Resveratrol affects the expression of glutamate cysteine ligase in the kidneys of aged rats.

Jiangshui Yuan,Weiqing Song,Li Li,Zongliang Zhang

doi:10.3892/etm.2014.1664

Abstract

The aim of the present study was to evaluate the effect that a dietary intake of resveratrol (RSV) had on the expression of glutamate cysteine ligase (GCL) in the kidneys of aged rats. Young, middle-aged and aged rats were each randomly divided into two groups. The control groups were fed a controlled diet and the experimental groups received a controlled diet supplemented with RSV. GCL activity levels in the kidneys were determined. Protein content and relative gene expression levels of the two subunits of GCL were evaluated by western blot analysis and quantitative polymerase chain reaction, respectively. GCL activity levels significantly increased in the kidneys of aged rats fed the RSV-supplemented diet. In addition, RSV markedly increased the protein content and relative mRNA expression levels of the GCL subunits in the kidneys of aged rats. These observations have important implications for the development of therapeutic agents for the kidneys that may enable the elderly population to combat oxidative stress.

Highlights

Glutathione (GSH) is a tripeptide that functions as an antioxidant
In order to understand the increase of glutamate cysteine ligase (GCL) activity levels in the kidneys of aged rats, the protein content of the two subunits of GCL was determined
The results showed that the relative expression levels of GCLM mRNA (Fig. 4A) in kidneys of aged rats (1.55 ± 0.15, P=0.001) fed a diet supplemented with RSV were significantly higher than those in the respective controls; they were markedly increased in young rats (2.13 ± 0.23, P=0.001) fed the RSV‐supplemented diet

Summary

Introduction

Glutathione (GSH) is a tripeptide that functions as an antioxidant. GSH conjugation with oxidants is catalyzed by the enzyme glutathione S‐transferase. GSH‐dependent detoxifying reactions protect cells from oxidative damage, but reduce intracellular GSH levels. The replenishment of GSH is achieved by recycling and biosynthesis [2], which is regulated by substrate availability and the synthesis rate. Intracellular synthesis of GSH occurs by two consecutive adenosine triphosphate (ATP)‐dependent enzymatic reactions. Glutamate is coupled with cysteine to form γ‐glutamylcysteine (γ‐GC). This is catalyzed by glutamate cysteine ligase (GCL), which is the rate‐limiting enzyme of GSH biosynthesis. Γ‐GC is coupled with glycine to form GSH and this is catalyzed by GSH synthetase [2]

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