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Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress

Philasterides dicentrarchi is a free-living microaerophilic scuticociliate that can become a facultative parasite and cause a serious parasitic disease in farmed fish. Both the free-living and parasitic forms of this scuticociliate are exposed to oxidative stress associated with environmental factor...

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Autores principales: Folgueira, Iria, Lamas, Jesús, de Felipe, Ana Paula, Sueiro, Rosa Ana, Leiro, José Manuel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6746850/
https://www.ncbi.nlm.nih.gov/pubmed/31527617
http://dx.doi.org/10.1038/s41598-019-49750-5
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author Folgueira, Iria
Lamas, Jesús
de Felipe, Ana Paula
Sueiro, Rosa Ana
Leiro, José Manuel
author_facet Folgueira, Iria
Lamas, Jesús
de Felipe, Ana Paula
Sueiro, Rosa Ana
Leiro, José Manuel
author_sort Folgueira, Iria
collection PubMed
description Philasterides dicentrarchi is a free-living microaerophilic scuticociliate that can become a facultative parasite and cause a serious parasitic disease in farmed fish. Both the free-living and parasitic forms of this scuticociliate are exposed to oxidative stress associated with environmental factors and the host immune system. The reactive oxygen species (ROS) generated by the host are neutralized by the ciliate by means of antioxidant defences. In this study we aimed to identify metalloenzymes with superoxide dismutase (SOD) activity capable of inactivating the superoxide anion (•O(2)(−)) generated during induction of oxidative stress. P. dicentrarchi possesses the three characteristic types of SOD isoenzymes in eukaryotes: copper/zinc-SOD, manganese-SOD and iron-SOD. The Cu/Zn-SOD isoenzymes comprise three types of homodimeric proteins (CSD1-3) of molecular weight (MW) 34–44 kDa and with very different AA sequences. All Cu/Zn-SODs are sensitive to NaCN, located in the cytosol and in the alveolar sacs, and one of them (CSD2) is extracellular. Mn- and Fe-SOD transcripts encode homodimeric proteins (MSD and FSD, respectively) in their native state: a) MSD (MW 50 kDa) is insensitive to H(2)O(2) and NaN(3) and is located in the mitochondria; and b) FSD (MW 60 kDa) is sensitive to H(2)O(2), NaN(3) and the polyphenol trans-resveratrol and is located extracellularly. Expression of SOD isoenzymes increases when •O(2)(−) is induced by ultraviolet (UV) irradiation, and the increase is proportional to the dose of energy applied, indicating that these enzymes are actively involved in cellular protection against oxidative stress.
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spelling pubmed-67468502019-09-27 Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress Folgueira, Iria Lamas, Jesús de Felipe, Ana Paula Sueiro, Rosa Ana Leiro, José Manuel Sci Rep Article Philasterides dicentrarchi is a free-living microaerophilic scuticociliate that can become a facultative parasite and cause a serious parasitic disease in farmed fish. Both the free-living and parasitic forms of this scuticociliate are exposed to oxidative stress associated with environmental factors and the host immune system. The reactive oxygen species (ROS) generated by the host are neutralized by the ciliate by means of antioxidant defences. In this study we aimed to identify metalloenzymes with superoxide dismutase (SOD) activity capable of inactivating the superoxide anion (•O(2)(−)) generated during induction of oxidative stress. P. dicentrarchi possesses the three characteristic types of SOD isoenzymes in eukaryotes: copper/zinc-SOD, manganese-SOD and iron-SOD. The Cu/Zn-SOD isoenzymes comprise three types of homodimeric proteins (CSD1-3) of molecular weight (MW) 34–44 kDa and with very different AA sequences. All Cu/Zn-SODs are sensitive to NaCN, located in the cytosol and in the alveolar sacs, and one of them (CSD2) is extracellular. Mn- and Fe-SOD transcripts encode homodimeric proteins (MSD and FSD, respectively) in their native state: a) MSD (MW 50 kDa) is insensitive to H(2)O(2) and NaN(3) and is located in the mitochondria; and b) FSD (MW 60 kDa) is sensitive to H(2)O(2), NaN(3) and the polyphenol trans-resveratrol and is located extracellularly. Expression of SOD isoenzymes increases when •O(2)(−) is induced by ultraviolet (UV) irradiation, and the increase is proportional to the dose of energy applied, indicating that these enzymes are actively involved in cellular protection against oxidative stress. Nature Publishing Group UK 2019-09-16 /pmc/articles/PMC6746850/ /pubmed/31527617 http://dx.doi.org/10.1038/s41598-019-49750-5 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Folgueira, Iria
Lamas, Jesús
de Felipe, Ana Paula
Sueiro, Rosa Ana
Leiro, José Manuel
Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress
title Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress
title_full Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress
title_fullStr Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress
title_full_unstemmed Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress
title_short Identification and Molecular Characterization of Superoxide Dismutases Isolated From A Scuticociliate Parasite: Physiological Role in Oxidative Stress
title_sort identification and molecular characterization of superoxide dismutases isolated from a scuticociliate parasite: physiological role in oxidative stress
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6746850/
https://www.ncbi.nlm.nih.gov/pubmed/31527617
http://dx.doi.org/10.1038/s41598-019-49750-5
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