scholarly journals Liver Metabolome and Proteome Response of Turbot (Scophthalmus maximus) to Lysine and Leucine in Free and Dipeptide Forms

2021 ◽  
Vol 8 ◽  
Author(s):  
Yuliang Wei ◽  
Benxiang Li ◽  
Houguo Xu ◽  
Mengqing Liang
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Scophthalmus Maximus ◽  
Protein Digestion ◽  
Metabolic Processes ◽  
Differential Proteins ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Omics approaches provide more metabolic information to explain the relationship between dietary nutrition and fish growth. This study aimed to explore the metabolome and proteome response of turbot (Scophthalmus maximus) fed diets containing lysine and leucine in free and dipeptide forms by the approaches of integrated liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based metabolomics and isobaric tags for relative and absolute quantification (iTRAQ)-based proteomics. Plant protein-based diets were formulated to contain the equivalent of lysine and leucine in free amino acid [crystalline amino acid (CAA)] and synthetic Lys-Leu (Lys-Leu) forms. The metabolome and proteome profiles of the liver were screened in fish fed either the CAA diet or the Lys-Leu diet after an 8-week feeding trial. Fish fed the Lys-Leu diet showed a significantly higher final body weight and a specific growth rate compared with fish fed the CAA diet. Protein- and amino acid-related metabolic processes in the liver were identified between the Lys-Leu and CAA groups based on differential metabolites and proteins. The proteolytic enzymes and amino acid transporters from differential proteins of the liver showed that the process of protein digestion and absorption may be affected by the different forms of lysine and leucine in the feed. A mechanistic target of rapamycin complex 1 and ubiquitin proteasome pathways were identified by differential proteins, which were involved in the processes of protein synthesis and degradation in the liver. Lysine degradation, tryptophan metabolism, alanine, aspartate, and glutamate metabolism, arginine biosynthesis, arginine and proline metabolism, and glycine, serine, and threonine metabolism were identified based on differential metabolites and proteins, which showed that the metabolism of various amino acids, including lysine, had been affected by both the CAA and Lys-Leu groups. In conclusion, the data of integrated metabonomics and proteomics suggested that different forms of lysine and leucine in the feed may affect liver metabolic processes including protein digestion and absorption, protein synthesis and degradation, and amino acid metabolism. In addition, a good correlation between differential metabolites and proteins was observed in amino acid metabolism by using the approaches of integrated LC-MS/MS-based metabolomics and iTRAQ-based proteomics.

AMINO ACID CONTROL OF PROTEIN SYNTHESIS AND DEGRADATION IN ISOLATED RAT HEPATOCYTES*

1980 ◽  
Vol 349 (1) ◽  
pp. 1-17 ◽  
Author(s):  
Per O. Seglen ◽  
Anne E. Solheim ◽  
Bjørn Grinde ◽  
Paul B. Gordon ◽  
Per E. Schwarze ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Rat Hepatocytes ◽  
Isolated Rat Hepatocytes ◽  
Acid Control ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation ◽  
Isolated Rat

scholarly journals Rates of protein synthesis in skin and bone, and their importance in the assessment of protein degradation in the perfused rat hemicorpus

1981 ◽  
Vol 194 (1) ◽  
pp. 373-376 ◽  
Author(s):  
V R Preedy ◽  
P J Garlick
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Degradation ◽  
Muscle Tissue ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Muscle Protein ◽  
Muscle Metabolism ◽  
Muscle Protein Degradation

The perfused rat hemicorpus preparation, which has frequently been used to study muscle metabolism, contains 39% by weight of non-muscle tissue such as skin and bone. Both the concentration of RNA and the incorporation of [U-14C]tyrosine into protein indicate that the non-muscle components are more active in protein synthesis than is muscle. These observations have important implications for studies of amino acid metabolism, and in particular for the measurement of muscle protein degradation in the hemicorpus.

scholarly journals Reducing plasma HIV RNA improves muscle amino acid metabolism

2005 ◽  
Vol 288 (1) ◽  
pp. E278-E284 ◽  
Author(s):  
Kevin E. Yarasheski ◽  
Samuel R. Smith ◽  
William G. Powderly
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Hiv Rna ◽  
Muscle Protein Synthesis Rate

We reported (Yarasheski KE, Zachwieja JJ, Gischler J, Crowley J, Horgan MM, and Powderly WG. Am J Physiol Endocrinol Metab 275: E577–E583, 1998) that AIDS muscle wasting was associated with an inappropriately low rate of muscle protein synthesis and an elevated glutamine rate of appearance (Ra Gln). We hypothesized that high plasma HIV RNA caused dysregulation of muscle amino acid metabolism. We determined whether a reduction in HIV RNA (≥1 log) increased muscle protein synthesis rate and reduced Ra Gln and muscle proteasome activity in 10 men and 1 woman (22–57 yr, 60–108 kg, 17–33 kg muscle) with advanced HIV (CD4 = 0–311 cells/μl; HIV RNA = 10–375 × 103 copies/ml). We utilized stable isotope tracer methodologies ([13C]Leu and [15N]Gln) to measure the fractional rate of mixed muscle protein synthesis and plasma Ra Gln in these subjects before and 4 mo after initiating their first or a salvage antiretroviral therapy regimen. After treatment, median CD4 increased (98 vs. 139 cells/μl, P = 0.009) and median HIV RNA was reduced (155,828 vs. 100 copies/ml, P = 0.003). Mixed muscle protein synthesis rate increased (0.062 ± 0.005 vs. 0.078 ± 0.006%/h, P = 0.01), Ra Gln decreased (387 ± 33 vs. 323 ± 15 μmol·kg fat-free mass−1·h−1, P = 0.04), and muscle proteasome chymotrypsin-like catalytic activity was reduced 14% ( P = 0.03). Muscle mass was only modestly increased (1 kg, P = not significant). We estimated that, for each 10,000 copies/ml reduction in HIV RNA, ∼3 g of additional muscle protein are synthesized per day. These findings suggest that reducing HIV RNA increases muscle protein synthesis and reduces muscle proteolysis, but muscle protein synthesis relative to whole body protein synthesis rate is not restored to normal, so muscle mass is not substantially increased.

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