Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand
Perrott, M.R.; Lovett, B.A.; De Clercq, A.; Davie, P.S.; Munday, J.S.; Morel, P.C.H.; Preece, M.A.; Symonds, J.E.; Walker, S.P.; Loo, T.; Norris, G.; Naffa, R. (2020). Type I collagen differences in farmed Chinook salmon (Oncorhynchus tshawytscha) in New Zealand. Aquaculture 525: 735264. https://hdl.handle.net/10.1016/j.aquaculture.2020.735264 In: Aquaculture. Elsevier: Amsterdam; London; New York; Oxford; Tokyo. ISSN 0044-8486; e-ISSN 1873-5622, more |  |
| Keywords | Oncorhynchus tshawytscha (Walbaum, 1792) [WoRMS]; Salmo salar Linnaeus, 1758 [WoRMS]
| | Author keywords | Collagen; Crosslinks; Chinook salmon; Atlantic salmon; Spinal curvature |
| Authors | | Top | - Perrott, M.R.
- Lovett, B.A.
- De Clercq, A., more
- Davie, P.S.
| - Munday, J.S.
- Morel, P.C.H.
- Preece, M.A.
- Symonds, J.E.
| - Walker, S.P.
- Loo, T.
- Norris, G.
- Naffa, R.
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| Abstract | 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 crosslinks (HLNL, HHMD) associated with loose connective tissue and the extracellular matrix were seen in salmon from Farm 1 and also associated with condition factor. These results demonstrated differences in the amount of Col-I and crosslink profile of farmed Chinook salmon which could be linked with a population-based susceptibility toward LKS. The association between LKS and genetic and/or husbandry differences requires additional controlled experiments to determine these relationships more precisely.
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