidemias of type IIA and type IIB
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Date
Authors
Tsimihodimos, V.
Karabina, S. A. P.
Tambaki, A. P.
Bairaktari, E.
Goudevenos, J. A.
Chapman, M. J.
Elisaf, M.
Tselepis, A. D.
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American Heart Association, Inc.
Abstract
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peer reviewed
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Arteriosclerosis Thrombosis and Vascular Biology
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Description
Human plasma platelet-activating factor acetylhydrolase (PAF-AH) is a phospholipase A(2) that is primarily associated with low density lipoprotein (LDL). PAF-AH activity has also been found in high density lipoprotein (HDL), although it has recently been indicated that there is no PAF-AH protein in HDL. Plasma paraoxonase 1 (PON1) is an HDL-associated esterase, which also exhibits PAF-AH-like activity. The effect of atorvastatin (20 mg per day for 4 months) on PAF-AH and PON1 activities in patients with dyslipidemia of type IIA (n=55) or type IIB (n=21) was studied. In both patient groups, atorvastatin significantly reduced plasma PAF-AH activity because of the decrease in LDL plasma levels and the preferential decrease in PAF-AH activity on dense LDL subfractions (LDL-4 and LDL-5). Drug therapy did not affect HDL-associated PAF-AH activity or serum PON1 activities toward paraoxon and phenylacetate in either patient group. However, because of the reduction in LDL cholesterol levels, the ratios of HDL-associated PAF-AH and serum PON1 activities to LDL cholesterol levels were significantly increased after drug administration. The reduction of the LDL-associated PAF-AH activity and the elevation in the ratios of HDL-associated PAF-AH and PON1 activities to LDL plasma levels may represent a new dimension in the antiatherogenic effect of atorvastatin.
Description
Keywords
hyperlipidemia, monocytes/macrophages, platelet-activating factor acetylhydrolase, paraoxonase, atorvastatin, low-density-lipoprotein, dependent diabetes-mellitus, human-plasma, familial hypercholesterolemia, paraoxonase activity, paf-acetylhydrolase, phospholipase a(2), coronary heart, oxidation, therapy
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<Go to ISI>://000173786600017
http://atvb.ahajournals.org/content/22/2/306.full.pdf
http://atvb.ahajournals.org/content/22/2/306.full.pdf
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en
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Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας