Ellagic acid and its methyl-derivatives inhibit a newly found nitratase activity

被引：0

作者：

Leger, Claude L. ^{[1
]}

Torres-Rasgado, Enrique ^{[1
]}

Fouret, Gilles ^{[1
]}

Lauret, Celine ^{[1
]}

Carbonneau, Marie-Annette ^{[1
]}

机构：

[1] Univ Montpellier I, EA Nutr Humaine & Atherogenese 2993, F-34000 Montpellier, France

来源：

FUNDAMENTAL & CLINICAL PHARMACOLOGY | 2010年 / 24卷 / 01期

关键词：

albumin; denitrating activity; low density lipoprotein; nitratase; peroxynitrite; polyphenol; ALBUMIN; PLASMA; L; EXTRACT; CELLS;

D O I：

10.1111/j.1472-8206.2009.00734.x

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

We have recently shown that low density lipoprotein (LDL) was able to denitrate albumin-bound 3-NO2-Tyr residues and to concomitantly release NO3- through a Ca2+-dependent process that has been ascribed to a specific protein structure. A lipophilic food component (gamma-tocopherol), which is easily loaded into LDL has been found to totally inhibit denitrating activity. We presently found that ellagic acid (EA) and its methylated derivatives, 4,4'O-methyl- and 3,3'O-methyl-ellagic acids (MeEA1 and MeEA2, respectively), amphipathic phenolic components of certain fruits and beverages, were also able to inhibit this activity, with a total inhibition for EA and a 60% inhibition for MeEA1 and MeEA2. EA exhibited the highest affinity for protein plasma, whereas a higher affinity of MeEA1 and MeEA2 (with MeEA1 > MeEA2) than EA was found for lipoprotein fractions, suggesting that the inhibition-driving property is protein affinity. As a result of this nitratase-inhibition property EA and its natural metabolite MeEA2 may have a beneficial role in special physiopathological conditions.

引用

页码：115 / 119

页数：5

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