ArticleThe Biochemical journal2001
Hydrolysis of platelet-activating factor by human serum paraoxonase.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
25 citing papers in PubMed, 138 citations in OpenAlex.
- Antioxidant Role of High-Density Lipoprotein.Antioxidants (Basel, Switzerland) · 2026Article
- How Does HDL Participate in Atherogenesis? Antioxidant Activity Versus Role in Reverse Cholesterol Transport.Antioxidants (Basel, Switzerland) · 2025Review
- The Molecular Bases of Anti-Oxidative and Anti-Inflammatory Properties of Paraoxonase 1.Antioxidants (Basel, Switzerland) · 2024Review
- Associations between healthy food groups and platelet-activating factor, lipoprotein-associated phospholipase AEuropean journal of nutrition · 2024Article
- Paraoxonase 1 and atherosclerosis.Frontiers in cardiovascular medicine · 2023Review
- Synthesis of ether lipids: natural compounds and analogues.Beilstein journal of organic chemistry · 2023Review
- Alterations of HDL's to piHDL's Proteome in Patients with Chronic Inflammatory Diseases, and HDL-Targeted Therapies.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Review
- HDL and Oxidation.Advances in experimental medicine and biology · 2022Article
- Decreases in Paraoxonase-1 Activities Promote a Pro-inflammatory Effect of Lipids Peroxidation Products in Non-smoking and Smoking Patients with Acute Pancreatitis.International journal of medical sciences · 2018Article
- Antioxidative activity of high-density lipoprotein (HDL): Mechanistic insights into potential clinical benefit.BBA clinical · 2017Review
- Antioxidant properties of HDL.Frontiers in pharmacology · 2015Review
- To hydrolyze or not to hydrolyze: the dilemma of platelet-activating factor acetylhydrolase.Journal of lipid research · 2014Review
- Lipid oxidation in carriers of lecithin:cholesterol acyltransferase gene mutations.Arteriosclerosis, thrombosis, and vascular biology · 2012Article
- Expression of human paraoxonase 1 decreases superoxide levels and alters bacterial colonization in the gut of Drosophila melanogaster.PloS one · 2012Article
- High Density Lipoprotein and it's Dysfunction.The open biochemistry journal · 2012Article
- Sequence identification, chromosomal mapping and tissue specific expression of the porcine paraoxonase 1 (PON1) gene.Molecular biology reports · 2010Article
- Paraoxonase: Its antiatherogenic role in chronic renal failure.Indian journal of nephrology · 2010Article
- Dramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes.Biochemistry · 2009Article
- Paraoxonase gene variants are associated with autism in North America, but not in Italy: possible regional specificity in gene-environment interactions.Molecular psychiatry · 2005Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human serum paraoxonase (human PON1) has been shown to be important in the metabolism of phospholipid and cholesteryl ester hydroperoxides, thereby preventing the oxidation of low-density lipoprotein (LDL) and retarding atherogenesis. However, the exact substrate specificity of PON1 has not been established. In the present study we show that purified PON1 hydrolyses platelet-activating factor (PAF). We could find no evidence for contamination of our preparation with authentic platelet-activating-factor acetylhydrolase (PAFAH) by immunoblotting with a PAFAH monoclonal antibody or by sequencing the purified protein. In addition the specific PAFAH inhibitor SB-222657 did not affect the ability of PON1 to hydrolyse PAF (30.1+/-2.8 micromol/min per mg of protein with no inhibitor; 31.4+/-2.2 micromol/min per mg of protein with 100 nM inhibitor) or phenyl acetate (242.6+/-30.8 versus 240.8+/-31.5 micromol/min per mg of protein with and without inhibitor respectively). SB-222657 was also unable to inhibit PAF hydrolysis by isolated human high-density lipoprotein (HDL), but completely abolished the activity of human LDL. Ostrich (Struthio camelus) HDL, which does not contain PON1, was unable to hydrolyse PAF. These data provide evidence that PON1 may limit the action of this bioactive pro-inflammatory phospholipid.
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