Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand

The integrity and function of Type I collagen (Col-I), a fundamental structural molecule, is central to fish movement. Farmed Chinook salmon in New Zealand are reported to develop a late onset curvature syndrome, lordosis, kyphosis and scoliosis (LKS), associated with inflammation and fibrosis, whic...

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Published in:Aquaculture
Main Authors: Perrott, Matthew R., Lovett, Bailey A., De Clercq, Adelbert, Davie, Peter S., Munday, John S., Morel, Patrick C.H., Preece, Mark A., Symonds, Jane E., Walker, Seumas P., Loo, Trevor, Norris, Gill, Naffa, Rafea
Format: Article in Journal/Newspaper
Language:English
Published: 2020
Subjects:
Online Access:https://biblio.ugent.be/publication/8671337
http://hdl.handle.net/1854/LU-8671337
https://doi.org/10.1016/j.aquaculture.2020.735264
https://biblio.ugent.be/publication/8671337/file/8673280
id ftunivgent:oai:archive.ugent.be:8671337
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spelling ftunivgent:oai:archive.ugent.be:8671337 2023-06-11T04:10:22+02:00 Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand Perrott, Matthew R. Lovett, Bailey A. De Clercq, Adelbert Davie, Peter S. Munday, John S. Morel, Patrick C.H. Preece, Mark A. Symonds, Jane E. Walker, Seumas P. Loo, Trevor Norris, Gill Naffa, Rafea 2020 application/pdf https://biblio.ugent.be/publication/8671337 http://hdl.handle.net/1854/LU-8671337 https://doi.org/10.1016/j.aquaculture.2020.735264 https://biblio.ugent.be/publication/8671337/file/8673280 eng eng https://biblio.ugent.be/publication/8671337 http://hdl.handle.net/1854/LU-8671337 http://dx.doi.org/10.1016/j.aquaculture.2020.735264 https://biblio.ugent.be/publication/8671337/file/8673280 No license (in copyright) info:eu-repo/semantics/restrictedAccess AQUACULTURE ISSN: 0044-8486 ISSN: 1873-5622 Biology and Life Sciences Collagen Crosslinks Chinook salmon Atlantic salmon Spinal curvature CROSS-LINK CONCENTRATION VERTEBRAL DEFORMITIES SALAR L FLESH QUALITY DIETARY PHOSPHORUS MUSCLE COLLAGEN LYSYL OXIDASE GROWTH-RATE ABNORMALITIES journalArticle info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 2020 ftunivgent https://doi.org/10.1016/j.aquaculture.2020.735264 2023-05-10T22:48:21Z The integrity and function of Type I collagen (Col-I), a fundamental structural molecule, is central to fish movement. Farmed Chinook salmon in New Zealand are reported to develop a late onset curvature syndrome, lordosis, kyphosis and scoliosis (LKS), associated with inflammation and fibrosis, which affects movement and product quality. To investigate if type I collagen integrity is associated with LKS, salmon from a farm with high LKS (Farm 1) were compared with a farm with low LKS (Farm 2). Representative salmon from Farm 1 and Farm 2 were harvested at 25 months of age and their physical metrics measured. Condition factor (K) was derived. White muscle samples from the abdominal and caudal regions were sampled and analysed. The properties of Col-I were determined using liquid chromatography-electrospray ionization mass spectrometry. The amount of Col-I in white muscle, inferred from hydroxy-proline [Hyp], was 0.071 and 0.130 ([Hyp (mg) / Dry sample (mg)]%) for Farm 1 and Farm 2 respectively. There was a significant (p < .0004) difference (~2-fold) in [Hyp] between farms and significant differences for all crosslinks reported below. Mature crosslinks histidinohydroxymerodesmosine (HHMD) were ~2.5-fold higher in Farm 1 salmon. Immature crosslinks were ~3-fold dihydroxylysinonorleucine (DHLNL) and >4-fold hydroxylysinonorleucine (HLNL) higher in Farm 1 salmon. Mature pyridinoline (PYR) crosslinks were readily detectable in salmon from Farm 2 but below the threshold for reliable detection in those from Farm 1. The mature crosslink of elastin, desmosine (DES), was ~1.5-fold higher in Farm 2 salmon. We have quantified Col-I in the white muscle compartment of farmed Chinook salmon and established methods to compare the crosslink profile. PYR and DHLNL crosslinks associated with myosepta were significantly different between the populations. Salmon from Farm 2 had both a higher proportion of mature PYR crosslinks and higher [Hyp], additive differences that may be of functional significance. Higher levels of ... Article in Journal/Newspaper Atlantic salmon Ghent University Academic Bibliography New Zealand Aquaculture 525 735264
institution Open Polar
collection Ghent University Academic Bibliography
op_collection_id ftunivgent
language English
topic Biology and Life Sciences
Collagen
Crosslinks
Chinook salmon
Atlantic salmon
Spinal curvature
CROSS-LINK CONCENTRATION
VERTEBRAL DEFORMITIES
SALAR L
FLESH QUALITY
DIETARY PHOSPHORUS
MUSCLE COLLAGEN
LYSYL OXIDASE
GROWTH-RATE
ABNORMALITIES
spellingShingle Biology and Life Sciences
Collagen
Crosslinks
Chinook salmon
Atlantic salmon
Spinal curvature
CROSS-LINK CONCENTRATION
VERTEBRAL DEFORMITIES
SALAR L
FLESH QUALITY
DIETARY PHOSPHORUS
MUSCLE COLLAGEN
LYSYL OXIDASE
GROWTH-RATE
ABNORMALITIES
Perrott, Matthew R.
Lovett, Bailey A.
De Clercq, Adelbert
Davie, Peter S.
Munday, John S.
Morel, Patrick C.H.
Preece, Mark A.
Symonds, Jane E.
Walker, Seumas P.
Loo, Trevor
Norris, Gill
Naffa, Rafea
Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand
topic_facet Biology and Life Sciences
Collagen
Crosslinks
Chinook salmon
Atlantic salmon
Spinal curvature
CROSS-LINK CONCENTRATION
VERTEBRAL DEFORMITIES
SALAR L
FLESH QUALITY
DIETARY PHOSPHORUS
MUSCLE COLLAGEN
LYSYL OXIDASE
GROWTH-RATE
ABNORMALITIES
description The integrity and function of Type I collagen (Col-I), a fundamental structural molecule, is central to fish movement. Farmed Chinook salmon in New Zealand are reported to develop a late onset curvature syndrome, lordosis, kyphosis and scoliosis (LKS), associated with inflammation and fibrosis, which affects movement and product quality. To investigate if type I collagen integrity is associated with LKS, salmon from a farm with high LKS (Farm 1) were compared with a farm with low LKS (Farm 2). Representative salmon from Farm 1 and Farm 2 were harvested at 25 months of age and their physical metrics measured. Condition factor (K) was derived. White muscle samples from the abdominal and caudal regions were sampled and analysed. The properties of Col-I were determined using liquid chromatography-electrospray ionization mass spectrometry. The amount of Col-I in white muscle, inferred from hydroxy-proline [Hyp], was 0.071 and 0.130 ([Hyp (mg) / Dry sample (mg)]%) for Farm 1 and Farm 2 respectively. There was a significant (p < .0004) difference (~2-fold) in [Hyp] between farms and significant differences for all crosslinks reported below. Mature crosslinks histidinohydroxymerodesmosine (HHMD) were ~2.5-fold higher in Farm 1 salmon. Immature crosslinks were ~3-fold dihydroxylysinonorleucine (DHLNL) and >4-fold hydroxylysinonorleucine (HLNL) higher in Farm 1 salmon. Mature pyridinoline (PYR) crosslinks were readily detectable in salmon from Farm 2 but below the threshold for reliable detection in those from Farm 1. The mature crosslink of elastin, desmosine (DES), was ~1.5-fold higher in Farm 2 salmon. We have quantified Col-I in the white muscle compartment of farmed Chinook salmon and established methods to compare the crosslink profile. PYR and DHLNL crosslinks associated with myosepta were significantly different between the populations. Salmon from Farm 2 had both a higher proportion of mature PYR crosslinks and higher [Hyp], additive differences that may be of functional significance. Higher levels of ...
format Article in Journal/Newspaper
author Perrott, Matthew R.
Lovett, Bailey A.
De Clercq, Adelbert
Davie, Peter S.
Munday, John S.
Morel, Patrick C.H.
Preece, Mark A.
Symonds, Jane E.
Walker, Seumas P.
Loo, Trevor
Norris, Gill
Naffa, Rafea
author_facet Perrott, Matthew R.
Lovett, Bailey A.
De Clercq, Adelbert
Davie, Peter S.
Munday, John S.
Morel, Patrick C.H.
Preece, Mark A.
Symonds, Jane E.
Walker, Seumas P.
Loo, Trevor
Norris, Gill
Naffa, Rafea
author_sort Perrott, Matthew R.
title Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand
title_short Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand
title_full Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand
title_fullStr Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand
title_full_unstemmed Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand
title_sort type i collagen differences in farmed chinook salmon (oncorhynchus tshawytscha) in new zealand
publishDate 2020
url https://biblio.ugent.be/publication/8671337
http://hdl.handle.net/1854/LU-8671337
https://doi.org/10.1016/j.aquaculture.2020.735264
https://biblio.ugent.be/publication/8671337/file/8673280
geographic New Zealand
geographic_facet New Zealand
genre Atlantic salmon
genre_facet Atlantic salmon
op_source AQUACULTURE
ISSN: 0044-8486
ISSN: 1873-5622
op_relation https://biblio.ugent.be/publication/8671337
http://hdl.handle.net/1854/LU-8671337
http://dx.doi.org/10.1016/j.aquaculture.2020.735264
https://biblio.ugent.be/publication/8671337/file/8673280
op_rights No license (in copyright)
info:eu-repo/semantics/restrictedAccess
op_doi https://doi.org/10.1016/j.aquaculture.2020.735264
container_title Aquaculture
container_volume 525
container_start_page 735264
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