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Regulation of mammalian protein synthesis in vivo. Stimulated liver ribonucleic acid synthesis in vivo after cycloheximide treatment.

ABSTRACT: 1. As shown by a double-radioisotope technique in vivo, at a non-lethal dose of cycloheximide, a stimulation of nuclear RNA synthesis occurred by 12 h after the treatment; the stimulation lasted over 48 h. Analysis of radioactive nuclear RNA by gel electrophoresis demonstrated that most of the cycloheximide-stimulated synthesis could be accounted for by known rRNA precursors (45 S, 41 S, 32 S and 28 S). 2. During the inhibitory phase of protein synthesis, 2 h after cycloheximide treatment, synthesis of the poly(A)-containing mRNA isolated from the cytoplasmic ribonucleoprotein complexes with an oligo(dT)-cellulose column was stimulated, whereas the synthesis of rRNA was slightly inhibited. However, during the stimulatory phase of protein synthesis, 24 h after cycloheximide treatment, the syntheses of both poly(A)-containing mRNA and rRNA were enhanced. 3. Kinetic studies revealed that the newly synthesized RNA species were transported from the nuclei, integrated into the ribonucleoprotein complexes, and associated with both free and membrane-bound polyribosomes. 4. These data corroborate our proposal that the stimulated protein synthesis after cycloheximide administration involves gene transcription.

SUBMITTER: Ch'ih JJ

PROVIDER: S-EPMC1184117 | biostudies-other | 1977 Oct

REPOSITORIES: biostudies-other

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Regulation of mammalian protein synthesis in vivo. Stimulated protein synthesis in liver in vivo after cycloheximide treatment.

Project description:Protein synthesis in rat liver in vivo was measured between 0 and 72 h after administration of a non-lethal dose of cycloheximide. There was a period of inhibition of [3H]leucine incorporation into both intra- and extra-cellular proteins at 2 h after administration of the drug, which was followed by a recovery phase in which amino acid incorporation varied significantly among the various proteins evaluated. At 12 h there was a marked stimulation of incorporation into nascent polypeptides released from polyribosomes and plasma fibrinogen, but incorporation into ribosomal proteins as well as albumin was still inhibited. Between 12 and 48 h, nascent-polypeptide synthesis remained elevated, but ribosomal-protein synthesis recovered slowly from the inhibition to normal rates only, and plasma-albumin synthesis increased slowly to above control values up to 48 h before returning to normal. A differential pattern of incorporation was also observed for incorporation into free and membrane-bound polyribosomes.

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Regulation of mammalian protein synthesis in vivo. Simulated transport of nuclear ribonucleoprotein complexes to the cytoplasm after cycloheximide treatment.

Project description:By studies in vivo with purified nuclei from rat liver, it was shown that a non-lethal dose of cycloheximide causes a decrease in the content of total nuclear ribonucleoprotein complexes by 2h after treatment. Analysis of the complex by sucrose-density-gradient centrifugation substantiated this observation for the faster-sedimenting complex, but showed an increase in the content of a smaller complex. Radioisotope incorporation studies showed that the overall decrease in nuclear ribonucleoprotein content was not due to a decreased synthesis, but rather to an increased transport to the cytoplasm. The results of a double-radioisotope technique support the conclusion that, during the inhibitory phase of protein synthesis brough on by cycloheximdie, gene transcription continues and the gene product is transported to the cytoplasm for subsequent translation.

| S-EPMC1186565 | biostudies-other

Effect of cycloheximide on protein and ribonucleic acid synthesis in cultured human lymphocytes.

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Amino acid regulation of synthesis of ribonucleic acid and protein in the liver of rats.

Project description:Weanling (23-day-old) rats were fed on either a low-protein diet (6% casein) or a diet containing an adequate amount of protein (18% casein) for 28 days. Hepatic cells from animals fed on the deficient diet were characterized by markedly lower concentrations of protein and RNA in all cellular fractions as compared with cells from control rats. The bound rRNA fraction was decreased to the greatest degree, whereas the free ribosomal concentrations were only slightly less than in control animals. A good correlation was observed between the rate of hepatic protein synthesis in vivo and the cellular protein content of the liver. Rates of protein synthesis both in vivo and in vitro were directly correlated with the hepatic concentration of individual free amino acids that are essential for protein synthesis. The decreased protein-synthetic ability of the ribosomes from the liver of protein-deprived rats was related to a decrease in the number of active ribosomes and heavy polyribosomes. The lower ribosomal content of the hepatocytes was correlated with the decreased concentration of essential free amino acids. In the protein-deprived rats, the rate of accumulation of newly synthesized cytoplasmic rRNA was markedly decreased compared with control animals. From these results it was concluded that amino acids regulate protein synthesis (1) by affecting the number of ribosomes that actively synthesize protein and (2) by inhibiting the rate of synthesis of new ribosomes. Both of these processes may involve the synthesis of proteins with a rapid rate of turnover.

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The effect of aflatoxin B 1 on normal and cortisol-stimulated rat liver ribonucleic acid synthesis.

Project description:1. Aflatoxin B(1), administered in vivo, inhibits the incorporation of [(14)C]orotic acid in vivo into rat liver nuclei, and also inhibits both Mg(2+)- and Mn(2+)-dependent RNA polymerase activities in nuclei assayed in vitro. 2. Aflatoxin B(1) inhibits the cortisol-induced increase in incorporation of [(14)C]leucine in vivo, but does not affect the control value of this activity. 3. Aflatoxin B(1) administered in vivo inhibits the increase in nuclear Mg(2+)-dependent RNA polymerase activity, assayed in vitro, which results from the treatment with cortisol. 4. Adrenalectomy causes a decrease in Mg(2+)-dependent RNA polymerase activity. The effect on this enzymic activity of adrenalectomy plus treatment with aflatoxin B(1) is no greater than that of treatment with aflatoxin B(1) alone. 5. These results suggest that the inhibition of cortisol-stimulated biochemical pathways by aflatoxin B(1) is due to an inhibition of cortisol-stimulated RNA synthesis. 6. The cytoplasmic action of aflatoxin is thought to be due to a competition for receptor sites on the endoplasmic reticulum between steroid hormones and aflatoxin B(1). No evidence was obtained for a similar competition for nuclear receptor sites between [(3)H]cortisol and aflatoxin B(1). 7. No differences were observed between the activities of RNA polymerase preparations solubilized from control or aflatoxin-inhibited nuclei. 8. No differences in ;melting' profiles were observed between DNA and chromatin preparations isolated from control nuclei or from aflatoxin-inhibited nuclei. 9. It is suggested that aflatoxin B(1) exerts its effect on RNA polymerase by decreasing the template capacity of the chromatin and that the aflatoxin ;target' area of the chromatin includes that region which is stimulated by cortisol. This process, however, does not involve inhibiting the movement of cortisol from the outside of the hepatic cell to the nuclear chromatin.

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Synthesis of ribonucleic acid by isolated rat liver mitochondria.

Project description:Rat liver mitochondria isolated in sucrose-N-tris(hydroxymethyl)methyl-2-aminoethane-sulphonic acid (TES) incorporated [(3)H]UTP into RNA for 1h. Incorporation was inhibited 50% by 1mug of actinomycin D/ml, 1mug of acriflavine/ml and 0.5mug of ethidium bromide/ml but was insensitive to rifampicin, rifamycin SV, streptovarcin and deoxyribonuclease. After the first 10min of incubation, the synthesis was insensitive to ribonuclease. RNA synthesis by mitochondria isolated in sucrose-EDTA was insensitive to actinomycin D and sensitive to ribonuclease during the first 10min of the incubation but thereafter the sensitivities were the same as for mitochondria isolated in sucrose-TES. In a hypo-osmotic medium the relative extent of incorporation of the four ribonucleoside triphosphates into RNA was CTP>UTP=ATP>>GTP. In an iso-osmotic medium the incorporation of CTP and GTP decreased. All four nucleotides were incorporated into RNA in a DNA-dependent process, as indicated by the inhibition by actinomycin D. In addition, CTP and ATP were incorporated into the CCA end of mitochondrial tRNA. ATP was also incorporated into an unidentified acid-insoluble compound, which hydrolysed in alkali to a product that was not ATP, ADP or 5'- or 2(3')-AMP. Atractyloside inhibited the incorporation of ATP into RNA with 50% inhibition at 2-3nmol/mg of protein. The [(3)H]UTP-labelled RNA had peaks of 16S and 13S characteristic of mitochondrial rRNA. In addition a peak at 20-21S was observed as well as heterogeneous RNA sedimenting throughout the gradient. The synthesis of all these species was inhibited by actinomycin D, indicating that rat liver mitochondrial DNA codes for mitochondrial rRNA as well as other as yet unidentified species.

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Ribonucleic acid synthesis in isolated rat liver nuclei under conditions of ribonucleic acid processing and transport.

Project description:A cell-free system is described which permits a significant and prolonged synthesis of RNA in isolated rat liver nuclei, under conditions previously demonstrated to support normal nuclear processing and transport of both rRNA and mRNA. The system contains cytosol but not (NH4)2SO4 or other non-physiological components. Evidence is presented for cytosol factors which stimulate ribosomal, and to a lesser degree, non-ribosomal RNA synthesis.

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Oestriol-stimulated synthesis of ribonucleic acid in the uterus of the immature rat.

Project description:Oestradiol-17beta and oestriol both sequentially stimulate the synthesis of heterogeneous nuclear RNA and rRNA in vivo. However, the stimulation by oestradiol-17beta, particularly of rRNA synthesis, is very much greater than that elicited by oestriol.

| S-EPMC1183877 | biostudies-other

Effect of allylisopropylacetamide on Nuclear Ribonucleic Acid synthesis in rat liver.

Project description:The porphyrogenic drug allylisopropylacetamide, a potent inducer of delta-aminolaevulinate synthetase, specifically increases nucleoplasmic RNA synthesis in rat liver. The drug-mediated increase in nucleoplasmic RNA synthesis is blocked by cycloheximide and haemin, which also inhibit the enzyme induction.

| S-EPMC1165390 | biostudies-other

The effect of ethionine on ribonucleic acid synthesis in rat liver.

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