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PubMed1982

Binding of cytochrome C to liver mitochondria and microsomes after inhibition of protein biosynthesis with cycloheximide and chloramphenicol.

The inhibition of extramitochondrial biosynthesis with cycloheximide considerably reduces the binding of exogenous cytochrome c to rat liver mitochondria. Tracing the binding of the exogenous cytochrome c to liver mitochondria and microsomal membranes in the period after application of cycloheximide (from 0 to 120 min) shows that the inhibitor evokes inhibition of the binding at the beginning of the period tested and afterwards there is a tendency to reaching the initial level. The above mentioned changes are more pronounced in the case of binding of cytochrome c to mitochondrial membranes. Chloramphenicol does not influence the number of high-affinity cytochrome c binding sites on the mitochondrial membranes. The cytochrome c--mitochondrial membrane complexes become less stable after inhibition of the mitochondrial protein biosynthesis with chloramphenicol.

Animals↗
PubMed1982

Degradation of proteins synthesized in the presence of cycloheximide in normal and transformed fibroblasts.

Monolayer cultures of 3T3 and WI-38 fibroblasts were pulse labeled with radioactive leucine in the presence of cycloheximide. The rate of protein degradation was measured and compared with that of SV-40 virus transformed cells. The results clearly show that normal and transformed cells have essentially identical rates of degradation of proteins synthesized in the presence of cycloheximide. These findings indicate that the lower rates of protein degradation observed in some transformed cells is not a general rule.

Animals↗
PubMed1978

Effect of cycloheximide on glucagon-induced autophagy. Quantitative examinations on hepatocytes in the rat.

By means of fine structural evaluation, a highly significant inhibitory effect of cycloheximide (20 mg/kg) on glucagon-induced autophagy is demonstrated in rat hepatocytes, which also presumably affects physiologic autophagic activities. Contrary to other investigators, we think in vivo global inhibition experiments using cycloheximide as an inhibitor of protein synthesis do not provide substantial information on the origin of the segregating membranes.

Animals↗
PubMed1984

[Intraenterocytic metabolism and blood uptake of caproic and oleic acids in control and actidione-cycloheximide-treated rats].

Intestinal absorption of capric and oleic acids from the intestinal lumen into mesenteric portal vein blood was investigated in control and actidione-cycloheximide-treated rats using the ex vivo vascular perfusion technique. The measurement of 14C-labeled lipids, 14CO2 and 14C-labeled acid-soluble products was simultaneously carried out with blood collected at 5-min intervals for 60 min. The enterocyte catabolism of capric and oleic acids, one of which was preferentially absorbed via the blood, has been interpreted by the different processes of absorption. The greater enterocyte catabolic activity with capric acid, compared to oleic acid, could be related to the slight affinity of FABP Z for this medium-chain fatty acid and also to lack of capric acid esterification; a non-negligible fraction of this fatty acid actually disappeared from the lumen and was catabolized into the enterocyte at an early stage of its absorption. The actidione-cycloheximide treatment affected oleic acid absorption via the blood to a greater degree than that of capric acid. But it modified both intestinal blood absorption and the catabolism of the two fatty acids in the same manner.

Animals↗
PubMed1983

Effect of cycloheximide and of anti-C3 Fab' on the intrinsic synthesis and secretion of lysosomal enzyme and of complement components by guinea-pig peritoneal macrophages.

Without any additional stimulus, the lysosomal enzyme N-acetyl-beta-D-glucosaminidase (beta-GLU) is secreted immediately from starch gel induced guinea-pig peritoneal macrophages. A more than three-fold increase of the total enzyme activity in the course of 3 days and the reversible inhibition of this enzyme increase by cycloheximide prove the synthesis of beta-GLU. The synthesis rate of beta-GLU remains rather constant after the second day, despite rapid cell death in the same culture period which could be explained by heterogeneity of the macrophage population. Cycloheximide immediately inhibits secretion of C3 whereas inhibition of beta-GLU secretion is only observed after a lag phase of 24 h. Secretion of factor D and of beta-GLU is not altered if secreted C3 is totally neutralized by the addition of anti-C3 Fab' to macrophage cultures. Thus, endogenous C3 as well as its endogenously generated fragments do not influence these macrophage functions. In the same cultures with anti-C3 Fab', conversion of secreted factor B into its fragments is inhibited as indicated by the detection of functional B activity. These results indicate that the secretion of factor D and of beta-GLU is also independent of endogenous B-derived fragments such as Bb. Finally, the detection of functional B in cultures with anti-C3 Fab' proves that C3b is required for factor B activation. The apparent interaction of secreted C3 and factors D and B in regular macrophage cultures suggests the constant formation of the labile C3 convertase C3bBb of the alternative pathway.

Acetylglucosaminidase↗
PubMedDate not supplied

[Effect of the combined action of metronidazole and cycloheximide on protein synthesis and tumor regression following irradiation].

A radiosensitizing effect of metronidazole on a tumor was enhanced by a small dose of cycloheximide. Metronidazole caused a considerable inhibition of the protein synthesis during the first six hours following irradiation. Cycloheximide, in the dose used, did not enhance the effect of metronidazole on the postirradiation protein synthesis.

Animals↗
PubMedDate not supplied

[Biological activity of tRNA in rat liver during cycloheximide-blocked translation].

The aminoacylation of tRNA was investigated with respect to protein synthesis in the rat liver. No correlation was found between the 85-90% inhibition of protein synthesis 2 h after cycloheximide injection and aminoacylation level of some tRNAs both in vivo and in vitro. A decrease in aminoacylation (28%) was established only for lysine. During the recovery phase of protein synthesis 12 and 24 h after cycloheximide treatment the aminoacylation maximal level of mixture with 14C amino acids, 14C leucine, 14C glutamic acid was unchanged.

Animals↗
PubMed1978

[Stimulation of nuclear membrane components and DNA biosynthesis in rat liver cells after inhibition of translation with cycloheximide].

After a drastic inhibition of protein synthesis (95%) in rat liver by cycloheximide (0.2-0.4 mg/100 g of body weight) the recovery and subsequently prolonged marked stimulation of proteins, lipids and DNA were found. The correlation of nuclear membrane proteins and lipids synthesis was observed in a recovery and stimulation phases. Nuclear DNA synthesis increases after the stimulation biosynthesis of nuclear membrane components (36-40 hours after cycloheximide injection). The changes of a phospholipid composition and structure organisation of nuclear membrane hydrophobic zones (by spin probe) were found in stimulated DNA synthesis (48-60 hours).

Animals↗
PubMed1993

Endo-lysosomal acidification in Dictyostelium discoideum amoebae. Effects of two endocytosis inhibitors: caffeine and cycloheximide.

Fluid-phase endocytosis (pinocytosis) is highly active in amoebae of the cellular slime mould Dictyostelium discoideum as it provides an efficient entry of nutrients in axenic strains. Detailed kinetic analyses were conducted using fluorescein-labeled dextran (FITC-dextran) as fluid-phase marker and pH probe. Cells were first pulsed with FITC-dextran during a short period then chased by suspension in probe-free medium. Chase kinetics were characterized by a lag phase of about 40 min before pseudo-first order FITC-dextran efflux and thus reflected the progression of the probe cohort through the various endosomal compartments along the endosomal pathway. Temporal evolution of endo-lysosomal pH showed a rapid acidification (T1/2 approximately 10 min) to pH 5.0 followed by an increase up to pH 6.2 to 6.3. The effects of cycloheximide and caffeine, two inhibitors of endocytosis in Dictyostelium amoebae, on the evolution of endosomal pH during fluid-phase endocytosis, have been investigated. Cycloheximide fully blocked the cellular transit of FITC-dextran but acidification of endo-lysosomal compartments still took place. Caffeine increased endo-lysosomal pH, probably as a consequence of an elevation of cytosolic [Ca2+]. Furthermore, it allowed the functional identification of a caffeine-insensitive terminal segment of the endocytic pathway. It corresponded to a recycling, postlysosomal compartment at pH 6.2 to 6.3 with an apparent volume of 160 microns 3/amoebae.

Animals↗
PubMed1976

Selective inhibition of protein synthesis initiation in Saccharomyces cerevisiae by low concentrations of cycloheximide.

We have previously determined the amounts of time required to complete various macromolecular synthetic processes needed for induction of allophanate hydrolase in Saccharomyces cerevisiae. This information provided a means of testing, in vivo, an early hypothesis suggesting that cycloheximide inhibited the initiation as well as elongation steps of protein synthesis. Our data suggest that initiation of protein synthesis in yeast may be inhibited by low concentrations of cycloheximide which do not significantly affect polypeptide chain elongation.

Allophanate Hydrolase↗
PubMed1976

The dynamics of production and the sensitivity to cycloheximide and actinomycin D of interferon-inducing and interferon messenger RNA.

In the process of virus-induced interferon production, two kinds of RNA appear in the cells. One of them induces production by the recipient cells of interferon with the species-specificity of the latter cells (interferon-inducing RNA), and the other is translated by the recipient cells pre-treated with actinomycin D into interferon with the species-specificity of the donor cells of RNA (interferon mRNA). The interferon-inducing RNA appears 20-30 minutes after virus induction and shows maximal activity after 1 hour. Its formation is not influenced by cycloheximide or actinomycin D. This RNA is assumed to be a transcriptive intermediate form of viral RNA. Interferon mRNA appears in the cells 1 hour after virus induction and shows maximal activity after 6-8 hours. Its synthesis is inhibited by cycloheximide and actinomycin D.

Animals↗
PubMed1975

[The effect of puromycin, nalidixic acid, and cycloheximide acetylcholinesterase purified from Electrophorus electricus L].

The action of puromycin, nalidixic acid and cycloheximide on acetylcholinesterase has been studied using an "electrophoretically pure" preparation. Results obtained show that these well known inhibitors of protein synthesis have an inhibitory effect on acetylcholinesterase activity. The inhibitory action exercised by puromycin and nalidixic acid is of a mixed inhibition type, similar to the one seen when decamethonium and d-tubocurarine are used as inhibitory agents. Cycloheximide acts in a non competitive way on the enzyme activity.

Cycloheximide↗
PubMed1975

[Effect of puromycin, nalidixic acid and cycloheximide on neuromuscular transmission].

The action of puromycin, nalidixic acid and cycloheximid on neuromuscular transmission has been assayed using diaphragm-phrenic nerve preparation from rat. The results demonstrate that all antibiotics used, reversibly blodk neuromuscular transmission. Cycloheximid seems to act presynaptically by inhibiting acetylcholine release from nerve terminal. Puromycin and nalidixic acid act as curare-like agents. They seem to compete with acetylcholine for fixation at the cholinergic receptor.

Animals↗
PubMed1993

Regulation of IFN-gamma and tumor necrosis factor-alpha expression in vivo. Effects of cycloheximide and cyclosporine in normal and lipopolysaccharide-treated mice.

Despite accumulating information about cytokine expression in vitro, relatively little is known about the regulation and biologic relevance of these mediators in vivo. In order to study the effects of inhibition of protein synthesis and cyclosporine in vivo, we made use of systemically administered LPS, which induces the expression of a variety of cytokines. The expression of IFN-gamma and TNF-alpha mRNA in normal and LPS-treated mice was examined by Northern blot analysis and amplification using the polymerase chain reaction. IFN-gamma activity was monitored using the biologic end point of MHC induction. TNF-alpha activity in serum was assessed using a L929 cytotoxicity assay. Messenger RNA for IFN-gamma and TNF-alpha could not be reliably detected by Northern analysis in spleens or kidneys of normal mice. After treatment with cycloheximide, a protein synthesis inhibitor, IFN-gamma and TNF-alpha mRNA could be detected in both sites in otherwise normal mice. The level of both IFN-gamma and TNF-alpha mRNA increased after LPS, although the temporal patterns of expression were different. The concurrent administration of cycloheximide led to marked superinduction of both cytokine mRNA levels. Similar effects were seen in T cell-deficient nude mice, suggesting that these responses are T cell independent. Cyclosporin A blocked induction of IFN-gamma in a dose dependent manner, but failed to significantly inhibit TNF-alpha mRNA or protein expression. Thus at least part of the immunosuppressive effect of cyclosporin A in vivo may be caused by its ability to inhibit the expression of certain cytokine genes, as has been found in vitro systems. However, the cellular target for this effect may extend to cell populations other than T cells.

Animals↗
PubMed1993

Inhibition of brain protein synthesis by cycloheximide does not affect formation of long-term memory in honeybees after olfactory conditioning.

The honeybee forms a long-term memory in different training situations that lasts for a lifetime, but the cellular mechanisms of long-term memory formation are not known. We analyzed the dependency of long-term memory on the de novo brain protein synthesis. The protein synthesis inhibitor cycloheximide was injected via the median ocellus directly into the brain. 3H-leucine incorporation into brain proteins was inhibited by > 95% for > 3 hr. The time of protein synthesis inhibition was prolonged by a second injection of the same dose. Worker honeybees were conditioned to an olfactory stimulus at different times before and after injection. The proboscis extension response (PER) of bees restrained in tubes was classically conditioned with sugar water applied first to the antennae followed by feeding (unconditioned stimulus) paired with odor presentation (conditioned stimulus). The bees were tested by presenting the odor alone at different times up to 24 hr after injection. No significant reduction in the probability of the conditioned response in cycloheximide-treated bees was found when compared to the Ringer-injected controls in 4 series of experiments. Since protein synthesis was inhibited between 7 hr pre- and 7 hr postconditioning without affecting the formation of long-term memory, a possible role of de novo protein synthesis in the formation of long-term memory after olfactory conditioning of the PER is not supported by these experiments.

Animals↗
PubMed1977

[Action of cycloheximide on RNA synthesis and the formation of structures in the Venezuelan equine encephalomelitis virus].

The studies showed that the effect of cycloheximide on reproduction of the virus of Venezuelan equine encephalitis (VEE) depended on the time of the antibiotic administration. When the antibiotic was added 3--5 hours after the inoculation (after formation of the virus RNA-polymerase), accumulation of virus RNA and 60--100 S virus structures was observed in the cells, while virus nucleotides and infection virus did not practically form. The 60--100 S structures included the cell proteins. They were resistant to EDTA and their swimming density in cesium chloride was 1.3--1.4 gm/cm3, it was characteristic of RNA of a non-ribosomic nature. According to these properties 60--100 S structures may be classified as belonging to the "hybrid" RNA analogous to the RNA complexes of VEE virus with the cell proteins. Probably addition of cycloheximide provided conditions in the infected cells for increase of the "hybrid", structural pool since the synthesis of the structural virus proteins was suppressed.

Carbon Radioisotopes↗
PubMedDate not supplied

[Changes in monoamine oxidase activity and catecholamine content in the tissues of guinea pigs saturated with ascorbic acid under the influence of actinomycin D, tetracycline and cycloheximide].

A short-time saturation of guinea pigs with ascorbic acid (100 mg per 1 kg of weight every hour for 5 h) causes its accumulation in the adrenals and blood, an increase in the monoaminooxidase activity in the liver and in the content of adrenaline in the adrenals. The content of noradrenaline in the liver and brain does not change. Inhibitors of protein synthesis, actinomycin D, tetracycline and cycloheximide, have a different effect on the increase in the monoaminooxidase activity evoked by introduction of ascorbic acid: tetracycline blocks the increase in the enzyme activity, actinomycin D has no effect on it. Cycloheximide introduced against a background of chronic saturation of guinea pigs with ascorbic acid also blocks the increase in the monoaminooxidase activity in the liver mitochondria.

Adrenal Glands↗
PubMed1977

The effect of chloramphenicol and cycloheximide on the activity of enzyme "markers" of mitochondrial substructures of the rat liver.

Chloramphenicol and cycloheximide exert in vivo inhibitory effects on the synthesis of mitochondrial enzymes. Choloramphenicol action results in a significant decrease of the activity of enzymes being the "markers" of all submitochondrial structures including that of the outer membrane. This suggests that chloramphenicol affects biosynthesis of of "assembly protein" on mitochondrial ribosomes and thus affects incorporation of proteins, wherever they are synthesized, into the structure of the mitochondrion as a functional entity. The effect of cycloheximide depends markedly on the concentration of the inhibitor and on the time of its administration. The differences in sensitivity of examined enzymes to the drug are probably related to their differential turnover.

Animals↗