scholarly journals Protein synthesis and degradation gene SNPs related to feed intake, feed efficiency, growth, and ultrasound carcass traits in Nellore cattle

2013 ◽  
Vol 12 (3) ◽  
pp. 2923-2936 ◽  
Author(s):  
R.C. Gomes ◽  
S.L. Silva ◽  
M.E. Carvalho ◽  
F.M. Rezende ◽  
L.F.B. Pinto ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Feed Intake ◽  
Feed Efficiency ◽  
Carcass Traits ◽  
Nellore Cattle ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

scholarly journals Impact of porcine reproductive and respiratory syndrome virus on muscle metabolism of growing pigs1

2019 ◽  
Vol 97 (8) ◽  
pp. 3213-3227 ◽  
Author(s):  
Emma T Helm ◽  
Shelby M Curry ◽  
Carson M De Mille ◽  
Wesley P Schweer ◽  
Eric R Burrough ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Growth Performance ◽  
Feed Intake ◽  
Feed Efficiency ◽  
Growing Pigs ◽  
Nutrient Restriction ◽  
Viral Challenge ◽  
Prrs Virus ◽  
Ad Libitum

Abstract Porcine reproductive and respiratory syndrome (PRRS) virus is one of the most economically significant pig pathogens worldwide. However, the metabolic explanation for reductions in tissue accretion observed in growing pigs remains poorly defined. Additionally, PRRS virus challenge is often accompanied by reduced feed intake, making it difficult to discern which effects are virus vs. feed intake driven. To account for this, a pair-fed model was employed to examine the effects of PRRS challenge and nutrient restriction on skeletal muscle and liver metabolism. Forty-eight pigs were randomly selected (13.1 ± 1.97 kg BW) and allotted to 1 of 3 treatments (n = 16 pigs/treatment): 1) PRRS naïve, ad libitum fed (Ad), 2) PRRS-inoculated, ad libitum fed (PRRS+), and 3) PRRS naïve, pair-fed to the PRRS-inoculated pigs’ daily feed intake (PF). At days postinoculation (dpi) 10 and 17, 8 pigs per treatment were euthanized and tissues collected. Tissues were assayed for markers of proteolysis (LM only), protein synthesis (LM only), oxidative stress (LM only), gluconeogenesis (liver), and glycogen concentrations (LM and liver). Growth performance, feed intake, and feed efficiency were all reduced in both PRRS+ and PF pigs compared with Ad pigs (P < 0.001). Furthermore, growth performance and feed efficiency were additionally reduced in PRRS+ pigs compared with PF pigs (P < 0.05). Activity of most markers of LM proteolysis (μ-calpain, 20S proteasome, and caspase 3/7) was not increased (P > 0.10) in PRRS+ pigs compared with Ad pigs, although activity of m-calpain was increased in PRRS+ pigs compared with Ad pigs (P = 0.025) at dpi 17. Muscle reactive oxygen species production was not increased (P > 0.10) in PRRS+ pigs compared with Ad pigs. However, phosphorylation of protein synthesis markers was decreased in PRRS+ pigs compared with both Ad (P < 0.05) and PF (P < 0.05) pigs. Liver gluconeogenesis was not increased as a result of PRRS; however, liver glycogen was decreased (P < 0.01) in PRRS+ pigs compared with Ad and PF pigs at both time points. Taken together, this work demonstrates the differential impact a viral challenge and nutrient restriction have on metabolism of growing pigs. Although markers of skeletal muscle proteolysis showed limited evidence of increase, markers of skeletal muscle synthesis were reduced during PRRS viral challenge. Furthermore, liver glycogenolysis seems to provide PRRS+ pigs with glucose needed to fuel the immune response during viral challenge.

Competition for transport of amino acids into rat heart: Effect of competitors on protein synthesis and degradation

Metabolism ◽  
1992 ◽  
Vol 41 (9) ◽  
pp. 925-933 ◽  
Author(s):  
Armando R. Tovar ◽  
Jean K. Tews ◽  
Nimbe Torres ◽  
David C. Madsen ◽  
Alfred E. Harper
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Rat Heart ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Human protein metabolism: its measurement and regulation

2002 ◽  
Vol 283 (6) ◽  
pp. E1105-E1112 ◽  
Author(s):  
Zhenqi Liu ◽  
Eugene J. Barrett
Keyword(s):  
Protein Synthesis ◽  
Whole Body ◽  
Body Protein ◽  
Architectural Support ◽  
Protein Mass ◽  
Protein Pool ◽  
Tracer Kinetic ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

The body's protein mass not only provides architectural support for cells but also serves vital roles in maintaining their function and survival. The whole body protein pool, as well as that of individual tissues, is determined by the balance between the processes of protein synthesis and degradation. These in turn are regulated by interactions among hormonal, nutritional, neural, inflammatory, and other influences. Prolonged changes in either the synthetic or degradative processes (or both) that cause protein wasting increase morbidity and mortality. The application of tracer kinetic methods, combined with measurements of the activity of components of the cellular signaling pathways involved in protein synthesis and degradation, affords new insights into the regulation of both protein synthesis and breakdown in vivo. These insights, including those from studies of insulin, insulin-like growth factor I, growth hormone, and amino acid-mediated regulation of muscle and whole body protein turnover, provide opportunities to develop and test therapeutic approaches with promise to minimize or prevent these adverse health consequences.

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