Inhibition of protein synthesis stimulates the transcription of human beta-interferon genes in Chinese hamster ovary cells.

Ringold, Gordon M.; Dieckmann, B; Vannice, James L.; Trahey, Meg; McCormick, Frank

doi:10.1073/pnas.81.13.3964

Cited by 116 publications

(63 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, the combination of 22K plus cycloheximide gave positive signals in all experiments, regardless of the technique of analysis. In accordance with reports in the literature (Ringold et al, 1984;Maroteaux et al, 1983;Tan & Berthold, 1977) that cycloheximide by itself can activate the interferon-/~ system, we occasionally found detectable IFN-/~ mRNA in cells treated with cycloheximide alone. However, this occurred in only two out of eight experiments and the levels induced were much lower than those obtained with the combination of 22K plus cycloheximide.…”

Section: Discussionsupporting

confidence: 79%

Stimulation of Fibroblast Interferon Production by a 22K Protein from Human Leukocytes

Damme

Opdenakker

Billiau

et al. 1985

Journal of General Virology

View full text Add to dashboard Cite

SUMMARYWe have studied the appearance of human interferon-fl (HuIFN-fl) as well as its mRNA in cells treated with a protein, 22K factor, isolated from the culture supernatant of mitogen-stimulated human peripheral blood leukocytes. By itself 22K was found to be unable to induce production of significant amounts of HuIFN-fl protein. However, when aided by treatment with cycloheximide or cycloheximide and actinomycin D (superinduction), 22K caused increases in production ranging from 3-to 20-fold, depending on the cells (diploid or MG-63 osteosarcoma) and the induction schedule. Cells treated with 22K alone produced small amounts of HuIFN-fl mRNA, which was only detectable with a highly sensitive method. In combination with cycloheximide, 22K induced levels of mRNA detectable with less sensitive methods as well. These experiments provide further support for the concept that the antiviral activity of 22K is mediated by its ability to stimulate transcription of the HuIFN-fl gene in cells.

show abstract

Section: Discussionsupporting

confidence: 79%

Stimulation of Fibroblast Interferon Production by a 22K Protein from Human Leukocytes

Damme

Opdenakker

Billiau

et al. 1985

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…Light-induced cytoplasmic protein synthesis could mediate plastid transcription by changes in the protein composition of the RNA polymerase ( 19), synthesis of sequence-specific DNA-binding factors ( 17), light-induced changes in local template topology (15) or the light-induced synthesis of prokaryotic-like sigma factors ( 19 4) and from illuminated seedlings incubated without (lanes 2 and 5, control) or with Tagetin (lanes 3 and 6) were fractionated, electrophoresed, and autoradiographed as described in Figure 4. Legends same as Figure 4 (2,9,26). In most of these cases, the models that were presented emphasized that inhibition of protein synthesis would decrease the concentration of a labile factor, which acts to inhibit expression of select genes.…”

Section: Light-induced Plastid Transcriptionmentioning

confidence: 99%

Regulation of Light-Induced Chloroplast Transcription and Translation in Eight-Day-Old Dark-Grown Barley Seedlings

Klein¹

1991

Plant Physiol.

View full text Add to dashboard Cite

Plastid transcription and translation are light-activated in 8-day-old dark-grown barley (Hordeum vulgare L.) seedlings. Pretreatment of dark-grown seedlings with cycloheximide (inhibitor of cytoplasmic protein synthesis) abolished the activation of rbcL, psbA, and psaA-B transcription by light. In contrast, inhibition of plastid protein synthesis by chloramphenicol stimulated lightactivated transcription of rbcL, psbA, and psaA-B. Light-induced transcription of the plastid genome occurred normally in the chlorophyll-deficient mutant xan-J". These results suggest that although the light-induced activation of plastid transcription is modulated by cytoplasmic and organellar protein synthesis, transcriptional activation is not dependent on the absorption of light by protochlorophyllide or the attainment of photosynthetic competence. In addition, plastid translation increased dramatically when 8-day-old dark-grown seedlings were illuminated and activation was dependent on cytoplasmic protein synthesis. Blockage of light-activated plastid transcription by Tagetin treatment (inhibitor of plastid RNA polymerase) did not attenuate the activation of plastid translation by light. These results suggest that while light simultaneously activates plastid transcription and translation, the rapid burst in plastid protein synthesis is due mainly to cytoplasmic-denved changes that regulate the rate of translation of pre-existing mRNAs.

show abstract

“…Histone mRNAs (38,40), c-myc mRNA (2,5,21), p53 mRNA (5), and c-myb mRNA (44), for example, all have been shown to be stabilized in the presence of inhibitors of protein synthesis. The induction of gene transcription by protein synthesis inhibitors is less common but has been reported for a limited number of genes (7,11,33). In particular, the P-and y-actin genes in mouse embryo cells have been shown to be induced by epidermal growth factor and superinduced by epidermal growth factor in the presence of cycloheximide (7).…”

mentioning

confidence: 99%

Mitogens and protein synthesis inhibitors induce ornithine decarboxylase gene transcription through separate mechanisms in the BC3H1 muscle cell line.

Olson¹,

Spizz²

1986

Mol. Cell. Biol.

View full text Add to dashboard Cite

Ornithine decarboxylase (ODCase), the rate-limiting enzyme in polyamine biosynthesis, exhibits dramatic fluctuations in activity in response to a variety of hormones and growth factors and has been shown to be down-regulated during myogenesis. In the present study, the molecular mechanisms involved in expression of ODCase mRNA were examined in cells of the BC3H1 muscle line. Proliferating, undifferentiated Skeletal muscle differentiation involves the withdrawal of proliferating myoblasts from the cell cycle and their subsequent fusion to form multinucleated myotubes. Myogenesis is accompanied by the expression of a variety of musclespecific gene products involved in the specialized functions of the myofiber (25). During this time period, some genes encoding proteins associated with cell proliferation are down-regulated (8,26,32,41). Among the proteins that are deinduced during muscle differentiation is ornithine decarboxylase (ODCase), the rate-limiting enzyme in polyamine biosynthesis. Previous studies have shown that ODCase activity decreases dramatically at the time of myoblast fusion, suggesting that the down-regulation of this enzyme may play a central role in control of the onset of differentiation (8,41). In addition to its regulation during muscle development, ODCase has been shown to be rapidly induced in quiescent cells by a variety of hormones and growth factors (for review, see reference 34). ODCase is also regulated in a cell cycle-specific manner, with large increases in enzyme activity being required for progression of cells from the G1 to the S phase of the cell cycle (34). Despite the apparent importance of ODCase in the control of cell proliferation and possibly differentiation, the molecular mechanisms involved in regulation of ODCase gene expression remain to be determined.The BC3H1 nonfusing muscle cell line has been used as a model to study certain aspects of both smooth-muscle and skeletal-muscle differentiation (29-31, 35, 42 rapidly and do not express the muscle phenotype (20,(29)(30)(31). The removal of serum from the culture media results in the withdrawal of cells from the cell cycle and the induction of a variety of muscle-specific gene products. The accumulation of muscle-specific mRNAs can be rapidly reversed by reexposure of quiescent differentiated cells to serum (29,30) or to fibroblast growth factor (G. Spizz, D. Roman, A. Strauss, and E. Olson, J. Biol. Chem., in press).Previously, Olson et al. (30) reported that an mRNA encoding a polypeptide of Mr -50,000 was preferentially expressed in undifferentiated BC3H1 cells and was downregulated during differentiation. Because of its Mr and pattern of regulation, we considered the possibility that this mRNA might encode ODCase. In the present study, we have analyzed the molecular mechanisms involved in the regulation of ODCase mRNA expression during differentiation of BC3H1 cells. ODCase mRNA was expressed at relatively high levels in proliferating undifferentiated cells in media with 20% serum.

show abstract

Inhibition of protein synthesis stimulates the transcription of human beta-interferon genes in Chinese hamster ovary cells.

Cited by 116 publications

References 29 publications

Stimulation of Fibroblast Interferon Production by a 22K Protein from Human Leukocytes

Stimulation of Fibroblast Interferon Production by a 22K Protein from Human Leukocytes

Regulation of Light-Induced Chloroplast Transcription and Translation in Eight-Day-Old Dark-Grown Barley Seedlings

Mitogens and protein synthesis inhibitors induce ornithine decarboxylase gene transcription through separate mechanisms in the BC3H1 muscle cell line.

Contact Info

Product

Resources

About