scholarly journals A comparison of rates of protein turnover in rat diaphragm in vivo and in vitro

1986 ◽  
Vol 233 (1) ◽  
pp. 279-282 ◽  
Author(s):  
V R Preedy ◽  
D M Smith ◽  
P H Sugden
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Rat Diaphragm ◽  
Degradation Rates ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Protein synthesis and degradation rates in diaphragms from fed or starved rats were compared in vivo and in vitro. For fed rats, synthesis rates in vivo were approximately twice those in vitro, but for starved rats rates were similar. Degradation rates were less in vivo than in vitro in diaphragms from either fed or starved rats.

scholarly journals Effect of hypophysectomy on the rates of protein synthesis and degradation in rat liver

1979 ◽  
Vol 178 (3) ◽  
pp. 725-731 ◽  
Author(s):  
R D Conde
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Rat Liver ◽  
Protein Metabolism ◽  
Plasma Proteins ◽  
Degradation Rates ◽  
Hypophysectomized Rats ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

The effect of hypophysectomy on the protein metabolism of the liver in vivo was studied. Fractional rates of protein synthesis and degradation were determined in the livers of normal and hypophysectomized rats. Synthesis was measured after the injection of massive amounts of radioactive leucine. Degradation was estimated either as the balance between synthesis and accumulation of stable liver proteins or from the disappearance of radioactivity from the proteins previously labelled by the injection of NaH14CO3. The results indicate that: (1) hypophysectomy diminishes the capacity of the liver to synthesize proteins in vivo, mainly of those that are exported as plasma proteins; (2) livers of both normal and hypophysectomized rats show identical protein-degradation rates, whereas plasma proteins are degraded slowly after hypophysectomy.

Extensive changes in collagen synthesis and degradation during compensatory lung growth

1988 ◽  
Vol 255 (6) ◽  
pp. C754-C759 ◽  
Author(s):  
R. J. McAnulty ◽  
L. H. Staple ◽  
D. Guerreiro ◽  
G. J. Laurent
Keyword(s):  
Protein Synthesis ◽  
Collagen Synthesis ◽  
Collagen Degradation ◽  
Lung Growth ◽  
Compensatory Lung Growth ◽  
Fractional Rate ◽  
Degradation Rates ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Unilateral pneumonectomy in rats causes compensatory growth of the remaining lung. This growth involves rapid production of collagen and noncollagen proteins, but the mechanisms for these changes have not been fully investigated. Rates of collagen metabolism were measured using previously validated in vivo methods. Six days after pneumonectomy, a threefold increase in the fractional rate of collagen synthesis was observed (control 11.8 +/- 0.9%/day, pneumonectomy 30.0 +/- 4.6%/day). Collagen degradation rates also increased but returned to normal more rapidly than the synthesis rates. These changes in synthesis and degradation resulted in a 75% increase in collagen content by 28 days. Although degradation of extracellular collagens was apparently increased, the fraction degraded intracellularly decreased by approximately 30%. Noncollagen protein synthesis and degradation rates both increased by approximately 80% (control 44.3 +/- 3.4%/day, pneumonectomy 80.3 +/- 10.2%/day) with a slightly greater increase in synthesis that led to an 85% increase in noncollagen protein content 28 days after pneumonectomy. The data obtained show dramatic changes in protein synthesis and degradation during compensatory lung growth and indicate extensive remodeling of structural elements in lung tissue. The changes for intracellular collagen degradation provide further evidence that this pathway may have an important role in regulating collagen deposition.

scholarly journals Response of muscle protein turnover to insulin after acute exercise and training

1986 ◽  
Vol 240 (3) ◽  
pp. 651-657 ◽  
Author(s):  
T A Davis ◽  
I E Karl
Keyword(s):  
Protein Synthesis ◽  
Exercise Training ◽  
Protein Turnover ◽  
Acute Exercise ◽  
Muscle Protein ◽  
Muscle Protein Turnover ◽  
Exercise And Training ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

To determine whether the enhanced insulin-sensitivity of glucose metabolism in muscle after acute exercise also extends to protein metabolism, untrained and exercise-trained rats were subjected to an acute bout of exercise, and the responses of protein synthesis and degradation to insulin were measured in epitrochlearis muscles in vitro. Acute exercise of both untrained and trained rats decreased protein synthesis in muscle in the absence or presence of insulin, but protein degradation was not altered. Exercise training alone had no effect on protein synthesis or degradation in muscle in the absence or presence of insulin. Acute exercise or training alone enhanced the sensitivities of both protein synthesis and degradation to insulin, but the enhanced insulin-sensitivities from training alone were not additive to those after acute exercise. These results indicate that: a decrease in protein synthesis is the primary change in muscle protein turnover after acute exercise and is not altered by prior exercise training, and the enhanced insulin-sensitivities of metabolism of both glucose and protein after either acute exercise or training suggest post-binding receptor events.

scholarly journals Rates of protein turnover in vivo and in vitro in ventricular muscle of hearts from fed and starved rats

1984 ◽  
Vol 222 (2) ◽  
pp. 395-400 ◽  
Author(s):  
V R Preedy ◽  
D M Smith ◽  
N F Kearney ◽  
P H Sugden
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Protein Turnover ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Ventricular Muscle ◽  
Degradation Rates ◽  
Perfused Hearts

Starvation of 300 g rats for 3 days decreased ventricular-muscle total protein content and total RNA content by 15 and 22% respectively. Loss of body weight was about 15%. In glucose-perfused working rat hearts in vitro, 3 days of starvation inhibited rates of protein synthesis in ventricles by about 40-50% compared with fed controls. Although the RNA/protein ratio was decreased by about 10%, the major effect of starvation was to decrease the efficiency of protein synthesis (rate of protein synthesis relative to RNA). Insulin stimulated protein synthesis in ventricles of perfused hearts from fed rats by increasing the efficiency of protein synthesis. In vivo, protein-synthesis rates and efficiencies in ventricles from 3-day-starved rats were decreased by about 40% compared with fed controls. Protein-synthesis rates and efficiencies in ventricles from fed rats in vivo were similar to values in vitro when insulin was present in perfusates. In vivo, starvation increased the rate of protein degradation, but decreased it in the glucose-perfused heart in vitro. This contradiction can be rationalized when the effects of insulin are considered. Rates of protein degradation are similar in hearts of fed animals in vivo and in glucose/insulin-perfused hearts. Degradation rates are similar in hearts of starved animals in vivo and in hearts perfused with glucose alone. We conclude that the rates of protein turnover in the anterogradely perfused rat heart in vitro closely approximate to the rates in vivo in absolute terms, and that the effects of starvation in vivo are mirrored in vitro.

scholarly journals The effect of glutamine on protein turnover in chick skeletal muscle in vitro

1990 ◽  
Vol 265 (2) ◽  
pp. 593-598 ◽  
Author(s):  
G Wu ◽  
J R Thompson
Keyword(s):  
Protein Synthesis ◽  
Skeletal Muscles ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Plasma Concentrations ◽  
Glutamine Concentration ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

The effect of glutamine on the rates of protein synthesis and degradation was studied in isolated chick extensor digitorum communis muscles incubated in the presence of plasma concentrations of amino acids. Addition of 0.5-15 mM-glutamine increases (P less than 0.01) intracellular glutamine concentrations by 31-670%. There is a positive relationship (r = 0.975, P less than 0.01) between intracellular glutamine concentration and the rate of muscle protein synthesis measured by the incorporation of [3H]phenylalanine. The stimulating effect of 15 mM-glutamine on protein synthesis was decreased from 58 to 19% in muscles incubated in the absence of tyrosine. The rates of protein degradation, estimated from [3H]phenylalanine release from muscle proteins prelabelled in vivo, decreased (P less than 0.05) by 15-30% in the presence of 4-15 mM-glutamine when compared with muscles incubated in the presence of physiological concentrations of glutamine (0.5-1 mM). Glutamine concentrations ranging from 2 to 15 mM appear to have an overall anabolic effect on chick skeletal muscles incubated in vitro.

scholarly journals Roles for ClpXP in regulating the circadian clock in Synechococcus elongatus

2018 ◽  
Vol 115 (33) ◽  
pp. E7805-E7813 ◽  
Author(s):  
Susan E. Cohen ◽  
Briana M. McKnight ◽  
Susan S. Golden
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Cell Division ◽  
Circadian Rhythms ◽  
External Environment ◽  
Long Period ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

In cyanobacteria, the KaiABC posttranslational oscillator drives circadian rhythms of gene expression and controls the timing of cell division. The Kai-based oscillator can be reconstituted in vitro, demonstrating that the clock can run without protein synthesis and degradation; however, protein degradation is known to be important for clock function in vivo. Here, we report that strains deficient in the ClpXP1P2 protease have, in addition to known long-period circadian rhythms, an exaggerated ability to synchronize with the external environment (reduced “jetlag”) compared with WT strains. Deletion of the ClpX chaperone, but not the protease subunits ClpP1 or ClpP2, results in cell division defects in a manner that is dependent on the expression of a dusk-peaking factor. We propose that chaperone activities of ClpX are required to coordinate clock control of cell division whereas the protease activities of the ClpXP1P2 complex are required to maintain appropriate periodicity of the clock and its synchronization with the external environment.

Effects of food deprivation on protein synthesis and degradation in rat skeletal muscles

1976 ◽  
Vol 231 (2) ◽  
pp. 441-448 ◽  
Author(s):  
JB Li ◽  
AL Goldberg
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Food Deprivation ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Rna Content ◽  
Fasted Rats ◽  
Synthesis And Degradation

The effects of food deprivation on protein turnover in rat soleus and extensor digitorum longus (EDL) were investigated. Muscles were removed from fed or fasted growing rats, and protein synthesis and breakdown were measured during incubation in vitro. Rates of synthesis and degradation were higher in the dark soleus than in the pale EDL. One day after food removal protein synthesis and RNA content in the EDL decreased. On the 2nd day of fasting, rates of protein catabolism in this muscle increased. Little or no change in synthesis and degradation occurred in the soleus. Consequently, during fasting the soleus lost much less weight than the EDL and other rat muscles. In unsupplemented buffer or in medium containing amino acids, glucose, and insulin, the muscles of fasted rats showed a lower rate of protein synthesis expressed per milligram of tissue but not per microgram of RNA. Thus the decrease in muscle RNA on fasting was responsible for the reduced synthesis observed under controlled in vitro conditions. In vivo the reduction in muscle protein synthesis on fasting results both from a lower RNA content and lower rate of synthesis per microgram of RNA. Reduced supply of glucose, insulin, and amino acids may account for the lower rate of synthesis per microgram of RNA demonstrable in vivo.

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