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Stress Impairs Skin Barrier Function and Induces α2-3 Linked N-Acetylneuraminic Acid and Core 1 O-Glycans on Skin Mucins in Atlantic Salmon, Salmo salar
The skin barrier consists of mucus, primarily comprising highly glycosylated mucins, and the epithelium. Host mucin glycosylation governs interactions with pathogens and stress is associated with impaired epithelial barrier function. We characterized Atlantic salmon skin barrier function during chro...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7867331/ https://www.ncbi.nlm.nih.gov/pubmed/33540792 http://dx.doi.org/10.3390/ijms22031488 |
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author | Benktander, John Sundh, Henrik Sundell, Kristina Murugan, Abarna V. M. Venkatakrishnan, Vignesh Padra, János Tamás Kolarevic, Jelena Terjesen, Bendik Fyhn Gorissen, Marnix Lindén, Sara K. |
author_facet | Benktander, John Sundh, Henrik Sundell, Kristina Murugan, Abarna V. M. Venkatakrishnan, Vignesh Padra, János Tamás Kolarevic, Jelena Terjesen, Bendik Fyhn Gorissen, Marnix Lindén, Sara K. |
author_sort | Benktander, John |
collection | PubMed |
description | The skin barrier consists of mucus, primarily comprising highly glycosylated mucins, and the epithelium. Host mucin glycosylation governs interactions with pathogens and stress is associated with impaired epithelial barrier function. We characterized Atlantic salmon skin barrier function during chronic stress (high density) and mucin O-glycosylation changes in response to acute and chronic stress. Fish held at low (LD: 14–30 kg/m(3)) and high densities (HD: 50-80 kg/m(3)) were subjected to acute stress 24 h before sampling at 17 and 21 weeks after start of the experiment. Blood parameters indicated primary and secondary stress responses at both sampling points. At the second sampling, skin barrier function towards molecules was reduced in the HD compared to the LD group (P(app) mannitol; p < 0.01). Liquid chromatography–mass spectrometry revealed 81 O-glycan structures from the skin. Fish subjected to both chronic and acute stress had an increased proportion of large O-glycan structures. Overall, four of the O-glycan changes have potential as indicators of stress, especially for the combined chronic and acute stress. Stress thus impairs skin barrier function and induces glycosylation changes, which have potential to both affect interactions with pathogens and serve as stress indicators. |
format | Online Article Text |
id | pubmed-7867331 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-78673312021-02-07 Stress Impairs Skin Barrier Function and Induces α2-3 Linked N-Acetylneuraminic Acid and Core 1 O-Glycans on Skin Mucins in Atlantic Salmon, Salmo salar Benktander, John Sundh, Henrik Sundell, Kristina Murugan, Abarna V. M. Venkatakrishnan, Vignesh Padra, János Tamás Kolarevic, Jelena Terjesen, Bendik Fyhn Gorissen, Marnix Lindén, Sara K. Int J Mol Sci Article The skin barrier consists of mucus, primarily comprising highly glycosylated mucins, and the epithelium. Host mucin glycosylation governs interactions with pathogens and stress is associated with impaired epithelial barrier function. We characterized Atlantic salmon skin barrier function during chronic stress (high density) and mucin O-glycosylation changes in response to acute and chronic stress. Fish held at low (LD: 14–30 kg/m(3)) and high densities (HD: 50-80 kg/m(3)) were subjected to acute stress 24 h before sampling at 17 and 21 weeks after start of the experiment. Blood parameters indicated primary and secondary stress responses at both sampling points. At the second sampling, skin barrier function towards molecules was reduced in the HD compared to the LD group (P(app) mannitol; p < 0.01). Liquid chromatography–mass spectrometry revealed 81 O-glycan structures from the skin. Fish subjected to both chronic and acute stress had an increased proportion of large O-glycan structures. Overall, four of the O-glycan changes have potential as indicators of stress, especially for the combined chronic and acute stress. Stress thus impairs skin barrier function and induces glycosylation changes, which have potential to both affect interactions with pathogens and serve as stress indicators. MDPI 2021-02-02 /pmc/articles/PMC7867331/ /pubmed/33540792 http://dx.doi.org/10.3390/ijms22031488 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Benktander, John Sundh, Henrik Sundell, Kristina Murugan, Abarna V. M. Venkatakrishnan, Vignesh Padra, János Tamás Kolarevic, Jelena Terjesen, Bendik Fyhn Gorissen, Marnix Lindén, Sara K. Stress Impairs Skin Barrier Function and Induces α2-3 Linked N-Acetylneuraminic Acid and Core 1 O-Glycans on Skin Mucins in Atlantic Salmon, Salmo salar |
title | Stress Impairs Skin Barrier Function and Induces α2-3 Linked N-Acetylneuraminic Acid and Core 1 O-Glycans on Skin Mucins in Atlantic Salmon, Salmo salar |
title_full | Stress Impairs Skin Barrier Function and Induces α2-3 Linked N-Acetylneuraminic Acid and Core 1 O-Glycans on Skin Mucins in Atlantic Salmon, Salmo salar |
title_fullStr | Stress Impairs Skin Barrier Function and Induces α2-3 Linked N-Acetylneuraminic Acid and Core 1 O-Glycans on Skin Mucins in Atlantic Salmon, Salmo salar |
title_full_unstemmed | Stress Impairs Skin Barrier Function and Induces α2-3 Linked N-Acetylneuraminic Acid and Core 1 O-Glycans on Skin Mucins in Atlantic Salmon, Salmo salar |
title_short | Stress Impairs Skin Barrier Function and Induces α2-3 Linked N-Acetylneuraminic Acid and Core 1 O-Glycans on Skin Mucins in Atlantic Salmon, Salmo salar |
title_sort | stress impairs skin barrier function and induces α2-3 linked n-acetylneuraminic acid and core 1 o-glycans on skin mucins in atlantic salmon, salmo salar |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7867331/ https://www.ncbi.nlm.nih.gov/pubmed/33540792 http://dx.doi.org/10.3390/ijms22031488 |
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