Alterations in Translational Control Mechanisms in Friend Erythroleukemic Cells During DMSO Induced Differentiation

Koch, Gebhard; Weber, Carsten; Bilello, J. A.

doi:10.1007/978-3-642-67057-2_37

Cited by 5 publications

(4 citation statements)

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“…However, ouabain is a relatively poor inducer compared with DMSO in wild-type ouabain-sensitive cells (Bernstein et al, 1976). Since ouabain is known to inhibit protein synthesis in intact cells Garry et al, 19791, the induction of terminal differentiation by ouabain may also point to the importance of the inhibition of protein synthesis during the commitment phase as proposed by previous data from our laboratory Koch et al, 1979Koch et al, , 1980. Inhibition of the initiation of protein synthesis could trigger differentiation in Friend cells either by the preferential inhibition of a Friend virus coded or induced protein, or amplification of translational control favoring the synthesis of differentiation specific proteins Bilello et al, 1980).…”

Section: Discussionmentioning

confidence: 78%

“…Ostertag, Heinrich-Pette-Institut fur Experimentelle Virologie, Hamburg, West Germany, and maintained in culture in our laboratory since 1975 Koch et al, 1979Koch et al, , 1980. The cells were grown in suspension cultures in Joklik minimal essential medium + 20 mM N-2-hydroxyethylpiperazine-N-2-eth anesulfonic acid (HEPES; pH 7.4) supplemented with 10% fetal calf serum (Boehringer).…”

Section: Cell Culturesmentioning

confidence: 99%

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A reduction in the activity of the NA⁺, K⁺ ‐pump in dimethylsulfoxide‐treated friend erythroleukemia cells is not due to partial inactivation of the NA⁺, K⁺ ‐ATPase

Schaefer

Munter

Geck

et al. 1984

Journal Cellular Physiology

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Treatment of Friend-erythroleukemia cells with 1.5% dimethylsulfoxide (DMSO) caused a decrease in ouabain sensitive 86Rb+-uptake beginning six to seven hours after DMSO addition indicating a reduced function of the Na+, K+-pump. However, analysis of the ouabain sensitive 86Rb+-uptake after Na+-preloading of the cells as well as measurements on the Na+, K+-ATPase activity in isolated membrane fragments revealed that no inhibition of the Na+, K+-ATPase occurred during the first 12 hours. On the contrary the Na+, K+-ATPase activity was initially enhanced and then returned to control levels during the early phase of induction by DMSO. On the other hand, 22Na+-transport into DMSO-treated cells was reduced similar to the ouabain sensitive 86Rb+ uptake in cells without Na+ preloading. The piretanide sensitive 86Rb+-uptake, due to the Na+, K+, 2Cl - cotransport system was inhibited after seven hours exposure to DMSO. Some three hours after DMSO addition the incorporation of 35S-methionine into proteins began to decrease, which was accompanied with or followed by a reduction in the methionine uptake of DMSO treated cells. Membrane-potential-dependent tetraphenylphosphonium cation uptake was not altered relative to the controls in the first 12 hours following DMSO addition. These results suggest that the reduced activity of the Na+, K+-pump in Friend cells after DMSO exposure is not due to inhibition of the Na+, K+-ATPase, but most probably due to a smaller Na+-influx, which results from inhibition of Na+-cotransport processes (amino acid uptake, Na+, K+, 2Cl - cotransport system).

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Section: Discussionmentioning

confidence: 78%

Section: Cell Culturesmentioning

confidence: 99%

A reduction in the activity of the NA⁺, K⁺ ‐pump in dimethylsulfoxide‐treated friend erythroleukemia cells is not due to partial inactivation of the NA⁺, K⁺ ‐ATPase

Schaefer

Munter

Geck

et al. 1984

Journal Cellular Physiology

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“…Induction of Friend cell differentiation results in early changes in membrane transport (17,20), in the agglutinability of Friend cells by lectins (19), and in increased viscosity of the membrane hydrocarbon layer (18). The membrane transport changes may be directly related to differentiation induction through a mechanism that would induce an alteration in-the ionic conditions which would favorthe preferential translation of RNA species with higher affinity for polysomes (21). Hypertonic treatment of mammalian cells was shown to induce these changes in RNA utilization (16,21).…”

Section: Resultsmentioning

confidence: 99%

“…The membrane transport changes may be directly related to differentiation induction through a mechanism that would induce an alteration in-the ionic conditions which would favorthe preferential translation of RNA species with higher affinity for polysomes (21). Hypertonic treatment of mammalian cells was shown to induce these changes in RNA utilization (16,21).…”

Section: Resultsmentioning

confidence: 99%

Erythroid differentiation and commitment in rat erythroleukemia cells with hypertonic culture conditions.

Yamaguchi¹,

Kluge²,

Ostertag³

et al. 1981

Proc. Natl. Acad. Sci. U.S.A.

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Friend virus-transformed mouse erythroleukemia (FLC) (1-3), chemically transformed rat erythroleukemia cells (RLC) (4,5), and human erythroid cells of leukemic origin (6) can grow in tissue culture permanently as paraproerythroblasts. These cells can be induced to differentiate if they are exposed to chemical substances such as dimethyl sulfoxide (Me2SO) (1) or hexamethylenebisacetamide (HMBA) (7), to hormones (8), or to inhibitors of ion transport (9). There are three phases of cell differentiation of transformed erythroid cells (10): (a) the precommitment phase, (b) the time ofcommitment, and (c) terminal differentiation. The precommitment phase is reversible; removal of the inducer in this phase does not evoke the loss of proliferative capacity, nor does it lead to an increase in terminally differentiating benzidine-staining cells (B+) in the cell population, both being characteristics of terminal differentiation which leads to loss of proliferative capacity (11-13).Accumulation of the inducing substances within the cells requires considerable time (13,14). Removal of the inducer, which is necessary to study the timing of commitment, decreases the inducer concentration within the cell at a similarly slow rate. Lower concentrations of inducers are known to induce commitment at exactly the same time as optimal inducer concentrations (11). Commitment thus may still occur after removal of inducer. This would introduce uncertainties in measuring the timing of commitment if commitment were caused by a direct interaction ofan intracellular target with the inducer. The exact timing of the commitment event should be more accurate with inducing conditions that do not involve chemical inducers.We show in this paper that optimal induction of RLC, but not of FLC, can be obtained by such conditions-namely, a change in tonicity of the medium. The osmotic pressure ofthe culture medium was determined with a Knauer pressure osmometer.Detection ofHemoglobin. Heme in the cells was stained with benzidine (8). Hemoglobin-containing cells (Hb+) were detected by use of the indirect fluorescein-labeled antibody staining method. Cell smears were prepared and fixed for 5 min at 20°C with methanol/acetone, 1:10 (vol/vol). Anti-rat Hb antiserum obtained by immunization ofrabbits was allowed to react with the fixed cells. Fluorescein isothiocyanate-conjugated goat anti-rabbit IgG antiserum (Miles; fluorescein/protein ratio = 4.1) was used as the second antibody. Cells were then observed and scored by fluorescence microscopy.Measurement of Cell Volume. Cells in suspension were photographed (x4000) at different times of incubation and their diameter was determined. The approximate cell volume was calculated by assuming the cell to be spherical. In each experiment the mean volume of 100 cells was determined. The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. RESULTS

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Biosynthesis, Modification and Processing of Viral Polyproteins

Koch

Bilello

et al. 1982

Protein Biosynthesis in Eukaryotes

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Alterations in Translational Control Mechanisms in Friend Erythroleukemic Cells During DMSO Induced Differentiation

Cited by 5 publications

References 11 publications

A reduction in the activity of the NA⁺, K⁺ ‐pump in dimethylsulfoxide‐treated friend erythroleukemia cells is not due to partial inactivation of the NA⁺, K⁺ ‐ATPase

A reduction in the activity of the NA⁺, K⁺ ‐pump in dimethylsulfoxide‐treated friend erythroleukemia cells is not due to partial inactivation of the NA⁺, K⁺ ‐ATPase

Erythroid differentiation and commitment in rat erythroleukemia cells with hypertonic culture conditions.

Biosynthesis, Modification and Processing of Viral Polyproteins

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Alterations in Translational Control Mechanisms in Friend Erythroleukemic Cells During DMSO Induced Differentiation

Cited by 5 publications

References 11 publications

A reduction in the activity of the NA+, K+ ‐pump in dimethylsulfoxide‐treated friend erythroleukemia cells is not due to partial inactivation of the NA+, K+ ‐ATPase

A reduction in the activity of the NA+, K+ ‐pump in dimethylsulfoxide‐treated friend erythroleukemia cells is not due to partial inactivation of the NA+, K+ ‐ATPase

Erythroid differentiation and commitment in rat erythroleukemia cells with hypertonic culture conditions.

Biosynthesis, Modification and Processing of Viral Polyproteins

Contact Info

Product

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A reduction in the activity of the NA⁺, K⁺ ‐pump in dimethylsulfoxide‐treated friend erythroleukemia cells is not due to partial inactivation of the NA⁺, K⁺ ‐ATPase

A reduction in the activity of the NA⁺, K⁺ ‐pump in dimethylsulfoxide‐treated friend erythroleukemia cells is not due to partial inactivation of the NA⁺, K⁺ ‐ATPase