Proteomic analysis of muscle tissue from rainbow trout (Oncorhynchus mykiss) fed dietary β-glucan

Document Type : Full paper (Original article)

Authors

1 Graduated from Faculty of Marine Natural Resources, Khorramshahr University of Marine Science and Technology, Khorramshahr, Iran

2 Department of Fisheries, Faculty of Marine Natural Resources, Khorramshahr University of Marine Science and Technology, Khorramshahr, Iran

3 Department of Aquatic Animal Health and Diseases, School of Veterinary Medicine, Shiraz University, Shiraz, Iran

Abstract

The aim of this study was to examine the changes in muscle proteome of the rainbow trout fed dietary β-glucan. The experimental diets contained 0 (control), 0.1% and 0.2% β-1,3/1,6 yeast glucan. First, feeding larvae were fed to apparent satiation nine times per day with their respective diets over two months. The percentage of body weight gain and feed efficiency of fish fed 0.2% diet was significantly higher than those of fish fed the control and 0.1% diets. Fish fed the control and 0.2% diets were subjected to proteomic analysis. Proteins of the muscle tissue were analyzed using two-dimensional electrophoresis and mass spectrometry. Spots that were found to differ significantly in abundance between control and β-glucan fed fish were selected for identification. Out of 8 protein spots showing differential expression, 7 spots were successfully identified. Two protein spots that were found to be increased in abundance in the β-glucan treated rainbow trout corresponded to tropomyosin alpha-1 chain (spot 1) and slow myotomal muscle tropomyosin (spot 2). The five spots that were down-regulated with dietary β-glucan supplementation were identified as different forms of myosin: myosin light polypeptide 3-2 (spot 3), myosin light chain 1 (spots 4 and 5), fast myosin light chain 2 (spot 6) and myosin heavy chain (spot 7). The altered expression of structural proteins in fish fed β-glucan may be related to higher growth rate in rainbow trout. These findings provide basic information to understand possible mechanisms of dietary β-glucan contribution to better growth in rainbow trout.

Keywords

References

Addis, MF; Cappuccinelli, R; Tedde, V; Pagnozzi, D; Porcu, MC; Bonaglini, E; Roggio, T and Uzzau, S (2010). Proteomic analysis of muscle tissue from gilthead sea bream (Sparus aurata, L.) farmed in offshore floating cages. Aquaculture. 309: 245-252.
Alami-Durante, H; Cluzeaud, M; Bazin, D; Mazurais, D and Zambonino-Infante, JL (2011). Dietary cholecalci-ferol regulates the recruitment and growth of skeletal muscle fibers and the expressions of myogenic regulatory factors and the myosin heavy chain in European sea bass larvae. J. Nutr., 141: 2146-2151.
Bostock, J; McAndrew, B; Richards, R; Jauncey, K; Telfer, T; Lorenzen, K; Little, D; Ross, L; Handisyde, N; Gatward, I and Corner, R (2010). Aquaculture: global status and trends. Phil. Trans. R. Soc. B., 365: 2897-2912.
Bradford, MM (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72: 248-254.
Candiano, G; Bruschi, M; Musante, L; Santucci, L; Ghiggeri, GM; Carnemolla, B; Orecchia, P; Zardi, L and Righetti, PG (2004). Blue silver: a very sensitive colloidal coomassie G-250 staining for proteome analysis. Electrophoresis. 25: 1327-1333.
Dalmo, RA and Bøgwald, J (2008). β-glucans as conductors of immune symphonies. Fish shellfish Immunol., 25: 384-396.
Ghaedi, G; Keyvanshokooh, S; Azarm, HM and Akhlaghi, M (2015). Effects of dietary β-glucan on maternal immunity and fry quality of rainbow trout (Oncorhynchus mykiss). Aquaculture. 441: 78-83.
Goldspink, G; Wilkes, D and Ennion, S (2001). Myosin expression during ontogeny, post-hatching growth, and adaptation. Fish Physiol., 18: 43-72.
Greenlee, AR; Dodson, MV; Yablonka-Reuveni, Z; Kersten, CA and Cloud, JG (1995). In vitro differentia-tion of myoblasts from skeletal muscle of rainbow trout. J. Fish Biol., 46: 731-747.
Keyvanshokooh, S and Tahmasebi-Kohyani, A (2012). Proteome modifications of fingerling rainbow trout (Oncorhynchus mykiss) muscle as an effect of dietary nucleotides. Aquaculture. 324: 79-84.
Krasnov, A; Teerijoki, H; Gorodilov, Y and Mölsä, H (2003). Cloning of rainbow trout (Oncorhynchus mykiss) α-actin, myosin regulatory light chain genes and the 5′-flanking region of α-tropomyosin. Functional assessment of promoters. J. Exp. Biol., 206: 601-608.
Pionnier, N; Falco, A; Miest, J; Frost, P; Irnazarow, I; Shrive, A and Hoole, D (2013). Dietary β-glucan stimulate complement and C-reactive protein acute phase responses
in common carp (Cyprinus carpio) during an Aeromonas salmonicida infection. Fish Shellfish Immunol., 34: 819-831.
Rodrigues, PM; Silva, TS; Dias, J and Jessen, F (2012). Proteomics in aquaculture: applications and trends. J. Proteomics. 75: 4325-4345.
Rowlerson, A; Radaelli, G; Mascarello, F and Veggetti, A (1997). Regeneration of skeletal muscle in two teleost fish: Sparus aurata and Brachydanio rerio. Cell Tissue Res., 289: 311-322.
Terova, G; Addis, MF; Preziosa, E; Pisanu, S; Pagnozzi, D; Biosa, G; Gornati, R; Bernardini, G; Roggio, T and Saroglia, M (2011). Effects of postmortem storage temperature on sea bass (Dicentrarchus labrax) muscle protein degradation: analysis by 2-D DIGE and MS. Proteomics. 11: 2901-2910.

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