Changes in paraoxonase and apolipoproteins /A I, A II, B, C III, E/ during therapy of combined familial hyperlipidemia by ciprofibrate

Turay, J; Grniaková, V.; J, Válka

doi:10.1016/s0021-9150(99)80092-6

Cited by 10 publications

(11 citation statements)

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“…In accordance with previously published results (27), PON1 activities in dyslipidemic Type IIB or Type IV patient groups were not different from those observed in the control group; neither are they affected by fenofibrate therapy. Considering that, unlike PAF-AH, PON1 is not associated with the apoB-containing lipoproteins, the differential effect of fenofibrate on HDL-PAF-AH versus HDL-PON1 further supports the hypothesis for the PAF-AH transfer from triglyceride-rich apoB-containing lipoproteins to HDL during fenofibrate therapy in dyslipidemic Type IIB or Type IV patients.…”

supporting

confidence: 92%

Fenofibrate induces HDL-associated PAF-AH but attenuates enzyme activity associated with apoB-containing lipoproteins

Tsimihodimos

Kakafika

Tambaki

et al. 2003

Journal of Lipid Research

121

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Human plasma platelet-activating factor acetylhydrolase (PAF-AH) is an enzyme associated mainly with the apolipoprotein B (apoB)-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 Types IIA, IIB, and IV were studied. Fenofibrate reduced plasma PAF-AH activity in all patient groups. In Type IIA patients, this reduction was mainly due to a fall in enzyme activity associated with the dense LDL subspecies, whereas in Type IIB and Type IV patients, it 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 increase in enzyme activity associated with the HDL-3c subfraction. Fenofibrate did not affect serum PON1 activities toward 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 apoBcontaining lipoproteins in all patient groups, may represent a new and important antiatherogenic effect of this potent lipid-modulating agent.

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supporting

confidence: 92%

Fenofibrate induces HDL-associated PAF-AH but attenuates enzyme activity associated with apoB-containing lipoproteins

Tsimihodimos

Kakafika

Tambaki

et al. 2003

Journal of Lipid Research

121

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“…Understandably, most of the interest in pharmacological effects on PON1 activity has thus far been in effects of lipid-lowering drugs. Some of these studies, 38 -40 but not all, [41][42][43] suggest an effect of statins and fibrates in raising PON1 activity. The importance of further work in this area is that dietary or pharmacological interventions which will significantly increase PON1 activity may be discovered.…”

Section: See Page 1329mentioning

confidence: 99%

The Hunt for Nutritional and Pharmacological Modulators of Paraoxonase

Durrington

Mackness

2002

ATVB

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“…A few studies have investigated the effects of some lipid-lowering agents on serum paraoxonase activity [31][32][33][34] . The activity of serum PON1 was found to be increased in coronary patients who took low-dose aspirin (acetyl-salicylic acid) 35 .…”

Section: Discussionmentioning

confidence: 99%

Antidepressant and antipsychotic drugs differentially affect PON1 enzyme activity

Avcıkurt

Sinan

Köçkar

2014

Journal of Enzyme Inhibition and Medicinal Chemistry

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Human serum paraoxonase (PON1, EC 3.1.8.1.) is a high-density lipid (HDL)-associated, calciumdependent enzyme. In this study, the effects of Haloperidol, Fluoxetine hydrochloride, Diazepam and Acepromazine drugs used for the therapy of antidepressant and antipsychotic diseases, on paraoxonase enzyme activity was studied in in vitro inhibition studies on purified human serum PON1. PON1 enzyme was purified from human blood using two-step procedures, namely, ammonium sulfate precipitation and sepharose-4B-l-tyrosine-1-napthylamine hydrophobic interaction chromatography. The overall purification of human serum PON1 was obtained in a activity of 109.29 U/mL and this enzyme was purified 125-fold. The SDSpolyacrylamide gel electrophoresis of the enzyme indicates a single band with an apparent MW of 43 kDa. Inhibition studies indicated that haloperidol and fluoxetine hydrocloride were effective inhibitors on purified human serum PON1 activity with IC 50 of 0.187 and 3.08 mM values, respectively. The kinetics of interaction of haloperidol and fluoxetine hydrocloride with the purified human serum PON1 indicated uncompetitive inhibiton pattern with K i of 4.15 and 0.007 mM, respectively.

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Changes in paraoxonase and apolipoproteins /A I, A II, B, C III, E/ during therapy of combined familial hyperlipidemia by ciprofibrate

Cited by 10 publications

References 0 publications

Fenofibrate induces HDL-associated PAF-AH but attenuates enzyme activity associated with apoB-containing lipoproteins

Fenofibrate induces HDL-associated PAF-AH but attenuates enzyme activity associated with apoB-containing lipoproteins

The Hunt for Nutritional and Pharmacological Modulators of Paraoxonase

Antidepressant and antipsychotic drugs differentially affect PON1 enzyme activity

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