Regulation of mammalian protein synthesis <i>in vivo</i>. Protein synthesis in rat liver and kidney after the administration of sublethal doses of cyclohyximide

Rothblum, Lawrence I.; Devlin, Thomas M.; Ch'ih, John J.

doi:10.1042/bj1560151

Cited by 49 publications

(23 citation statements)

References 24 publications

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“…Cycloheximide was administered 4 h later in sufficient quantities to block the incorporation of amino acids into protein by more than 85% [26]. The activities of the enzymes tyrosine aminotransferase and tryptophan oxygenase were determined during the course of the experiment.…”

Section: Efsects Of Cycloheximide On the Induction Of Tyrosine Aminotmentioning

confidence: 99%

Cycloheximide Causes Increased Accumulation of Translatable mRNA for Tyrosine Aminotransferase and Tryptophan Oxygenase in Livers of Cortisol‐Treated Rats

Hofer

Sékeris²

1978

European Journal of Biochemistry

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Messenger RNA activities for two cortisol‐inducible enzymes, tyrosine aminotransferase and tryptophan oxygenase, have been determined by translation in a wheat germ system. The effects of cycloheximide on the two mRNA activities have been evaluated. Cortisol leads to an increase of the translatable mRNAs for tyrosine aminotransferase and tryptophan oxygenase with a maximum at approximately 6 h. Cycloheximide was administered 4 h after treatment with cortisol; 2 h later, the activities of tyrosine aminotransferase and tryptophan oxygenase mRNA had increased five‐fold and two‐fold, respectively, compared to the activities reached with cortisol alone. Thereafter the amount of the two translatable mRNAs declined, though 14 h after cortisol administration the mRNA activities were still severalfold higher than in control animals. Application of α‐amanitin together with cycloheximide did not prevent an increased accumulation of specific translatable mRNAs. The increase in tyrosine aminotransferase and tryptophan oxygenase activity by cortisol was immediately blocked by cycloheximide. Whereas tryptophan oxygenase activity rapidly declined after cycloheximide application, tyrosine aminotransferase activity remained at the same level. Approximately 4 h thereafter, both enzyme activities increased again.

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Section: Efsects Of Cycloheximide On the Induction Of Tyrosine Aminotmentioning

confidence: 99%

Cycloheximide Causes Increased Accumulation of Translatable mRNA for Tyrosine Aminotransferase and Tryptophan Oxygenase in Livers of Cortisol‐Treated Rats

Hofer

Sékeris²

1978

European Journal of Biochemistry

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“…The nature and degree of its effect on microsomal protein synthesis [3,7], induction of fatty liver and lipid synthesis [9,15], microsomal enzymes [6,7] and proteolytic enzyme activity [8] differ in suckling and adult rats. PC, PE and cholesterol are the major lipid components of microsomal membranes and they are necessary to maintain the structural and functional integrity of hepatic endoplasmic reticulum [16].…”

Section: Discussionmentioning

confidence: 99%

“…Cycloheximide is an effective inhibitor of mammalian microsomal protein synthesis [3,7] and its pharmacological properties have been stud ied in rats using non-lethal doses [3,[5][6][7]14]. The nature and degree of its effect on microsomal protein synthesis [3,7], induction of fatty liver and lipid synthesis [9,15], microsomal enzymes [6,7] and proteolytic enzyme activity [8] differ in suckling and adult rats.…”

Section: Discussionmentioning

confidence: 99%

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Effect of Cycloheximide on Hepatic Microsomal Lipids as a Function of Age in Rats

Pushpendran¹,

Devasagayam²,

Eapen³

1982

Dev Pharmacol Ther

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Cycloheximide, at a non-lethal dose of 2 mg/kg body weight, increases the level of total lipids and major lipid fractions in total, rough and smooth liver microsomes obtained from suckling, adult and old rats, but not in the newborns. The rates of increase differ in the different age-groups and fractions. Total lipids and phosphatidyl choline of rough and smooth microsomes in adult rats reach control levels at 6 h after the antibiotic treatment. Phospholipid fractions of old rats tend to approach control levels by 6 h after treatment whereas cholesterol levels remain relatively high. Total lipids, phosphatidyl choline and phosphatidyl ethanolamine of total, rough and smooth microsomes show significant quantitative differences during development.

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“…in Krebs-Ringer bicarbonate medium. The effect of cycloheximide (1 mg/ml of me dium), an antibiotic which inhibits protein synthesis [13], was also determined. The flask was gassed for 30 s with 95% oxygen and 5% carbon dioxide and incubated at 38°C for 10-40 min.…”

Section: Methodsmentioning

confidence: 99%

Amino Acid Administration Enhances Renal Protein Metabolism after Acute Tubular Necrosis

Toback¹,

Rc²,

Er³

et al. 1983

Nephron

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The capacity of exogenous amino acids to alter renal protein metabolism was studied during renal regeneration after mercuric chloride-induced acute tubular necrosis in the rat. In regenerating cortical tissue, the free leucine concentration was 17% lower than normal, and was decreased further after glucose infusion. The concentration was raised above normal by amino acid infusion thereby ameliorating the deficit of this amino acid. Synthesis and degradation of rapidly-turning over proteins in renal cortical cells was examined in vitro. Renal protein synthesis in cortical slices was assessed by measurements of tissue leucine specific radioactivity and cycloheximide-inhibitable [¹⁴C]leucine incorporation into protein. Protein synthesis in regenerating tissue was 52% higher than normal and was not increased further by glucose infusion. In contrast, amino acid infusion increased the rate 47% above that observed after an isocaloric glucose infusion, thereby demonstrating that amino acid enhancement of protein synthesis is superimposed upon the increased synthetic rate observed during renal regeneration. Renal protein degradation remained at the normal rate after amino acid infusion, but was increased in regenerating tissue and after glucose infusion. These results indicate that infused amino acids act on the kidney to enhance protein synthesis and reduce protein degradation in regenerating renal cells after acute tubular necrosis.

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Regulation of mammalian protein synthesis in vivo. Protein synthesis in rat liver and kidney after the administration of sublethal doses of cyclohyximide

Cited by 49 publications

References 24 publications

Cycloheximide Causes Increased Accumulation of Translatable mRNA for Tyrosine Aminotransferase and Tryptophan Oxygenase in Livers of Cortisol‐Treated Rats

Cycloheximide Causes Increased Accumulation of Translatable mRNA for Tyrosine Aminotransferase and Tryptophan Oxygenase in Livers of Cortisol‐Treated Rats

Effect of Cycloheximide on Hepatic Microsomal Lipids as a Function of Age in Rats

Amino Acid Administration Enhances Renal Protein Metabolism after Acute Tubular Necrosis

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