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Aim: Postprandial lipid level increases induce oxidative stress, which is involved in atherogenesis. The antioxidant properties of paraoxonase 1 (PON1) have attracted attention. However, changes in postprandial PON1 levels differ across prior studies, and changes in PON1 lactonase activity, potentially relevant to PON1 physiology, after the consumption of ordinary meals are unknown. Herein we evaluated postprandial serum lipid levels and PON1 changes following mixed-meal consumption of the amounts recommended for ordinary meals.
Methods: Nine healthy male volunteers consumed three different meals in a randomized cross-over design. The test meals were as follows: S, white rice; SMF, S with fat-containing protein-rich main dishes; and SMFV: SMF with vegetable dishes. The serum lipid concentrations and PON1 lactonase and arylesterase activities were determined during a three-hour period after the consumption of these meals.
Results: The postprandial triglyceride levels were higher after consuming the SMF and SMFV meals than after consuming the S meal. Despite postprandial high-density lipoprotein cholesterol being unchanged, PON1 lactonase activity was decreased, while PON1 arylesterase activity was increased in the postprandial state after all test meals. Postprandial changes in lactonase and arylesterase activities did not differ among the test meals.
Conclusions: Inverse changes in PON1 lactonase and arylesterase activities were observed after consuming recommended ordinary meals. This observation provides useful information for choosing PON1 species as postprandial markers.
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http://dx.doi.org/10.5551/jat.30585 | DOI Listing |
Int J Mol Sci
August 2025
Laboratorio de Contaminación y Toxicología Ambiental, Secretaría de Investigación y Posgrado, Universidad Autónoma de Nayarit, Tepic 63000, Nayarit, Mexico.
Paraoxonase 1 (PON1) is an antioxidant enzyme that plays physio-pathological roles. Prior in silico analysis revealed the presence of response elements of the nuclear receptor superfamily in the promoter, comparable to glucocorticoid receptors (GR), the vitamin D receptor (VDR), and the pregnenolone X receptor (PXR). The aim of this study was to evaluate the effects of 1α,25-dihydroxyvitamin D, a ligand specific to VDR, on the expression and activity of PON1 in hepatocarcinoma cells (HepG2 cells).
View Article and Find Full Text PDFChem Biol Interact
October 2025
University of Ljubljana, Faculty of Medicine, Institute of Biochemistry and Molecular Genetics, Vrazov trg 2, 1000, Ljubljana, Slovenia. Electronic address:
Paraoxonase 1 (PON1) is a metalloenzyme that requires calcium ions at both catalytic and structural binding sites to hydrolyze the substrates. The enzyme is efficiently inhibited by several metal ions, especially transition metals, which tend to bind non-specifically to oxygen, nitrogen, and sulfur ligands of amino acid residues on the PON1 surface. In contrast, several lanthanide ions can specifically replace isomorphous Ca ions from many protein binding sites, making them among the most potent metal inhibitors of PON1.
View Article and Find Full Text PDFClin Exp Rheumatol
July 2025
Division of Rheumatology, University of California Los Angeles, David Geffen School of Medicine, Los Angeles, CA, USA.
Objectives: To identify predictors of thrombotic events in patients with idiopathic inflammatory myopathies (IIM).
Methods: We conducted a retrospective study of a large, longitudinal IIM cohort followed at a single academic centre. We used Poisson regression models to estimate incidence-rate ratios (IRR) of prospective arterial and venous thrombotic events (ATE and VTE respectively).
Rep Biochem Mol Biol
October 2024
University of Baghdad, College of Science, Department of Chemistry, Baghdad, Iraq.
Background: Type 1 diabetes mellitus (T1DM) is a chronic autoimmune condition that can lead to long-term complications due to oxidative stress and metabolic dysregulation. Paraoxonase-1 (PON-1), an enzyme associated with high-density lipoprotein (HDL), has dual activities: arylesterase and lactonase. These activities protect lipids from oxidative damage.
View Article and Find Full Text PDFArthritis Res Ther
March 2025
UCLA David Geffen School of Medicine, Departmen of Medicine, Division of Rheumatology, University of California, 1000 Veteran Ave, Rm 32-59, Los Angeles, CA, 90095, USA.
Objective: To evaluate circulating levels of intercellular cell adhesion molecule-1 (ICAM-1), vascular cell adhesion molecule-1 (VCAM-1) in patients with dermatomyositis (DM) and DM associated interstitial lung disease (DM-ILD).
Methods: We performed a cross-sectional study in plasma samples from DM patients and matched healthy controls. Plasma ICAM-1 and VCAM-1 (CAM) levels were measured by ELISA.