scholarly journals Effects of dietary protein intake on muscle protein synthesis and degradation in rats with gentamicin-induced acute renal failure.

1991 ◽  
Vol 1 (11) ◽  
pp. 1230-1235
Author(s):  
R Baliga ◽  
S V Shah
Keyword(s):  
Renal Failure ◽  
Acute Renal Failure ◽  
Protein Synthesis ◽  
Protein Degradation ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Isotonic Saline ◽  
Net Protein ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

In the study presented here, the muscle protein synthesis and degradation in gentamicin-induced acute renal failure were examined in rats fed a low (7%)-, normal (22%)-, and high (35%)-isocaloric protein diet. Male Sprague-Dawley rats were fed equivalent amounts of these diets for 10 days and then received daily subcutaneous injections of either 1 mL of sterile isotonic saline or 100 mg/kg of gentamicin for 7 consecutive days. The rats were sacrificed the following day, and epitrochlearis muscles were obtained for measurement of protein turnover. The serum creatinine in each of the gentamicin-treated groups were significantly higher than that in the saline-treated controls but were no different from each other. Muscle protein synthesis (calculated from the incorporation of radiolabeled (U-14C) phenylalanine) was slightly but not significantly decreased in gentamicin-treated rats as compared with that of the corresponding saline controls in each of the dietary groups. Net protein degradation (the rate of tyrosine release into media) in the 7 and 22% gentamicin-treated groups was similar to that in the corresponding saline controls. In contrast, net protein degradation was significantly greater in the 35% gentamicin group of rats when compared with that in the 7 and 22% gentamicin groups and its own control. In the 7 and 22% saline- and gentamicin-treated protein groups, there was a reduction in net protein degradation in response to insulin. In contrast, the net protein degradation continued to remain significantly elevated in the 35% gentamicin-treated group, despite addition of insulin, when compared with that in the 7 and 22% gentamicin groups and its own control.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Comparison of protein synthesis and degradation in incubated and perfused muscle

1983 ◽  
Vol 212 (3) ◽  
pp. 649-653 ◽  
Author(s):  
A S Clark ◽  
W E Mitch
Keyword(s):  
Protein Synthesis ◽  
Protein Degradation ◽  
Insulin Treatment ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Muscle Protein Degradation ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Rates of muscle protein synthesis and degradation measured in the perfused hindquarter were compared with those in incubated epitrochlearis muscles. With fed or starved mature rats, results without insulin treatment were identical. With insulin treatment, protein synthesis in perfused hindquarters was greater, though protein degradation was the same. Thus rates of muscle protein degradation estimated by these two methods in vitro correspond closely.

scholarly journals Skeletal muscle protein synthesis and degradation in patients with chronic renal failure

1994 ◽  
Vol 45 (5) ◽  
pp. 1432-1439 ◽  
Author(s):  
Giacomo Garibotto ◽  
Rodolfo Russo ◽  
Antonella Sofia ◽  
Maria Rita Sala ◽  
Cristina Robaudo ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Renal Failure ◽  
Protein Synthesis ◽  
Chronic Renal Failure ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Skeletal Muscle Protein ◽  
Skeletal Muscle Protein Synthesis ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

scholarly journals Specificity of the effects of leucine and its metabolites on protein degradation in skeletal muscle

1984 ◽  
Vol 222 (3) ◽  
pp. 579-586 ◽  
Author(s):  
W E Mitch ◽  
A S Clark
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Protein Degradation ◽  
Muscle Protein ◽  
Adult Rats ◽  
Limb Muscles ◽  
Leucine Catabolism ◽  
Muscle Protein Degradation ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

The effects of leucine, its metabolites, and the 2-oxo acids of valine and isoleucine on protein synthesis and degradation in incubated limb muscles of immature and adult rats were tested. Leucine stimulated protein synthesis but did not reduce proteolysis when leucine transamination was inhibited. 4-Methyl-2-oxopentanoate at concentrations as low as 0.25 mM inhibited protein degradation but did not change protein synthesis. The 2-oxo acids of valine and isoleucine did not change protein synthesis or degradation even at concentrations as high as 5 mM. 3-Methylvalerate, the irreversibly decarboxylated product of 4-methyl-2-oxopentanoate, decreased protein degradation at concentrations greater than or equal to 1 mM. This was not due to inhibition of 4-methyl-2-oxopentanoate catabolism, because 0.5 mM-3-methylvalerate did not suppress proteolysis, even though it inhibited leucine decarboxylation by 30%; higher concentrations of 3-methylvalerate decreased proteolysis progressively without inhibiting leucine decarboxylation further. During incubation with [1-14C]- and [U-14C]-leucine, it was found that products of leucine catabolism formed subsequent to the decarboxylation of 4-methyl-2-oxopentanoate accumulated intracellularly. This pattern was not seen during incubation with radiolabelled valine. Thus, the effect of leucine on muscle proteolysis requires transamination to 4-methyl-2-oxopentanoate. The inhibition of muscle protein degradation by leucine is most sensitive to, but not specific for, its 2-oxo acid, 4-methyl-2-oxopentanoate.

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