Postprandial Paraoxonase 1 Activity Following Consumption of Recommended Amounts of Mixed Meals in Healthy Males

Abstract

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. J Atheroscler Thromb, 2016; 23: 225-232.

Effects of Cardiac Rehabilitation on High-Density Lipoprotein-mediated Cholesterol Efflux Capacity and Paraoxonase-1 Activity in Patients with Acute Coronary Syndrome

“…In contrast to the previous report 41 ) , the present study failed to show an association between AREA and MDA-LDL as surrogate marker for oxidative stress, while AREA at baseline was significantly inversely associated with hsCRP. Furthermore, Kameyama et al reported that postprandial increases in AREA and postprandial decreases in PON-1 lactonase activities in healthy men 43 ) . The baseline blood samples were collected at non-fasting state on admission in 92% of patients, and AREAs at baseline in these patients were slightly higher compared with the AREA in fasting state at the beginning of the CR (756.2 ± 170.2 vs 727.4 ± 129.0, respectively).…”

Serum paraoxonase activity in familial hypercholesterolaemia

“…While PON1 is a promiscuous enzyme, displaying esterase and lactonase activities, the current assay of its activity frequently takes advantage of the former; namely, phenylacetate is used, in which case PON1 activity is expressed as arylesterase activity [1]. On the other hand, much attention has recently been paid to lactones as physiologically relevant substrates that are still under investigation [1,2].…”

“…In fasted blood samples, the levels of lipids, such as cholesterol and triglycerides, were enzymatically determined. Serum PON1 arylesterase activity was kinetically determined using phenylacetate by recording absorbance changes at 270 nm [2]. Similarly, PON1 lactonase activity was kinetically determined using 5-(thiobutyl) butyrolactone by recording absorbance changes at 405 nm [2].…”

“…Serum PON1 arylesterase activity was kinetically determined using phenylacetate by recording absorbance changes at 270 nm [2]. Similarly, PON1 lactonase activity was kinetically determined using 5-(thiobutyl) butyrolactone by recording absorbance changes at 405 nm [2]. These values were measured with in-house A t-test and χ 2 test were used between the groups, as well as a general linear model analysis for the individual PON1 activities, after adjusting for the age, gender, and HDL cholesterol.…”

“…Of interest, the higher lactonase activity in patients with FH appeared to be the opposite of the results for arylesterase. The paradoxical observations among substrates used for measuring PON1 activities have been noted [2]. It may be due to differences in binding pockets at the active sites of PON1, where esterase activity exploits one pocket, and lactonase activity exploits another [2].…”