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At least 577 records · Page 32Linked to original sources
PubMed1989

Effects of indeloxazine hydrochloride on cognitive disturbance in cycloheximide-treated mice.

The effects of indeloxazine hydrochloride [(+/-)-2-[(inden-7-yloxy)methyl]morpholine hydrochloride] on cognitive disturbance in mice subjected to cycloheximide have been examined. Indeloxazine ameliorated cycloheximide-induced amnesia in mice, indicating a facilitatory effect of this drug on cerebral functions. Piracetam, Cahopantenate, dihydroergotoxine and viloxazine did not show significant effect on the amnesia. These results suggest that indeloxazine possesses a wider pharmacological profile than piracetam, Cahopantenate, dihydroergotoxine and viloxazine in anti-amnesic activities.

Animals↗
PubMed1964

CYCLOHEXIMIDE: ASPECTS OF INHIBITION OF PROTEIN SYNTHESIS IN MAMMALIAN CELLS.

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.

Amino Acids↗
PubMed1966

Puromycin and cycloheximide: different effects on hippocampal electrical activity.

Abstract. Mice were injected in the temporal region of the brain with cycloheximide or puromycin; both agents markedly inhibit protein synthesis in the brain. Recordings of electrical activity were made in the hippocampal region 5 hours after injection of these drugs. The amplitude and frequency observed in records from mice injected with cycloheximide were indistinguishable from those injected with saline alone. Records from puromycin-injected mice were strikingly abnormal. This finding may contribute to the differences in behavioral effects of intracerebral injections of the two inhibitors of protein synthesis studied.

Animals↗
PubMed1967

Failure of cycloheximide to induce tyrosine transaminase in the anesthetized rat.

It was recently reported that cycloheximide, an inhibitor of protein synthesis, induces tyrosine transaminase in the liver of adrenalectomized rats. We have been unable to confirm this effect in the anesthetized animal and our data show that cycloheximide inhibits the induction caused by hydrocortisone in adrenalectomized rats or by stress in intact rats.

Adrenalectomy↗
PubMed1979

Cycloheximide-dependent reversion of human cells transformed by MSV and chemical carcinogen.

The protein synthesis inhibitor cycloheximide, at a concentration of 0.08 microgram per milliliter, induced flat morphology within 24 to 48 hours and low saturation density in human osteosarcoma cells transformed by Kirsten murine sarcoma virus (Ki-MSV) or N-methyl-N' nitro-N-nitrosoguanidine. Removal of the protein synthesis inhibitor caused both transformed cells to revert to the transformed phenotype. The demonstration of cell-surface antigens, cross-reacted with antiserums induced by extracts of both types of transformed human cells, was dependent on the presence or absence of cycloheximide in the culture medium. The results show that protein synthesis is required to maintain the transformed state in virally or chemically transformed human cells.

Antigens, Surface↗
PubMed1980

Binding of cycloheximide to ribosomes from wild-type and mutant strains of Saccharomyces cerevisiae.

Cycloheximide bound to cytoplasmic (80S) ribosomes of the yeast Saccharomyces cerevisiae with an association constant (Ka) of 2.0 (+/- 0.5) x 10(7) M-1. The number of binding sites found per ribosome was between 0.4 and 0.6; it was reduced by high-salt treatment of ribosomes 60S particles prepared in the presence of high salt had a lower affinity (Ka: 5.5 [+/- 0.5] x 10(6) M-1) than did 80S ribosomes, but a greater proportion of particles (0.8) were able to bind. No specific binding to 40S subunits was observed. The addition of supernatant fractions (S100, high-salt wash fraction) increased the number of binding sites found per 80S ribosome up to 0.8, leaving the association constant unchanged. In contrast, the affinity of 60S subunits was enhanced to a Ka value of 3.5 x 10(-7) M-1 by the addition of supernatant fractions, whereas the number of binding sites stayed constant. A model to explain these facts is proposed. 80S ribosomes, as well as 60S subunits of strain cy32, which is highly resistant to cycloheximide and altered in ribosomal protein L29 (18), showed a drastically reduced affinity for the drug (Ka values of 2.0 x 10(6) M-1).

Binding Sites↗
PubMed1973

Differences in the growth of Aspergillus fumigatus on cycloheximide media at three temperatures.

Cycloheximide (up to 0.4 g/liter) was significantly more inhibitory to the growth of three isolates of Aspergillus fumigatus at 23 C than at 37 or 45 C. Preincubation of the media for 7 days at 45 C did not alter the inhibitory effect of the cycloheximide at 23 C. Neither mutation nor adaptation in the fungus seems to be the reason for its growth on the antibiotic at the higher temperature. The mechanism for the differences in sensitivity as related to temperature of incubation cannot be explained at this time.

Aspergillus fumigatus↗
PubMed1979

Biotyping of Chlamydia psittaci based on inclusion morphology and response to diethylaminoethyl-dextran and cycloheximide.

Strains of Chlamydia psittaci from cattle, sheep, pigs, mice, guinea pigs, rabbits, cats, and parrots were subdivided based on their biological characteristics. Chlamydiae grown in the yolk sac of chicken embryos were used to infect L cell monolayers. The host cells were infected without further treatment or treated with diethylaminoethyl-dextran, cycloheximide, or both. The following criteria were used for biotyping the strains: the morphology of the inclusions and time after infection at which they appeared, the effect of chlamydial multiplication on the host cell cytoskeleton, and the change in the number of cells infected in response to diethylaminoethyl-dextran and cycloheximide. These properties were determined for 29 strains of C. psittaci. Based on the results, the strains were placed into eight biotypes.

Animals↗
PubMed1981

Use of cycloheximide to study independent lipid metabolism of Chlamydia trachomatis cultivated in mouse L cells grown in serum-free medium.

A system for measuring chlamydial lipid synthesis was developed with mouse L cells grown in serum-free modified Waymouth 752/l medium in a shaker culture. Host lipid synthesis was reduced approximately 90% when cells were incubated for 24 h in medium containing cycloheximide (2 micrograms/ml). Lipid metabolism was monitored by measuring the incorporation of [3H]isoleucine into the total lipid of normal and infected cells. The results suggested that lipid synthesis of Chlamydia trachomatis lymphogranuloma venereum (LGV-404L) was not inhibited by cycloheximide treatment when the chlamydiae were grown in L cells, whereas host lipid synthesis was inhibited. Chlamydial lipid metabolism began about 6 to 12 h after infection when the noninfectious reticulate body was found and continually increased until the beginning of the appearance of intracellular infectious elementary bodies at 24 to 30 h.

Animals↗
PubMed1974

Cycloheximide-resistant glycosylation in L cells infected with Chlamydia psittaci.

L cells (mouse fibroblasts), uninfected and infected with the meningopneumonitis strain of Chlamydia psittaci, were labeled with [(14)C]glucosamine, and their membranous organelles were separated by isopycnic equilibrium centrifugation of whole cell homogenates on discontinuous sucrose gradients. Glycosylation of host membranes continued throughout the infection. Cycloheximide almost completely inhibited glycosylation in uninfected L cells, but it only partially inhibited the process in infected host cells. Cycloheximide-resistant glycosylation of membrane fractions with [(14)C]glucosamine increased as the infection proceeded and was probably due to the action of chlamydial enzymes. Modification of host membranes by glycosylation may play a role in the natural development of chlamydial infections.

Animals↗
PubMed1977

Ribosomal suppressors and antisuppressors in Podospora anserina: resistance to cycloheximide.

Informational suppressors and antisuppressors have been previously isolated in Podospora anserina, and a range of exclusively genetic arguments have led to the assumption that they correspond to ribosomal mutations. An in vivo and in vitro comparison of the effect of the ribosomal inhibitor cycloheximide on wildtype and mutant strains described in this paper confirms the ribosomal hypothesis for at least some mutants. Indeed, the four mutants in the AS3 gene were cycloheximide resistant, and their ribosomes were found to be resistant when analyzed by polyuridyl-directed polyphenylalanine systhesis. On the other hand, ribosomes from two su 1 mutants were hypersensitive to the drug.

Ascomycota↗
PubMed1978

Does cycloheximide-induced loss of phosphate uptake activity in Neurospora crassa reflect rapid turnover?

Addition of cycloheximide to Neurospora crassa germlings growing in liquid medium caused an exponential loss of phosphate uptake activity (half-life, ca. 2 h). No loss of activity resulted when germlings were resuspended, at the time of cycloheximide addition, in medium of a substantially lower phosphate concentration. It is concluded that the phosphate uptake systems are not subject to rapid turnover.

Cycloheximide↗
PubMed1983

Incorporation of radioactivity from amino acids in the presence of cycloheximide demonstrates gluconeogenic activity in Mucor rouxii.

Mucor rouxii cells induced for gluconeogenesis incorporated radioactivity from [14C]glutamic acid into trichloroacetic acid-precipitable material in the presence of 200 micrograms of cycloheximide per ml. This metabolic capacity was repressed by hexoses and required amino acids for induction. These results suggest that the incorporation of amino acids in the presence of cycloheximide represents gluconeogenic activity with associated polysaccharide synthesis.

Amino Acids↗
PubMed1986

Cloning in Saccharomyces cerevisiae of a cycloheximide resistance gene from the Candida maltosa genome which modifies ribosomes.

We have previously shown that cycloheximide resistance can be induced in a strain of Candida maltosa by modifying ribosomes (M. Takagi, S. Kawai, Y. Takata, N. Tanaka, M. Sunairi, M. Miyazaki, and K. Yano, J. Gen. Appl. Microbiol. 31:267-275, 1985). The present paper describes the cloning of the gene involved in this resistance (designated RIM-C for ribosome modification by cycloheximide) by using a host-vector system of Saccharomyces cerevisiae.

Candida↗
PubMed1995

Translation and M1 double-stranded RNA propagation: MAK18 = RPL41B and cycloheximide curing.

MAK18 is one of nearly 30 chromosomal genes of Saccharomyces cerevisiae necessary for propagation of the killer toxin-encoding M1 double-stranded RNA satellite of the L-A double-stranded RNA virus. We have cloned and sequenced MAK18 and find that it is identical to RPL41B, one of the two genes encoding large ribosomal subunit protein L41. The mak18-1 mutant is deficient in 60S subunits, which we suggest results in a preferential decrease in translation of viral poly(A)-deficient mRNA. We have reexamined the curing of M1 by low concentrations of cycloheximide (G. R. Fink and C. A. Styles, Proc. Natl. Acad. Sci. USA 69:2846-2849, 1972), which is known to act on ribosomal large subunit protein L29. We find that when M1 is supported by L-A proteins made from the poly(A)+ mRNA of a cDNA clone of L-A, cycloheximide does not decrease the M1 copy number, consistent with our hypothesis.

Cloning, Molecular↗
PubMed1966

Effects of cycloheximide and puromycin on synthesis of simian virus 40 T antigen in green monkey kidney cells.

Gilden, R. V. (Wistar Institute, Philadelphia, Pa.), and R. I. Carp. Effects of cycloheximide and puromycin on synthesis of simian virus 40 T antigen in green monkey kidney cells. J. Bacteriol. 91:1295-1297. 1966.-Synthesis of the simian virus 40 (SV40) T antigen in primary African green monkey kidney cells was abolished when cycloheximide was added up to 10 hr postinfection. In contrast, puromycin, another inhibitor of protein synthesis, did not suppress antigen production. The basis of this differential effect was the inability of puromycin to inhibit protein synthesis in the cells used. This was shown by the failure of the drug to depress the incorporation of labeled amino acid into protein and also failure to inhibit poliovirus synthesis. The puromycin preparation used was very effective in inhibiting poliovirus synthesis in HeLa cells. Thus, appearance of the SV40 T antigen is dependent on protein synthesis in infected cells.

Animals↗
PubMed1968

Separation of protein synthesis in meningopneumonitisgent from that in L cells by differential susceptibility to cycloheximide.

Cycloheximide had no effect on multiplication of the meningopneumonitis agent in L cells in concentrations which eliminated over 90% of the protein synthesis in the host cells. Infected L cells treated with cycloheximide, however, incorporated labeled amino acids into the trichloroacetic acid-insoluble fraction. This incorporation was attributed to the biosynthetic activity of the meningopneumonitis agent. Synthesis of meningopneumonitis protein was abolished by chloramphenicol and chlortetracycline, inhibitors of bacterial protein synthesis, at concentrations which did not inhibit protein synthesis in L cells. Protein synthesis in the meningopneumonitis agent was sustained at a high rate when the host cells remained viable and declined as the L cells died. Overall host protein synthesis was not inhibited by multiplication of the meningopneumonitis agent.

Bacterial Proteins↗
PubMed1977

Early detection of chlamydial inclusions combining the use of cycloheximide-treated McCoy cells and immunofluorescence staining.

Detection of Chlamydia trachomatis inclusions only 21 h after a specimen reaches the laboratory has been achieved by the combined use of cycloheximide-treated McCoy cells and immunofluorescence staining. Moreover, cells exposed to cycloheximide were more sensitive for detecting chlamydial inclusions than those pretreated by irradiation, since larger numbers of inclusions were found in the former cells. The application of this rapid and sensitive method allows a diagnosis of chlamydial infection to be made before antibiotic therapy is started. In this way, it should enable the treatment of nonspecific genital infections to be placed on a more rational basis.

Cell Line↗