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Dietary Effect on the Proteome of the Common Octopus (Octopus vulgaris) Paralarvae
Nowadays, the common octopus (Octopus vulgaris) culture is hampered by massive mortalities occurring during early life-cycle stages (paralarvae). Despite the causes of the high paralarvae mortality are not yet well-defined and understood, the nutritional stress caused by inadequate diets is pointed...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5434110/ https://www.ncbi.nlm.nih.gov/pubmed/28567020 http://dx.doi.org/10.3389/fphys.2017.00309 |
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author | Varó, Inmaculada Cardenete, Gabriel Hontoria, Francisco Monroig, Óscar Iglesias, José Otero, Juan J. Almansa, Eduardo Navarro, Juan C. |
author_facet | Varó, Inmaculada Cardenete, Gabriel Hontoria, Francisco Monroig, Óscar Iglesias, José Otero, Juan J. Almansa, Eduardo Navarro, Juan C. |
author_sort | Varó, Inmaculada |
collection | PubMed |
description | Nowadays, the common octopus (Octopus vulgaris) culture is hampered by massive mortalities occurring during early life-cycle stages (paralarvae). Despite the causes of the high paralarvae mortality are not yet well-defined and understood, the nutritional stress caused by inadequate diets is pointed out as one of the main factors. In this study, the effects of diet on paralarvae is analyzed through a proteomic approach, to search for novel biomarkers of nutritional stress. A total of 43 proteins showing differential expression in the different conditions studied have been identified. The analysis highlights proteins related with the carbohydrate metabolism: glyceraldehyde-3-phosphate-dedydrogenase (GAPDH), triosephosphate isomerase; other ways of energetic metabolism: NADP(+)-specific isocitrate dehydrogenase, arginine kinase; detoxification: glutathione-S-transferase (GST); stress: heat shock proteins (HSP70); structural constituent of eye lens: S-crystallin 3; and cytoskeleton: actin, actin-beta/gamma1, beta actin. These results allow defining characteristic proteomes of paralarvae depending on the diet; as well as the use of several of these proteins as novel biomarkers to evaluate their welfare linked to nutritional stress. Notably, the changes of proteins like S-crystallin 3, arginine kinase and NAD(+) specific isocitrate dehydrogenase, may be related to fed vs. starving paralarvae, particularly in the first 4 days of development. |
format | Online Article Text |
id | pubmed-5434110 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-54341102017-05-31 Dietary Effect on the Proteome of the Common Octopus (Octopus vulgaris) Paralarvae Varó, Inmaculada Cardenete, Gabriel Hontoria, Francisco Monroig, Óscar Iglesias, José Otero, Juan J. Almansa, Eduardo Navarro, Juan C. Front Physiol Physiology Nowadays, the common octopus (Octopus vulgaris) culture is hampered by massive mortalities occurring during early life-cycle stages (paralarvae). Despite the causes of the high paralarvae mortality are not yet well-defined and understood, the nutritional stress caused by inadequate diets is pointed out as one of the main factors. In this study, the effects of diet on paralarvae is analyzed through a proteomic approach, to search for novel biomarkers of nutritional stress. A total of 43 proteins showing differential expression in the different conditions studied have been identified. The analysis highlights proteins related with the carbohydrate metabolism: glyceraldehyde-3-phosphate-dedydrogenase (GAPDH), triosephosphate isomerase; other ways of energetic metabolism: NADP(+)-specific isocitrate dehydrogenase, arginine kinase; detoxification: glutathione-S-transferase (GST); stress: heat shock proteins (HSP70); structural constituent of eye lens: S-crystallin 3; and cytoskeleton: actin, actin-beta/gamma1, beta actin. These results allow defining characteristic proteomes of paralarvae depending on the diet; as well as the use of several of these proteins as novel biomarkers to evaluate their welfare linked to nutritional stress. Notably, the changes of proteins like S-crystallin 3, arginine kinase and NAD(+) specific isocitrate dehydrogenase, may be related to fed vs. starving paralarvae, particularly in the first 4 days of development. Frontiers Media S.A. 2017-05-17 /pmc/articles/PMC5434110/ /pubmed/28567020 http://dx.doi.org/10.3389/fphys.2017.00309 Text en Copyright © 2017 Varó, Cardenete, Hontoria, Monroig, Iglesias, Otero, Almansa and Navarro. 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) or licensor 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 | Physiology Varó, Inmaculada Cardenete, Gabriel Hontoria, Francisco Monroig, Óscar Iglesias, José Otero, Juan J. Almansa, Eduardo Navarro, Juan C. Dietary Effect on the Proteome of the Common Octopus (Octopus vulgaris) Paralarvae |
title | Dietary Effect on the Proteome of the Common Octopus (Octopus vulgaris) Paralarvae |
title_full | Dietary Effect on the Proteome of the Common Octopus (Octopus vulgaris) Paralarvae |
title_fullStr | Dietary Effect on the Proteome of the Common Octopus (Octopus vulgaris) Paralarvae |
title_full_unstemmed | Dietary Effect on the Proteome of the Common Octopus (Octopus vulgaris) Paralarvae |
title_short | Dietary Effect on the Proteome of the Common Octopus (Octopus vulgaris) Paralarvae |
title_sort | dietary effect on the proteome of the common octopus (octopus vulgaris) paralarvae |
topic | Physiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5434110/ https://www.ncbi.nlm.nih.gov/pubmed/28567020 http://dx.doi.org/10.3389/fphys.2017.00309 |
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