Cycloheximide: Aspects of Inhibition of Protein Synthesis in Mammalian Cells

@article{Ennis1964CycloheximideAO,
  title={Cycloheximide: Aspects of Inhibition of Protein Synthesis in Mammalian Cells},
  author={Herbert L. Ennis and Martin Lubin},
  journal={Science},
  year={1964},
  volume={146},
  pages={1474 - 1476}
}
Cycloheximide and acetoxy-cycloheximide specifically inhibit protein synthesis in L-cells growing in suspension culture. In extracts of rat liver, the drugs inhibit transfer of amino acid from soluble RNA to polypeptide. Unlike puromycin, these drugs do not accelerate release of nascent polypeptide chains. The drugs have no effect on protein synthesis in extracts of Escherichia coli. 

Inhibition of Protein Synthesis by Cyclo-heximide (Actidione) in Chlorella

TLDR
Investigations with extracts free of cells showed that the primary effect of cycloheximide was to inhibit synthesis of protein, and that it did this by preventing the transfer of the amino-acids from the sRNA–amino-acid complex to the polypeptide chain.

Does cycloheximide interfere with protein degradation?

Inhibition of protein synthesis and intestinal absorptive cell ultrastructure in cycloheximide or puromycin-treated rats.

TLDR
Inhibitors of protein synthesis are useful for the investigation of some aspects of intestinal fatty acid absorption and had different effects on absorptive cell morphology: cycloheximide definitely altered the apical surface of these cells, disorganizing their cytoplasm; puromycin did not modify brush border morphology but remodeled the mitochondria and the Golgi complexes.

Failure of Cycloheximide To Induce Tyrosine Transaminase in the Anesthetized Rat

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Data show that cycloheximide inhibits the induction caused by hydrocortisone in adrenalectomized rats or by stress in intact rats.
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