Effects of Cardiac Work and Leucine on Protein Turnover

1983 ◽  
pp. 115-125 ◽  
Author(s):  
B. Chua ◽  
D. L. Siehl ◽  
E. O. Fuller ◽  
H. E. Morgan
Keyword(s):  
Protein Turnover ◽  
Cardiac Work

Effects of diabetes on protein turnover in cardiac muscle

1980 ◽  
Vol 239 (3) ◽  
pp. E178-E185 ◽  
Author(s):  
I. H. Williams ◽  
B. H. Chua ◽  
R. H. Sahms ◽  
D. Siehl ◽  
H. E. Morgan
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Protein Turnover ◽  
Isolated Heart ◽  
Chain Elongation ◽  
Cardiac Work ◽  
Ribosomal Subunits ◽  
Heart Muscle Cells ◽  
Whole Heart

Effects of alloxan diabetes of 10-day duration on protein turnover were investigated in hearts perfused with buffers simulating control and diabetic sera. Diabetes produced a 30% inhibition of protein synthesis in hearts perfused as Langendorff or working preparations. This reduction was attributable to a 20% fall in RNA concentration and a 10% decrease in efficiency of protein synthesis. Determination of RNA in ribosomal subunits indicated that the reduction in efficiency that was observed with diabetes may be due to an inhibition of polypeptide chain elongation/termination. Pharmacological levels of insulin (25 mU/ml) and cardiac work stimulated protein synthesis in both control and diabetic hearts. Effects of diabetes and insulin on protein synthesis in isolated heart muscle cells were similar to those found in whole heart. Diabetes increased protein degradation in hearts perfused with buffer similating diabetic serum and under conditions of cardiac work. Insulin (25 mU/ml) decreased protein degradation in both control and diabetic hearts. These studies indicate that long-term diabetes produces a greater negative nitrogen balance that, in contrast to control hearts, cannot be normalized by pharmacological levels of insulin or by cardiac work.

Respiratory energy requirements and rate of protein turnover in vivo determined by the use of an inhibitor of protein synthesis and a probe to assess its effect

1994 ◽  
Vol 92 (4) ◽  
pp. 585-594 ◽  
Author(s):  
T. J. Bouma ◽  
R. De Visser ◽  
J. H. J. A. Janssen ◽  
M. J. De Kock ◽  
P H. Van Leeuwen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Energy Requirements ◽  
Inhibitor Of Protein Synthesis

Paroxetine treatment alters hippocampal protein turnover

2017 ◽  
Author(s):  
M Filiou ◽  
C Guillermier ◽  
C Poczatek ◽  
M Wang ◽  
A Chen ◽  
...  
Keyword(s):  
Protein Turnover ◽  
Paroxetine Treatment

Effects of insulin and amino acids on leg protein turnover in IDDM patients

Diabetes ◽  
1991 ◽  
Vol 40 (4) ◽  
pp. 499-508 ◽  
Author(s):  
W. M. Bennet ◽  
A. A. Connacher ◽  
R. T. Jung ◽  
P. Stehle ◽  
M. J. Rennie
Keyword(s):  
Amino Acids ◽  
Protein Turnover

Advanced glycation end products impair protein turnover in LLC-PK1: Amelioration by trypsin

2001 ◽  
Vol 59 (s78) ◽  
pp. 53-57 ◽  
Author(s):  
Guangsheng Xiang ◽  
Reinhard Schinzel ◽  
Andreas Simm ◽  
Katarina Sebekova ◽  
August Heidland
Keyword(s):  
Advanced Glycation End Products ◽  
Protein Turnover ◽  
Advanced Glycation ◽  
Glycation End Products ◽  
End Products

scholarly journals RAPID COMMUNICATION: Residual feed intake in beef cattle is associated with differences in protein turnover and nutrient transporters in ruminal epithelium

2019 ◽  
Vol 97 (5) ◽  
pp. 2181-2187
Author(s):  
Ahmed A Elolimy ◽  
Emad Abdel-Hamied ◽  
Liangyu Hu ◽  
Joshua C McCann ◽  
Daniel W Shike ◽  
...  
Keyword(s):  
Amino Acid ◽  
Beef Cattle ◽  
Protein Degradation ◽  
Insulin Signaling ◽  
Feed Intake ◽  
Feed Efficiency ◽  
Protein Turnover ◽  
Residual Feed Intake ◽  
Ubiquitin Proteasome ◽  
Ruminal Epithelium

Abstract Residual feed intake (RFI) is a widely used measure of feed efficiency in cattle. Although the precise biologic mechanisms associated with improved feed efficiency are not well-known, most-efficient steers (i.e., with low RFI coefficient) downregulate abundance of proteins controlling protein degradation in skeletal muscle. Whether cellular mechanisms controlling protein turnover in ruminal tissue differ by RFI classification is unknown. The aim was to investigate associations between RFI and signaling through the mechanistic target of rapamycin (MTOR) and ubiquitin-proteasome pathways in ruminal epithelium. One hundred and forty-nine Red Angus cattle were allocated to 3 contemporary groups according to sex and herd origin. Animals were offered a finishing diet for 70 d to calculate the RFI coefficient for each. Within each group, the 2 most-efficient (n = 6) and least-efficient animals (n = 6) were selected. Compared with least-efficient animals, the most-efficient animals consumed less feed (P < 0.05; 18.36 vs. 23.39 kg/d DMI). At day 70, plasma samples were collected for insulin concentration analysis. Ruminal epithelium was collected immediately after slaughter to determine abundance and phosphorylation status of 29 proteins associated with MTOR, ubiquitin-proteasome, insulin signaling, and glucose and amino acid transport. Among the proteins involved in cellular protein synthesis, most-efficient animals had lower (P ≤ 0.05) abundance of MTOR, p-MTOR, RPS6KB1, EIF2A, EEF2K, AKT1, and RPS6KB1, whereas MAPK3 tended (P = 0.07) to be lower. In contrast, abundance of p-EEF2K, p-EEF2K:EEF2K, and p-EIF2A:EIF2A in most-efficient animals was greater (P ≤ 0.05). Among proteins catalyzing steps required for protein degradation, the abundance of UBA1, NEDD4, and STUB1 was lower (P ≤ 0.05) and MDM2 tended (P = 0.06) to be lower in most-efficient cattle. Plasma insulin and ruminal epithelium insulin signaling proteins did not differ (P > 0.05) between RFI groups. However, abundance of the insulin-responsive glucose transporter SLC2A4 and the amino acid transporters SLC1A3 and SLC1A5 also was lower (P ≤ 0.05) in most-efficient cattle. Overall, the data indicate that differences in signaling mechanisms controlling protein turnover and nutrient transport in ruminal epithelium are components of feed efficiency in beef cattle.

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