scholarly journals Long-term modulation of type L pyruvate kinase activity in young and mature rats

1982 ◽  
Vol 204 (1) ◽  
pp. 329-338 ◽  
Author(s):  
Milinda E. James ◽  
James B. Blair
Keyword(s):  
Protein Synthesis ◽  
Pyruvate Kinase ◽  
Total Protein ◽  
Time Course ◽  
Enzyme Level ◽  
Enzyme Synthesis ◽  
Synthesis Rate ◽  
Adult Rats ◽  
Young Rats ◽  
Sucrose Diet

The regulation of type L pyruvate kinase concentrations in liver of young (35–45 days old) and adult (60–85 days old) rats starved and re-fed a 71% sucrose diet was investigated. Re-feeding is accompanied by an increase in the enzyme level in liver determined kinetically and immunologically. A constant ratio of kinetic activity to immunological activity was observed under all conditions examined, indicating that activity changes are the result of a regulation of synthesis or degradation and not an interconversion between kinetically active and inactive forms of the enzyme. Synthesis of pyruvate kinase was directly examined by using hepatocytes isolated from starved and re-fed rats. A stimulation of pyruvate kinase synthesis is observed on re-feeding. This increase in synthesis of pyruvate kinase is retained by the isolated hepatocyte for up to 7h in the absence of hormonal stimuli. Administration of glucagon (1μm) to the isolated hepatocytes had no influence on synthesis of pyruvate kinase and no evidence for a glucagon-directed degradation of the enzyme was found. Re-feeding the rat was followed by a transient increase in the synthesis of pyruvate kinase. The peak rate of synthesis was observed before a detectable increase in the enzyme concentration. After a rapid synthesis period, a new steady-state level of the enzyme was achieved and synthesis rates declined. The time course and magnitude for the response to the sucrose diet was dependent on the age of the rat. In young rats, an increase in pyruvate kinase synthesis is observed within 6h and peak synthesis occurs at 11h after re-feeding sucrose. The peak synthesis rate for pyruvate kinase for young rats represents approx. 1% of total protein synthesis. With adult rats, increased pyruvate kinase synthesis is not observed for 11h, with peak synthesis occurring at 24h after re-feeding. In the older rats, peak pyruvate kinase synthesis constitutes greater than 4% of total protein synthesis. Continued re-feeding of the adult rat beyond 24h is accompanied by a decline of pyruvate kinase synthesis to approx. 1.5% of total protein synthesis. The concentration of the enzyme, however, does not decline during this period, suggesting that control of pyruvate kinase degradation as well as synthesis occurs.

scholarly journals Dietary Ornithine Affects the Tissue Protein Synthesis Rate in Young Rats

2012 ◽  
Vol 58 (4) ◽  
pp. 297-302 ◽  
Author(s):  
Kazuyo TUJIOKA ◽  
Takashi YAMADA ◽  
Mami AOKI ◽  
Koji MORISHITA ◽  
Kazutoshi HAYASE ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Tissue Protein ◽  
Young Rats ◽  
Tissue Protein Synthesis

Regrowth of atrophied skeletal muscle in adult rats after ending immobilization

1978 ◽  
Vol 44 (2) ◽  
pp. 225-230 ◽  
Author(s):  
F. W. Booth
Keyword(s):  
Skeletal Muscle ◽  
Body Weight ◽  
Adult Female ◽  
Total Protein ◽  
Recovery Time ◽  
Time Course ◽  
Citrate Synthase ◽  
Female Rats ◽  
Adult Rats ◽  
Wet Weight

The recovery time course of muscle atrophied by immobilization was followed after removal of hindlimb casts from adult female rats. Increases of only 9% in body weight, 4% in gastrocnemius weight, and 10% in soleus weight occurred in controls during the 78-day duration of the experiment. There were no increases in the amounts of total protein or of citrate synthase activities in gastrocnemius or soleus during the first 3 days after removal of hindlimb casts; thereafter, there were increases in these paramters. Citrate synthase activities per mg of gastrocnemius protein were significantly higher at the 16th and 50th day of recovery. No significant differences for citrate synthase activity per mg of soleus occurred during recovery. Until the 50th day of recovery, no significant differences for total protein in soleus and for total protein and wet weight of gastrocnemius were observed between control and recovery values. However, the wet weight of the soleus returned rapidly during recovery and was not significantly different from control during recovery.

Glucocorticoid-induced skeletal muscle atrophy in vitro is attenuated by mechanical stimulation

1992 ◽  
Vol 262 (6) ◽  
pp. C1471-C1477 ◽  
Author(s):  
J. A. Chromiak ◽  
H. H. Vandenburgh
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Protein Content ◽  
Total Protein ◽  
Weight Lifting ◽  
Mechanical Activity ◽  
Synthesis Rate ◽  
Protein Synthesis Rate

Glucocorticoids induce rapid atrophy of fast skeletal myofibers in vivo, and either weight lifting or endurance exercise reduces this atrophy by unknown mechanisms. We examined the effects of the synthetic glucocorticoid dexamethasone (Dex) on protein turnover in tissue-cultured avian fast skeletal myofibers and determined whether repetitive mechanical stretch altered the myofiber response to Dex. In static cultures after 3-5 days, 10(-8) M Dex decreased total protein content 42-74%, total protein synthesis rates 38-56%, mean myofiber diameter 35%, myosin heavy chain (MHC) content 86%, MHC synthesis rate 44%, and fibronectin synthesis rate 29%. Repetitive 10% stretch-relaxations of the cultured myofibers for 60 s every 5 min for 3-4 days prevented 52% of the Dex-induced decrease in protein content, 42% of the decrease in total protein synthesis rate, 77% of the decrease in MHC content, 42% of the decrease in MHC synthesis rate, and 67% of the decrease in fibronectin synthesis rate. This in vitro model system will complement in vivo studies in understanding the mechanism by which mechanical activity and glucocorticoids interact to regulate skeletal muscle growth.

scholarly journals Comparison of the Effects of Ornithine and Arginine on the Brain Protein Synthesis Rate in Young Rats

2015 ◽  
Vol 61 (5) ◽  
pp. 417-421 ◽  
Author(s):  
Shoko SUZUMURA ◽  
Kazuyo TUJIOKA ◽  
Takashi YAMADA ◽  
Hidehiko YOKOGOSHI ◽  
Saori AKIDUKI ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Brain Protein ◽  
Young Rats ◽  
Brain Protein Synthesis ◽  
The Brain

scholarly journals Glucose-dependent induction of acetyl-CoA carboxylase in rat hepatocyte cultures

1984 ◽  
Vol 221 (2) ◽  
pp. 343-350 ◽  
Author(s):  
S Giffhorn ◽  
N R Katz
Keyword(s):  
Enzyme Activity ◽  
Enzyme Level ◽  
Enzyme Synthesis ◽  
Acetyl Coa Carboxylase ◽  
Enzyme Protein ◽  
Atp Citrate Lyase ◽  
Acetyl Coa ◽  
Adult Rats ◽  
Hepatocyte Cultures

The carbohydrate-dependent long-term regulation of acetyl-CoA carboxylase was studied in primary hepatocyte cultures from adult rats. (1) The enzyme activity was increased 2-fold either by elevation of the glucose concentration to 20mM or by enhancement of the insulin concentration to 0.1 microM. Simultaneous increases in glucose and insulin resulted in a 5-fold increase in the enzyme activity. (2) As shown by immunochemical titration, the enhancement of the enzyme activity was due to an increase in the enzyme protein. (3) Incorporation of [35S]methionine and immunoprecipitation of the enzyme revealed that the increase in enzyme protein was due to an increased rate of enzyme synthesis. The rate of enzyme degradation remained essentially unchanged. (4) The glucose- and insulin-dependent induction of acetyl-CoA carboxylase was prevented by the addition of alpha-amanitin (10 microM) or cordycepin (10 microM), indicating a transcriptional regulation of the enzyme level. (5) The parallel induction of acetyl-CoA carboxylase and of ATP citrate lyase indicates a co-ordinate long-term regulation of lipogenic enzymes.

scholarly journals The Effects of Age and Adiposity on Casein Digestibility and Tissue Protein Synthesis in Rats

2021 ◽  
Vol 5 (Supplement_2) ◽  
pp. 1196-1196
Author(s):  
Nathalie Atallah ◽  
Claire Gaudichon ◽  
Audrey Boulier ◽  
Alain Baniel ◽  
Dalila Azzout-Marniche ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Dietary Intervention ◽  
Metabolic Response ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Standard Diet ◽  
Young Rats ◽  
Funding Sources ◽  
Significant Difference ◽  
Tissue Protein Synthesis

Abstract Objectives Age and adiposity can impact the digestibility of dietary proteins and the metabolic response to their ingestion. The objective was to evaluate the effects of age and adiposity on casein digestibility and protein synthesis in tissues and organs. Methods Wistar rats of 1 month (n = 15) and 10 months (n = 15) at their arrival were fed ad libitum with a standard diet or High Fat diet to obtain rats of normal and high adiposity levels. Four groups were constituted (n = 7/8): 2 months/normal adiposity, 2 months/high adiposity, 11 months/normal adiposity and 11 months/high adiposity. At the end of the dietary intervention, they were fed the standard diet for 1 week before the test meal. The rats consumed a 4g meal containing 15N-labeled casein (Prodiet® 85B). Six hours after meal ingestion, the rats were euthanized. Intravenous injection of a massive dose of 13C-valine prior to euthanasia was used to determine protein synthesis rate in liver, kidneys, skin and muscle. Body composition was evaluated and digestive contents were collected to measure casein digestibility. Results No weight difference between rats of the same age was observed. However, a significant difference in adiposity was noted, with a surge in body fat of 3% in young rats and 7% in older rats. Digestibility increased with a higher adiposity level (P = 0.04). In young rats, it was 94.1 ± 1.1% in lean rats and 95.2 ± 1.7% in fat rats. In older rats, it was 94.5 ± 2.2% and 95.8 ± 0.7%, in lean and fat rats respectively. Significant effects of age (P < 0.01) and adiposity (P < 0.01) were observed in the muscle fractional synthesis rate (FSR), with age decreasing it and adiposity increasing it. In young rats, FSR was 10.1 ± 2.1%/day and 12.0 ± 3.0%/day in lean and fat rats, respectively, these values being 6.2 ± 1.5%/day and 10.6 ± 2.0%/day in older rats. In the skin, younger rats exhibited a higher FSR (P < 0.01) as it was 11.1 ± 2.6%/day and 12.6 ± 3.7%/day in lean and fat rats respectively, and 8.3 ± 2.3%/day and 8.2 ± 2.7%/day in older rats. No differences were found for the liver and kidneys. Conclusions Protein synthesis in muscle decreased with age while adiposity increased it. This is consistent with an improvement in ribosomal activity at an intermediate state of obesity. The surge in casein digestibility with higher adiposity, although moderate, could have contributed to the improvement in muscle anabolism response. Funding Sources Ingredia.

Induction and maintenance of 2',5'-oligoadenylate synthetase in interferon-treated chicken embryo cells

1982 ◽  
Vol 2 (11) ◽  
pp. 1436-1443
Author(s):  
D K West ◽  
L A Ball
Keyword(s):  
Protein Synthesis ◽  
Chicken Embryo ◽  
Time Course ◽  
Enzyme Level ◽  
Primary Cultures ◽  
Synthetase Activity ◽  
Control Mechanisms ◽  
Oligoadenylate Synthetase ◽  
Cell Extracts ◽  
Embryo Cells

Treatment of primary cultures of chicken embryo cells with homologous interferon results in a substantial increase in the level of 2',5'-oligoadenylate synthetase activity that can be detected in cell extracts. This increase can be prevented by inhibitors of RNA or protein synthesis and is thus thought to represent the induction of an interferon-inducible gene, perhaps the 2',5'-oligoadenylate synthetase gene itself. To examine this response in greater detail, we studied its kinetics under the following conditions: (i) cessation of interferon treatment after different lengths of time, (ii) delayed inhibition of RNA or protein synthesis, and (iii) combinations of these treatments. The results showed that in cells treated continuously with interferon, the enzyme level reached a peak after 9 h of treatment and then decreased with a half-life of about 30 h, despite the continued presence of interferon. Removal of interferon during induction reduced the peak level of activity that was attained and somewhat accelerated its decline but did not otherwise affect the time-course of the response. On the other hand, removal of interferon after maximum induction clearly accelerated the decay of enzyme activity. This process could be delayed by inhibitors of protein synthesis, which effectively stabilized the induced enzyme. This behavior is reminiscent of other inducible enzymes, such as the steroid-induced tyrosine aminotransferase, and suggests that the level of 2',5'-oligoadenylate synthetase, which is also inducible by steroid hormones in some cell types, is subject to similar control mechanisms.

The effect of lactation on protein synthesis in ovine skeletal muscle

1982 ◽  
Vol 99 (2) ◽  
pp. 319-323 ◽  
Author(s):  
D. T. W. Bryant ◽  
R. W. Smith
Keyword(s):  
Protein Synthesis ◽  
Total Protein ◽  
Skeletal Muscles ◽  
Whole Body ◽  
Synthesis Rate ◽  
Longissimus Dorsi ◽  
Early Lactation ◽  
Lipid Contents ◽  
Plasma Tyrosine ◽  
Two Stages

SUMMARYProtein synthesis was measured in non-breeding sheep and in sheep at two stages of lactation by constant intravenous infusion of [3H] tyrosine. In early lactation plasma tyrosine flux was 50% higher than in non-breeding ewes and it remained somewhat higher in late lactation. Estimates of protein synthesis per day in the whole body showed similar changes.In early lactation the weights of the longissimus dorsi and semitendinosus muscles were respectively 37 and 28% lower than those for non-breeding ewes, but both muscles regained weight in late lactation. There were corresponding changes in the total protein, total RNA and total lipid contents of both muscles.The fractional rates of protein synthesis in the longissimus dorsi and the semitendinosus were between 2 and 3% per day, but it was higher in heart muscle. At both stages of lactation the synthesis rate in the longissimus dorsi was similar to that in nonbreeding ewes, but in the semitendinosus and in the heart synthesis rates were lower in lactating animals. In both skeletal muscles the total protein synthesized per day was lower in early lactation because their total protein contents were lower at this time. It is concluded that the maternal skeletal muscles may undergo a controlled depletion during lactation.

scholarly journals Transient induction of cyclin A in loaded chicken skeletal muscle

2003 ◽  
Vol 95 (4) ◽  
pp. 1664-1671
Author(s):  
Martin Flück ◽  
Magali Kitzmann ◽  
Christoph Däpp ◽  
Matthias Chiquet ◽  
Frank W. Booth ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Total Protein ◽  
Time Course ◽  
Cell Activation ◽  
Control Level ◽  
Cyclin A ◽  
Interstitial Cells ◽  
Synthesis Rate ◽  
Total Protein Content ◽  
Cyclin Dependent Kinase

Cell proliferation is believed to contribute to the increased synthesis rate during load-induced growth of avian anterior latissimus dorsi (ALD) skeletal muscle, but the relative contribution of different cell types to this proliferative response and the time course of cell activation are not well documented. The present investigation measured the abundance and localization of cyclin A protein, which is uniquely present in proliferating cells and required for the entry of vertebrate cells into the DNA synthesis phase during the time course of chicken ALD loading. Total protein content in 1.5-, 7-, and 13-day loaded ALD increased by 60, 191, and 294%, respectively. Immunoblotting analysis identified that cyclin A protein per total protein was dramatically increased in ALD muscle after 1.5 days of loading but returned to control level at 7 days. In vitro kinase assays demonstrated a corresponding massive activation of the cyclin A-regulated, cyclin-dependent kinase 2 but not of cyclin-dependent kinase 2 protein level in muscle homogenates after 1.5 days of muscle loading. Immunofluorescence experiments demonstrated that the increase of cyclin A in 1.5 days of loaded ALD was primarily confined to nuclei of interstitial cells (92%) but was also found in fiber-associated cells (8%). In situ hybridization demonstrated an increased number of nuclei of interstitial cells expressing collagen I transcripts after 1.5 days of loading. These data show that the cell cycle protein cyclin A is induced in fiber-associated cells during the early growth response in loaded ALD but also implicate an activation of interstitial cells as playing an early role in this model for muscle growth.

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