Elevation of Glucose 6-Phosphate Dehydrogenase Activity Induced by Amplified Insulin Response in Low Glutathione Levels in Rat Liver

Weanling male Wistar rats were fed on a 10% soybean protein isolate (SPI) diet for 3 weeks with or without supplementing 0.3% sulfur-containing amino acids (SAA; methionine or cystine) to examine relationship between glutathione (GSH) levels and activities of NADPH-producing enzymes, glucose 6-phosp...

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Main Authors: Misako Taniguchi, Nobuko Mori, Chizuru Iramina, Akira Yasutake
Format: Article
Language:English
Published: Wiley 2016-01-01
Series:The Scientific World Journal
Online Access:http://dx.doi.org/10.1155/2016/6382467
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author Misako Taniguchi
Nobuko Mori
Chizuru Iramina
Akira Yasutake
author_facet Misako Taniguchi
Nobuko Mori
Chizuru Iramina
Akira Yasutake
author_sort Misako Taniguchi
collection DOAJ
description Weanling male Wistar rats were fed on a 10% soybean protein isolate (SPI) diet for 3 weeks with or without supplementing 0.3% sulfur-containing amino acids (SAA; methionine or cystine) to examine relationship between glutathione (GSH) levels and activities of NADPH-producing enzymes, glucose 6-phosphate dehydrogenase (G6PD) and malic enzyme (ME), in the liver. Of rats on the 10% SPI diet, GSH levels were lower and the enzyme activities were higher than of those fed on an SAA-supplemented diet. Despite the lower GSH level, γ-glutamylcysteine synthetase (γ-GCS) activity was higher in the 10% SPI group than other groups. Examination of mRNAs of G6PD and ME suggested that the GSH-suppressing effect on enzyme induction occurred prior to and/or at transcriptional levels. Gel electrophoresis of G6PD indicated that low GSH status caused a decrease in reduced form and an increase in oxidized form of the enzyme, suggesting an accelerated turnover rate of the enzyme. In primary cultured hepatocytes, insulin response to induce G6PD activity was augmented in low GSH levels manipulated in the presence of buthionine sulfoximine. These findings indicated that elevation of the G6PD activity in low GSH levels was caused by amplified insulin response for expression of the enzyme and accelerated turnover rate of the enzyme molecule.
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institution Kabale University
issn 2356-6140
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publisher Wiley
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series The Scientific World Journal
spelling doaj-art-b348edb3828a4159ab120158699638da2025-02-03T05:59:14ZengWileyThe Scientific World Journal2356-61401537-744X2016-01-01201610.1155/2016/63824676382467Elevation of Glucose 6-Phosphate Dehydrogenase Activity Induced by Amplified Insulin Response in Low Glutathione Levels in Rat LiverMisako Taniguchi0Nobuko Mori1Chizuru Iramina2Akira Yasutake3Department of Nutrition Sciences, Nakamura Gakuen University, Fukuoka 814-0198, JapanDepartment of Biomedical Laboratory Sciences, Faculty of Life Sciences, Kumamoto University, 4-24-1 Kuhonji, Kumamoto 862-0976, JapanDepartment of Nutrition Sciences, Nakamura Gakuen University, Fukuoka 814-0198, JapanKumamoto University Graduate School of Science and Technology, 2-39-1 Kurokami, Kumamoto 860-8555, JapanWeanling male Wistar rats were fed on a 10% soybean protein isolate (SPI) diet for 3 weeks with or without supplementing 0.3% sulfur-containing amino acids (SAA; methionine or cystine) to examine relationship between glutathione (GSH) levels and activities of NADPH-producing enzymes, glucose 6-phosphate dehydrogenase (G6PD) and malic enzyme (ME), in the liver. Of rats on the 10% SPI diet, GSH levels were lower and the enzyme activities were higher than of those fed on an SAA-supplemented diet. Despite the lower GSH level, γ-glutamylcysteine synthetase (γ-GCS) activity was higher in the 10% SPI group than other groups. Examination of mRNAs of G6PD and ME suggested that the GSH-suppressing effect on enzyme induction occurred prior to and/or at transcriptional levels. Gel electrophoresis of G6PD indicated that low GSH status caused a decrease in reduced form and an increase in oxidized form of the enzyme, suggesting an accelerated turnover rate of the enzyme. In primary cultured hepatocytes, insulin response to induce G6PD activity was augmented in low GSH levels manipulated in the presence of buthionine sulfoximine. These findings indicated that elevation of the G6PD activity in low GSH levels was caused by amplified insulin response for expression of the enzyme and accelerated turnover rate of the enzyme molecule.http://dx.doi.org/10.1155/2016/6382467
spellingShingle Misako Taniguchi
Nobuko Mori
Chizuru Iramina
Akira Yasutake
Elevation of Glucose 6-Phosphate Dehydrogenase Activity Induced by Amplified Insulin Response in Low Glutathione Levels in Rat Liver
The Scientific World Journal
title Elevation of Glucose 6-Phosphate Dehydrogenase Activity Induced by Amplified Insulin Response in Low Glutathione Levels in Rat Liver
title_full Elevation of Glucose 6-Phosphate Dehydrogenase Activity Induced by Amplified Insulin Response in Low Glutathione Levels in Rat Liver
title_fullStr Elevation of Glucose 6-Phosphate Dehydrogenase Activity Induced by Amplified Insulin Response in Low Glutathione Levels in Rat Liver
title_full_unstemmed Elevation of Glucose 6-Phosphate Dehydrogenase Activity Induced by Amplified Insulin Response in Low Glutathione Levels in Rat Liver
title_short Elevation of Glucose 6-Phosphate Dehydrogenase Activity Induced by Amplified Insulin Response in Low Glutathione Levels in Rat Liver
title_sort elevation of glucose 6 phosphate dehydrogenase activity induced by amplified insulin response in low glutathione levels in rat liver
url http://dx.doi.org/10.1155/2016/6382467
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AT nobukomori elevationofglucose6phosphatedehydrogenaseactivityinducedbyamplifiedinsulinresponseinlowglutathionelevelsinratliver
AT chizuruiramina elevationofglucose6phosphatedehydrogenaseactivityinducedbyamplifiedinsulinresponseinlowglutathionelevelsinratliver
AT akirayasutake elevationofglucose6phosphatedehydrogenaseactivityinducedbyamplifiedinsulinresponseinlowglutathionelevelsinratliver