FEEDING AWAY INFLAMMATION – CONJUGATED LINOLEIC ACIDS DECREASE PANCREATIC PHOSPHOLIPASE A2 ACTIVITY*

EWA STACHOWSKA, VIOLETTA DZIEDZIEJKO, KRZYSZTOF SAFRANOW, KATARZYNA JAKUBOWSKA, MARIA OLSZEWSKA, JOANNA BOBER, DARIUSZ CHLUBEK
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引用次数: 4

Abstract

ABSTRACT

Conjugated linoleic acids (CLAs) are positional and geometric isomers of linoleic acid derived from food, mainly from milk and meat products. CLAs are ligands of peroxisome proliferator-activated gamma receptors. Phospholipases A2 (PLA2) represent a diverse group of enzymes that catalyze the hydrolysis of ester bonds at the sn-2 position of membrane phospholipids and release fatty acids and lysophospholipids. The objective of the study was to answer the question whether the release of linoleic acid by pancreatic PLA2 may change in the CLA-containing environment. In this study, linoleic acid released by pancreatic PLA2 was a substrate for purified lipoxygenase – an enzyme converting it into hydroxylated derivatives including 9- and 13-hydroxyoctadecadienoic acid (9-,13-HODE). In this method, the activity of PLA2 was determined by high-performance liquid chromatography. In vitro incubation of hog PLA2 with CLA contributed to a noticeable fall in the synthesis of HODEs (P = 0.003; Kruskal–Wallis test). The concentration of HODEs decreased by 40.2% (for the cis-9, trans-11 CLA isomer; P = 0.007, Mann–Whitney test, n = 5) and by 27% (for the trans-10, cis-12 CLA isomer; P = 0.007, Mann–Whitney test, n = 5) as compared with the control (enzyme incubated without CLA). The inhibition exerted by cis-9, trans-11 CLA isomer was significantly greater than that by trans-10, cis-12 CLA isomer (P = 0.032, Mann–Whitney test, n = 5).

PRACTICAL APPLICATIONS

This study is an attempt to clarify the response to the question whether some food ingredients such as conjugated linoleic acid (CLA) may be useful as an agent supporting the treatment of gastrointestinal disorders. It was observed under in vitro conditions that CLA isomers inhibited the phosphatidylcholine hydrolysis. By using purified enzymes, CLA was shown to contribute to local reduction of availability of linoleic acid and its metabolites (9- and 13-hydroxyoctadecadienoic acid) through inhibition of phospholipid hydrolysis.

摄入炎症共轭亚油酸会降低胰腺磷脂酶a2活性*
共轭亚油酸(CLAs)是从食品中提取的亚油酸的位置和几何异构体,主要来源于牛奶和肉制品。cla是过氧化物酶体增殖体激活γ受体的配体。磷脂酶A2 (PLA2)代表了一组不同的酶,它们催化膜磷脂sn-2位置的酯键水解并释放脂肪酸和溶血磷脂。该研究的目的是回答胰腺PLA2释放亚油酸是否会在含有cla的环境中改变的问题。在本研究中,胰腺PLA2释放的亚油酸是纯化脂氧合酶的底物,这种酶将亚油酸转化为羟基化衍生物,包括9-和13-羟基十八烯二烯酸(9-,13-HODE)。本方法采用高效液相色谱法测定PLA2的活性。猪PLA2与CLA体外孵育显著降低了HODEs的合成(P = 0.003;克鲁斯卡尔-沃利斯测试)。hode浓度下降了40.2%(顺式-9、反式-11 CLA异构体;P = 0.007, Mann-Whitney检验,n = 5)和27%(对于反式-10,顺式-12 CLA异构体;P = 0.007, Mann-Whitney检验,n = 5)与对照组(不加CLA孵育的酶)比较。顺式-9、反式-11 CLA异构体的抑制作用显著大于反式-10、顺式-12 CLA异构体(P = 0.032, Mann-Whitney检验,n = 5)。本研究试图澄清一些食品成分,如共轭亚油酸(CLA)是否可能作为一种支持治疗胃肠道疾病的药物的问题。在体外条件下观察到CLA异构体对磷脂酰胆碱水解有抑制作用。通过使用纯化酶,CLA可以通过抑制磷脂水解来局部降低亚油酸及其代谢产物(9-和13-羟基十八烯二烯酸)的可用性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Journal of Food Lipids
Journal of Food Lipids 工程技术-食品科技
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