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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...

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Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
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.
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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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