Oxidative stress (OS) is important in the pathogenesis of atherosclerosis. Paraoxonase-1 (PON1) is an enzyme found in the circulation associated with high-density lipoprotein (HDL). HDL-associated enzyme PON1 has an important role in the attenuation of atherogenic low-density lipoprotein (LDL) oxidation. The aim of this study was to determine PON1 and arylesterase (AREST) enzyme levels in relation to insulin resistance (IR) or obesity among children and adolescents. The study included healthy school children and adolescents. Blood was drawn for the determination of blood glucose, lipid, PON1 and AREST enzyme levels. Overall, we observed a positive correlation between PON1 enzyme activity and high-density lipoprotein cholesterol (HDL-C) levels (r = 0.189, P = 0.014). The correlation appeared to be more significant in boys (r = 0.271, P = 0.009). For subjects with IR and obesity, PON1 enzyme activity did not correlate with HDL-C levels (r = 0.038, P = 0.790), instead PON1 levels correlated negatively with BMI (r = -0.309 and P = 0.026). Multiple linear regression analysis was performed to find the predictors of log PON1 activity. HDL-C level was the strongest predictor of PON1 activity in the lean control group, while BMI appeared to be the strongest predictor in the subjects with obesity or IR. In conclusion, determinants of PON1 enzyme activity are variable in children and adolescents based on IR and obesity. Future studies will shed light on the underlying mechanisms and biomarkers of OS in children and may reveal possible targets for therapeutic intervention.
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http://dx.doi.org/10.1080/ac.69.6.1000011 | DOI Listing |
Biomed Pharmacother
December 2024
Research Division, Mitsubishi Tanabe Pharma Corporation, 1000, Kamoshida-cho, Aoba-ku, Yokohama-shi, Kanagawa 227-0033, Japan. Electronic address:
Vavilovskii Zhurnal Genet Selektsii
November 2024
Institute of Biochemistry and Genetics - Subdivision of the Ufa Federal Research Centre of the Russian Academy of Sciences, Ufa, Russia.
Myocardial infarction (MI) is a multifactorial polygenic disease that develops as a result of a complex interaction of numerous genetic factors and the external environment. Accordingly, the contribution of each of them separately is usually not large and may significantly depend on the state of other accompanying factors. The purpose of the study was to search for informative predictors of MI risk based on polygenic analysis of polymorphic variants of (1) the antioxidant defense enzyme genes PON1 (rs662), PON2 (rs7493), CAT (rs1001179), MSRA (rs10098474) and GSTP1 (rs1695); (2) the apoptosis genes CASP8 (rs3834129), TP53 (rs1042522) and BCL2 (rs12454712); and (3) the inflammation genes CRP (rs1205), CX3CR1 (rs3732378), IL6 (rs1800795) and CCL2 (rs1024611).
View Article and Find Full Text PDFCurr Protein Pept Sci
December 2024
Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar (Mohali)- 160062, Punjab, India.
Human paraoxonase 1 (hPON1) is a Ca2+-dependent metalloenzyme with multifunctional properties. Due to its diverse roles as arylesterase, phosphotriesterase, and lactonase, it plays a significant role in disease conditions. Researchers across the globe have demonstrated different properties of PON1, like anti-oxidant, anti-inflammatory, anti-atherogenic, anti-diabetic, and OPneutralization.
View Article and Find Full Text PDFHum Exp Toxicol
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Department of Respiration, The 80th Group Army Hospital of People's Liberation Army, Weifang, China.
Objective: Sulfur mustard (SM) is an important chemical warfare agent. The mechanisms underlying SM toxicity have not been completely elucidated. However, oxidative stress and the subsequent damage to macromolecules have been considered ascrucial steps in SM toxicity.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Department of Pharmaceutical Biochemistry, Wroclaw Medical University, Borowska 211A St., 50-556 Wroclaw, Poland.
PON1 is a Ca-dependent enzyme that indicates a hydrolytic activity towards a broad spectrum of substrates. The mechanism of hydrolysis catalyzed by this enzyme is poorly understood. It was shown that the active site of PON1 is highly dynamic.
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