scholarly journals Different Dietary Levels of Protein to Lipid Ratio Affected Digestive Efficiency, Skeletal Growth, and Muscle Protein in Rainbow Trout Families

2009 ◽  
Vol 2009 ◽  
pp. 1-13 ◽  
Author(s):  
Krisna Rungruangsak-Torrissen ◽  
Lars H. Stien ◽  
Britt S. Daae ◽  
Tone Vågseth ◽  
Grethe B. Thorsheim ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Muscle Protein ◽  
Skeletal Growth ◽  
Digestive Efficiency ◽  
Lipid Ratio

scholarly journals Dietary methionine availability affects the main factors involved in muscle protein turnover in rainbow trout (Oncorhynchus mykiss)

2014 ◽  
Vol 112 (4) ◽  
pp. 493-503 ◽  
Author(s):  
Ikram Belghit ◽  
Sandrine Skiba-Cassy ◽  
Inge Geurden ◽  
Karine Dias ◽  
Anne Surget ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
White Muscle ◽  
Muscle Protein ◽  
Muscle Growth ◽  
Mrna Translation ◽  
Fish Feed ◽  
Mrna Levels ◽  
Methionine Deficiency ◽  
Main Factors

Methionine is a limiting essential amino acid in most plant-based ingredients of fish feed. In the present study, we aimed to determine the effect of dietary methionine concentrations on several main factors involved in the regulation of mRNA translation and the two major proteolytic pathways (ubiquitin–proteasome and autophagy-lysosomal) in the white muscle of rainbow trout (Oncorhynchus mykiss). The fish were fed for 6 weeks one of the three isonitrogenous diets providing three different methionine concentrations (deficient (DEF), adequate (ADQ) and excess (EXC)). At the end of the experiment, the fish fed the DEF diet had a significantly lower body weight and feed efficiency compared with those fed the EXC and ADQ diets. This reduction in the growth of fish fed the DEF diet was accompanied by a decrease in the activation of the translation initiation factors ribosomal protein S6 and eIF2α. The levels of the main autophagy-related markers (LC3-II and beclin 1) as well as the expression of several autophagy genes (atg4b, atg12 l, Uvrag, SQSTM1, Mul1 and Bnip3) were higher in the white muscle of fish fed the DEF diet. Similarly, the mRNA levels of several proteasome-related genes (Fbx32, MuRF2, MuRF3, ZNF216 and Trim32) were significantly up-regulated by methionine limitation. Together, these results extend our understanding of mechanisms regulating the reduction of muscle growth induced by dietary methionine deficiency, providing valuable information on the biomarkers of the effects of low-fishmeal diets.

Effect of dietary selenium on postprandial protein deposition in the muscle of juvenile rainbow trout (Oncorhynchus mykiss)

2020 ◽  
pp. 1-11
Author(s):  
Li Wang ◽  
Long Wang ◽  
Dianfu Zhang ◽  
Sai Li ◽  
Jiaojiao Yin ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
Muscle Protein ◽  
Retention Rate ◽  
Fish Muscle ◽  
Fish Growth ◽  
Fish Feed ◽  
Protein Deposition ◽  
Juvenile Rainbow Trout

Abstract Se, an essential biological trace element, is required for fish growth. However, the underlying mechanisms remain unclear. Protein deposition in muscle is an important determinant for fish growth. This study was conducted on juvenile rainbow trout (Oncorhynchus mykiss) to explore the nutritional effects of Se on protein deposition in fish muscle by analysing the postprandial dynamics of both protein synthesis and protein degradation. Trout were fed a basal diet supplemented with or without 4 mg/kg Se (as Se yeast), which has been previously demonstrated as the optimal supplemental level for rainbow trout growth. After 6 weeks of feeding, dietary Se supplementation exerted no influence on fish feed intake, whereas it increased fish growth rate, feed efficiency, protein retention rate and muscle protein content. Results of postprandial dynamics (within 24 h after feeding) of protein synthesis and degradation in trout muscle showed that dietary Se supplementation led to a persistently hyperactivated target of rapamycin complex 1 pathway and the suppressive expression of numerous genes related to the ubiquitin–proteasome system and the autophagy–lysosome system after the feeding. However, the ubiquitinated proteins and microtubule-associated light chain 3B (LC3)-II:LC3-I ratio, biomarkers for ubiquitination and autophagy activities, respectively, exhibited no significant differences among the fish fed different experimental diets throughout the whole postprandial period. Overall, this study demonstrated a promoting effect of nutritional level of dietary Se on protein deposition in fish muscle by accelerating postprandial protein synthesis. These results provide important insights about the regulatory role of dietary Se in fish growth.

Dietary carbohydrate-to-protein ratio affects TOR signaling and metabolism-related gene expression in the liver and muscle of rainbow trout after a single meal

2011 ◽  
Vol 300 (3) ◽  
pp. R733-R743 ◽  
Author(s):  
Iban Seiliez ◽  
Stéphane Panserat ◽  
Marine Lansard ◽  
Sergio Polakof ◽  
Elisabeth Plagnes-Juan ◽  
...  
Keyword(s):  
Gene Expression ◽  
Amino Acids ◽  
Rainbow Trout ◽  
Signaling Pathway ◽  
Fatty Acid Synthase ◽  
Muscle Protein ◽  
High Protein ◽  
Tor Signaling ◽  
Lipid Fatty Acid ◽  
Regulated Gene Expression

Most teleost fish are known to require high levels of dietary proteins. Such high-protein intake could have significant effects, particularly on insulin-regulated gene expression. We therefore analyzed the effects of an increase in the ratio of dietary carbohydrates/proteins on the refeeding activation of the Akt-target of rapamycin (TOR) signaling pathways in rainbow trout and the effects on the expression of several genes related to hepatic and muscle metabolism and known to be regulated by insulin, amino acids, and/or glucose. Fish were fed once one of three experimental diets containing high (H), medium (M), or low (L) protein (P) or carbohydrate (C) levels after 48 h of feed deprivation. Activation of the Akt/TOR signaling pathway by refeeding was severely impaired by decreasing the proteins-to-carbohydrates ratio. Similarly, postprandial regulation of several genes related to glucose (Glut4, glucose-6-phosphatase isoform 1), lipid (fatty acid synthase, ATP-citrate lyase, sterol responsive element binding protein, carnitine palmitoyltransferase 1, and 3-hydroxyacyl-CoA dehydrogenase), and amino acid metabolism (serine dehydratase and branched-chain α-keto acid dehydrogenase E2 subunit) only occurred when fish were fed the high-protein diet. On the other hand, diet composition had a low impact on the expression of genes related to muscle protein degradation. Interestingly, glucokinase was the only gene of those monitored whose expression was significantly upregulated by increased carbohydrate intake. In conclusion, this study demonstrated that macro-nutrient composition of the diet strongly affected the insulin/amino acids signaling pathway and expression pattern of genes related to metabolism.

scholarly journals Pathway-oriented action of dietary essential oils to prevent muscle protein oxidation and texture deterioration of farmed rainbow trout

animal ◽  
2019 ◽  
Vol 13 (9) ◽  
pp. 2080-2091 ◽  
Author(s):  
H.M.C. Santos ◽  
L. Méndez ◽  
G. Secci ◽  
G. Parisi ◽  
R. Martelli ◽  
...  
Keyword(s):  
Rainbow Trout ◽  
Essential Oils ◽  
Protein Oxidation ◽  
Muscle Protein

Muscle Protein Electrophoresis in the GenusSalmoof Eastern Canada

1970 ◽  
Vol 27 (11) ◽  
pp. 2109-2112 ◽  
Author(s):  
R. W. Gray ◽  
J. A. McKenzie
Keyword(s):  
Rainbow Trout ◽  
Atlantic Salmon ◽  
Brown Trout ◽  
Salmo Trutta ◽  
Muscle Protein ◽  
Protein Pattern ◽  
Geographical Location ◽  
Salmo Gairdneri ◽  
Muscle Proteins ◽  
Eastern Canada

The muscle protein pattern of Atlantic salmon (Salmo solar L.) examined differed markedly from that of brown trout (Salmo trutta L.) and rainbow trout (Salmo gairdneri Richardson). Atlantic salmon muscle proteins from six areas were not influenced by the differences in sex, stage of maturation, or geographical location. The muscle proteins of brown trout taken from two areas in Newfoundland were similar and could not be easily distinguished from that of rainbow trout from Newfoundland. A polymorphism was observed in the pattern of rainbow trout from Great Pond, Nfld. The consistency of the patterns within species suggests that they may provide useful characters for identification purposes.

Contribution of the autophagy-lysosomal and ubiquitin-proteasomal proteolytic systems to total proteolysis in rainbow trout (Oncorhynchus mykiss) myotubes

2014 ◽  
Vol 307 (11) ◽  
pp. R1330-R1337 ◽  
Author(s):  
Iban Seiliez ◽  
Karine Dias ◽  
Beth M. Cleveland
Keyword(s):  
Skeletal Muscle ◽  
Rainbow Trout ◽  
Protein Degradation ◽  
Total Protein ◽  
Muscle Protein ◽  
Culture Conditions ◽  
Minor Role ◽  
Mammalian Skeletal Muscle ◽  
Relative Contribution

The ubiquitin-proteasome system (UPS) is recognized as the major contributor to total proteolysis in mammalian skeletal muscle, responsible for 50% or more of total protein degradation in skeletal muscle, whereas the autophagic-lysosome system (ALS) plays a more minor role. While the relative contribution of these systems to muscle loss is well documented in mammals, little is known in fish species. The current study uses myotubes derived from rainbow trout myogenic precursor cells as an in vitro model of white muscle tissue. Cells were incubated in complete or serum-deprived media or media supplemented with insulin-like growth factor-1 (IGF-1) and exposed to selective proteolytic inhibitors to determine the relative contribution of the ALS and UPS to total protein degradation in myotubes in different culture conditions. Results indicate that the ALS is responsible for 30–34% and 50% of total protein degradation in myotubes in complete and serum-deprived media, respectively. The UPS appears to contribute much less to total protein degradation at almost 4% in cells in complete media to nearly 17% in serum-deprived cells. IGF-1 decreases activity of both systems, as it inhibited the upregulation of both proteolytic systems induced by serum deprivation. The combined inhibition of both the ALS and UPS reduced degradation by a maximum of 55% in serum-deprived cells, suggesting an important contribution of other proteolytic systems to total protein degradation. Collectively, these data identify the ALS as a potential target for strategies aimed at improving muscle protein retention and fillet yield through reductions in protein degradation.

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