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Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals

Glutathione transferases (GSTs) are enzymes devoted to the protection of cells against many different toxins. In erythrocytes, the isoenzyme (e-GST) mainly present is GSTP1-1, which is overexpressed in humans in case of increased blood toxicity, as it occurs in nephrophatic patients or in healthy su...

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Autores principales: Bocedi, A, Fabrini, R, Lai, O, Alfieri, L, Roncoroni, C, Noce, A, Pedersen, JZ, Ricci, G
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4979413/
https://www.ncbi.nlm.nih.gov/pubmed/27551520
http://dx.doi.org/10.1038/cddiscovery.2016.29
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author Bocedi, A
Fabrini, R
Lai, O
Alfieri, L
Roncoroni, C
Noce, A
Pedersen, JZ
Ricci, G
author_facet Bocedi, A
Fabrini, R
Lai, O
Alfieri, L
Roncoroni, C
Noce, A
Pedersen, JZ
Ricci, G
author_sort Bocedi, A
collection PubMed
description Glutathione transferases (GSTs) are enzymes devoted to the protection of cells against many different toxins. In erythrocytes, the isoenzyme (e-GST) mainly present is GSTP1-1, which is overexpressed in humans in case of increased blood toxicity, as it occurs in nephrophatic patients or in healthy subjects living in polluted areas. The present study explores the possibility that e-GST may be used as an innovative and highly sensitive biomarker of blood toxicity also for other mammals. All distinct e-GSTs from humans, Bos taurus (cow), Sus scrofa (pig), Capra hircus (goat), Equus caballus (horse), Equus asinus (donkey) and Ovis aries (sheep), show very similar amino acid sequences, identical kinetics and stability properties. Reference values for e-GST in all these mammals reared in controlled farms span from 3.5±0.2 U/g(Hb) in the pig to 17.0±0.9 U/g(Hb) in goat; such activity levels can easily be determined with high precision using only a few microliters of whole blood and a simple spectrophotometric assay. Possibly disturbing factors have been examined to avoid artifact determinations. This study provides the basis for future screening studies to verify if animals have been exposed to toxicologic insults. Preliminary data on cows reared in polluted areas show increased expression of e-GST, which parallels the results found for humans.
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spelling pubmed-49794132016-08-22 Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals Bocedi, A Fabrini, R Lai, O Alfieri, L Roncoroni, C Noce, A Pedersen, JZ Ricci, G Cell Death Discov Article Glutathione transferases (GSTs) are enzymes devoted to the protection of cells against many different toxins. In erythrocytes, the isoenzyme (e-GST) mainly present is GSTP1-1, which is overexpressed in humans in case of increased blood toxicity, as it occurs in nephrophatic patients or in healthy subjects living in polluted areas. The present study explores the possibility that e-GST may be used as an innovative and highly sensitive biomarker of blood toxicity also for other mammals. All distinct e-GSTs from humans, Bos taurus (cow), Sus scrofa (pig), Capra hircus (goat), Equus caballus (horse), Equus asinus (donkey) and Ovis aries (sheep), show very similar amino acid sequences, identical kinetics and stability properties. Reference values for e-GST in all these mammals reared in controlled farms span from 3.5±0.2 U/g(Hb) in the pig to 17.0±0.9 U/g(Hb) in goat; such activity levels can easily be determined with high precision using only a few microliters of whole blood and a simple spectrophotometric assay. Possibly disturbing factors have been examined to avoid artifact determinations. This study provides the basis for future screening studies to verify if animals have been exposed to toxicologic insults. Preliminary data on cows reared in polluted areas show increased expression of e-GST, which parallels the results found for humans. Nature Publishing Group 2016-05-23 /pmc/articles/PMC4979413/ /pubmed/27551520 http://dx.doi.org/10.1038/cddiscovery.2016.29 Text en Copyright © 2016 Cell Death Differentiation Association http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Bocedi, A
Fabrini, R
Lai, O
Alfieri, L
Roncoroni, C
Noce, A
Pedersen, JZ
Ricci, G
Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals
title Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals
title_full Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals
title_fullStr Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals
title_full_unstemmed Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals
title_short Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals
title_sort erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4979413/
https://www.ncbi.nlm.nih.gov/pubmed/27551520
http://dx.doi.org/10.1038/cddiscovery.2016.29
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