Data from: The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes
The unusual pattern of expression of hemoglobin (Hb) and myoglobin (Mb) among Antarctic notothenioid fishes provides an exceptional model system for assessing the impact of these proteins on oxidative stress. We tested the hypothesis that the lack of oxygen-binding proteins may reduce oxidative stre...
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ftzenodo:oai:zenodo.org:4979865 2024-09-15T17:40:27+00:00 Data from: The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes O'Brien, Kristin M. Crockett, Elizabeth L. Philip, Jacques Oldham, Corey A. Hoffman, Megan Kuhn, Donald E. Barry, Ronald McLaughlin, Jessica 2017-12-12 https://doi.org/10.5061/dryad.5228g unknown Zenodo https://doi.org/10.1242/jeb.162503 https://zenodo.org/communities/dryad https://doi.org/10.5061/dryad.5228g oai:zenodo.org:4979865 info:eu-repo/semantics/openAccess Creative Commons Zero v1.0 Universal https://creativecommons.org/publicdomain/zero/1.0/legalcode Notothenia coriiceps Pseudochaenichthys georgianus Champsocephalus gunnari Chaenocephalus aceratus Antarctic fish hemoglobin myoglobin Gobionotothen gibberifrons Chionodraco rastrospinosus info:eu-repo/semantics/other 2017 ftzenodo https://doi.org/10.5061/dryad.5228g10.1242/jeb.162503 2024-07-27T02:36:20Z The unusual pattern of expression of hemoglobin (Hb) and myoglobin (Mb) among Antarctic notothenioid fishes provides an exceptional model system for assessing the impact of these proteins on oxidative stress. We tested the hypothesis that the lack of oxygen-binding proteins may reduce oxidative stress. Levels and activity of pro-oxidants, small-molecule and enzymatic antioxidants, and levels of oxidized lipids and proteins in liver, oxidative skeletal muscle, and heart ventricle were quantified in five species of notothenioid fishes differing in the expression of Hb and Mb. Levels of ubiquitinated proteins and rates of protein degradation by the 20S proteasome were also quantified. Although levels of oxidized proteins and lipids, ubiquitinated proteins, and antioxidants are higher in red-blooded fishes than in Hb-less icefishes in some tissues, this pattern does not persist across all tissues. Expression of Mb is not associated with oxidative damage in heart ventricle, whereas the activity of citrate synthase and contents of heme are positively correlated with oxidative damage in most tissues. Despite some tissue differences in levels of protein carbonyls among species, rates of degradation by the 20S proteasome are not markedly different, suggesting either alternative pathways for eliminating oxidized proteins or redox tone varies among species. Together, our data indicate that the loss of Hb and Mb does not correspond with a clear pattern of either reduced oxidative defense or oxidative damage. Data Summary JEB O'Brien et al JEXBIO_2017_162503 Funding provided by: National Science Foundation Crossref Funder Registry ID: http://dx.doi.org/10.13039/100000001 Award Number: PLR 1043781 and PLR 1043576 Other/Unknown Material Antarc* Antarctic Zenodo |
institution |
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Zenodo |
op_collection_id |
ftzenodo |
language |
unknown |
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Notothenia coriiceps Pseudochaenichthys georgianus Champsocephalus gunnari Chaenocephalus aceratus Antarctic fish hemoglobin myoglobin Gobionotothen gibberifrons Chionodraco rastrospinosus |
spellingShingle |
Notothenia coriiceps Pseudochaenichthys georgianus Champsocephalus gunnari Chaenocephalus aceratus Antarctic fish hemoglobin myoglobin Gobionotothen gibberifrons Chionodraco rastrospinosus O'Brien, Kristin M. Crockett, Elizabeth L. Philip, Jacques Oldham, Corey A. Hoffman, Megan Kuhn, Donald E. Barry, Ronald McLaughlin, Jessica Data from: The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes |
topic_facet |
Notothenia coriiceps Pseudochaenichthys georgianus Champsocephalus gunnari Chaenocephalus aceratus Antarctic fish hemoglobin myoglobin Gobionotothen gibberifrons Chionodraco rastrospinosus |
description |
The unusual pattern of expression of hemoglobin (Hb) and myoglobin (Mb) among Antarctic notothenioid fishes provides an exceptional model system for assessing the impact of these proteins on oxidative stress. We tested the hypothesis that the lack of oxygen-binding proteins may reduce oxidative stress. Levels and activity of pro-oxidants, small-molecule and enzymatic antioxidants, and levels of oxidized lipids and proteins in liver, oxidative skeletal muscle, and heart ventricle were quantified in five species of notothenioid fishes differing in the expression of Hb and Mb. Levels of ubiquitinated proteins and rates of protein degradation by the 20S proteasome were also quantified. Although levels of oxidized proteins and lipids, ubiquitinated proteins, and antioxidants are higher in red-blooded fishes than in Hb-less icefishes in some tissues, this pattern does not persist across all tissues. Expression of Mb is not associated with oxidative damage in heart ventricle, whereas the activity of citrate synthase and contents of heme are positively correlated with oxidative damage in most tissues. Despite some tissue differences in levels of protein carbonyls among species, rates of degradation by the 20S proteasome are not markedly different, suggesting either alternative pathways for eliminating oxidized proteins or redox tone varies among species. Together, our data indicate that the loss of Hb and Mb does not correspond with a clear pattern of either reduced oxidative defense or oxidative damage. Data Summary JEB O'Brien et al JEXBIO_2017_162503 Funding provided by: National Science Foundation Crossref Funder Registry ID: http://dx.doi.org/10.13039/100000001 Award Number: PLR 1043781 and PLR 1043576 |
format |
Other/Unknown Material |
author |
O'Brien, Kristin M. Crockett, Elizabeth L. Philip, Jacques Oldham, Corey A. Hoffman, Megan Kuhn, Donald E. Barry, Ronald McLaughlin, Jessica |
author_facet |
O'Brien, Kristin M. Crockett, Elizabeth L. Philip, Jacques Oldham, Corey A. Hoffman, Megan Kuhn, Donald E. Barry, Ronald McLaughlin, Jessica |
author_sort |
O'Brien, Kristin M. |
title |
Data from: The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes |
title_short |
Data from: The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes |
title_full |
Data from: The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes |
title_fullStr |
Data from: The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes |
title_full_unstemmed |
Data from: The loss of hemoglobin and myoglobin does not minimize oxidative stress in Antarctic icefishes |
title_sort |
data from: the loss of hemoglobin and myoglobin does not minimize oxidative stress in antarctic icefishes |
publisher |
Zenodo |
publishDate |
2017 |
url |
https://doi.org/10.5061/dryad.5228g |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
https://doi.org/10.1242/jeb.162503 https://zenodo.org/communities/dryad https://doi.org/10.5061/dryad.5228g oai:zenodo.org:4979865 |
op_rights |
info:eu-repo/semantics/openAccess Creative Commons Zero v1.0 Universal https://creativecommons.org/publicdomain/zero/1.0/legalcode |
op_doi |
https://doi.org/10.5061/dryad.5228g10.1242/jeb.162503 |
_version_ |
1810486499041345536 |