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Plasma Albumin Redox State Is Responsive to the Amino Acid Balance of Dietary Proteins in Rats Fed a Low Protein Diet

We recently reported that plasma albumin redox state, which correlates with albumin synthesis rate, could be associated with the quality of dietary protein. Aiming to elucidate the association between them, plasma albumin redox state was investigated in rats fed various kinds of AIN-93G-based low pr...

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Autores principales: Wada, Yasuaki, Xijier, Seto, Namiko, Komatsu, Yosuke, Tsuda, Muneya, Kitamura, Yohei, Izumi, Hirohisa, Shimizu, Takashi, Takeda, Yasuhiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6385526/
https://www.ncbi.nlm.nih.gov/pubmed/30828577
http://dx.doi.org/10.3389/fnut.2019.00012
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author Wada, Yasuaki
Xijier,
Seto, Namiko
Komatsu, Yosuke
Tsuda, Muneya
Kitamura, Yohei
Izumi, Hirohisa
Shimizu, Takashi
Takeda, Yasuhiro
author_facet Wada, Yasuaki
Xijier,
Seto, Namiko
Komatsu, Yosuke
Tsuda, Muneya
Kitamura, Yohei
Izumi, Hirohisa
Shimizu, Takashi
Takeda, Yasuhiro
author_sort Wada, Yasuaki
collection PubMed
description We recently reported that plasma albumin redox state, which correlates with albumin synthesis rate, could be associated with the quality of dietary protein. Aiming to elucidate the association between them, plasma albumin redox state was investigated in rats fed various kinds of AIN-93G-based low protein diets. Plasma albumin redox state was shifted to a more oxidized state in rats fed 3% casein (CN) diet than those fed 3% whey protein or 3% wheat gluten diet, while supplementing 3% CN diet with cystine reversed it to a more reduced state, indicating that cystine would complement the shortage of cysteine in CN, thereby increasing albumin synthesis rate. Supplementation with glutathione, a cysteine-containing antioxidative tripeptide, normalized hepatic glutathione redox state modulated by ingestion of 3% CN diet, but it only reversed the oxidized shift of plasma albumin redox state to an extent similar to cystine alone or the constituting amino acid mixture of glutathione (i.e., glutamic acid, cystine, and glycine), indicating that glutathione would primarily serve as a source of cysteine rather than exert its antioxidative activity. Plasma albumin would thus be influenced by amino acid balance in dietary proteins, and it could be useful as a biomarker that contributes to prevention of protein under-nutriton, caused by not only insufficient protein intake but also ingestion of poor-quality protein.
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spelling pubmed-63855262019-03-01 Plasma Albumin Redox State Is Responsive to the Amino Acid Balance of Dietary Proteins in Rats Fed a Low Protein Diet Wada, Yasuaki Xijier, Seto, Namiko Komatsu, Yosuke Tsuda, Muneya Kitamura, Yohei Izumi, Hirohisa Shimizu, Takashi Takeda, Yasuhiro Front Nutr Nutrition We recently reported that plasma albumin redox state, which correlates with albumin synthesis rate, could be associated with the quality of dietary protein. Aiming to elucidate the association between them, plasma albumin redox state was investigated in rats fed various kinds of AIN-93G-based low protein diets. Plasma albumin redox state was shifted to a more oxidized state in rats fed 3% casein (CN) diet than those fed 3% whey protein or 3% wheat gluten diet, while supplementing 3% CN diet with cystine reversed it to a more reduced state, indicating that cystine would complement the shortage of cysteine in CN, thereby increasing albumin synthesis rate. Supplementation with glutathione, a cysteine-containing antioxidative tripeptide, normalized hepatic glutathione redox state modulated by ingestion of 3% CN diet, but it only reversed the oxidized shift of plasma albumin redox state to an extent similar to cystine alone or the constituting amino acid mixture of glutathione (i.e., glutamic acid, cystine, and glycine), indicating that glutathione would primarily serve as a source of cysteine rather than exert its antioxidative activity. Plasma albumin would thus be influenced by amino acid balance in dietary proteins, and it could be useful as a biomarker that contributes to prevention of protein under-nutriton, caused by not only insufficient protein intake but also ingestion of poor-quality protein. Frontiers Media S.A. 2019-02-15 /pmc/articles/PMC6385526/ /pubmed/30828577 http://dx.doi.org/10.3389/fnut.2019.00012 Text en Copyright © 2019 Wada, Xijier, Seto, Komatsu, Tsuda, Kitamura, Izumi, Shimizu and Takeda. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Nutrition
Wada, Yasuaki
Xijier,
Seto, Namiko
Komatsu, Yosuke
Tsuda, Muneya
Kitamura, Yohei
Izumi, Hirohisa
Shimizu, Takashi
Takeda, Yasuhiro
Plasma Albumin Redox State Is Responsive to the Amino Acid Balance of Dietary Proteins in Rats Fed a Low Protein Diet
title Plasma Albumin Redox State Is Responsive to the Amino Acid Balance of Dietary Proteins in Rats Fed a Low Protein Diet
title_full Plasma Albumin Redox State Is Responsive to the Amino Acid Balance of Dietary Proteins in Rats Fed a Low Protein Diet
title_fullStr Plasma Albumin Redox State Is Responsive to the Amino Acid Balance of Dietary Proteins in Rats Fed a Low Protein Diet
title_full_unstemmed Plasma Albumin Redox State Is Responsive to the Amino Acid Balance of Dietary Proteins in Rats Fed a Low Protein Diet
title_short Plasma Albumin Redox State Is Responsive to the Amino Acid Balance of Dietary Proteins in Rats Fed a Low Protein Diet
title_sort plasma albumin redox state is responsive to the amino acid balance of dietary proteins in rats fed a low protein diet
topic Nutrition
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6385526/
https://www.ncbi.nlm.nih.gov/pubmed/30828577
http://dx.doi.org/10.3389/fnut.2019.00012
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