Increased efficiency of translation of ornithine decarboxylase mRNA in mitogen‐activated lymphocytes
Open Access
- 1 December 1987
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 170 (1-2) , 87-92
- https://doi.org/10.1111/j.1432-1033.1987.tb13670.x
Abstract
Ornithine decarboxylase (ODC) mRNA was elevated ninefold by 6 h following concanavalin A (ConA) stimulation of bovine lymphocytes. Comparison of the increases in ODC mRNA and ODC activity revealed a fivefold discrepancy, which is consistent with a change in efficiency of translation of ODC mRNA. In resting cells, 45% of the total ODC mRNA was associated with particles sedimenting at about 40 S, and therefore was not translated. The untranslated ODC mRNA in resting cells could be completely shifted into polysomes by a 15-min treatment of the cells with appropriate concentrations of cycloheximide. In activated cells, the proportion of ODC mRNA in untranslated material was reduced to 18%. This shift in distribution of ODC mRNA occurred between 6 h and 12 h following mitogen stimulation with no increase in the cellular level of this message. The rate of synthesis of ODC protein was found in increase twofold between 6 h and 12 h, paralleling the increase in the amount of ODC mRNA associated with polysomes. Thus, in this time frame, a decrease in the amount of untranslated ODC mRNA with a corresponding increase in the amount associated with polysomes leads to an increase in the biosynthesis of ODC with no change in the cellular level of the message. These changes in translational efficiency were not observed with actin mRNA.This publication has 38 references indexed in Scilit:
- Posttranscriptional regulation of ornithine decarboxylase activityJournal of Cellular Physiology, 1986
- Ornithine decarboxylase inhibitors increase the cellular content of the enzyme: Implications for translational regulationBiochemical and Biophysical Research Communications, 1985
- Insulin‐stimulated protein synthesis in adipocytesEuropean Journal of Biochemistry, 1985
- The effect of serum, EGF, PGF2α and insulin on S6 phosphorylation and the initiation of protein and DNA synthesisCell, 1982
- Preferential Utilization of Phosphorylated 40‐S Ribosomal Subunits during Initiation Complex FormationEuropean Journal of Biochemistry, 1982
- Rapid Alterations in Initiation Rate and Recruitment of Inactive RNA Are Temporally Correlated with S6 PhosphorylationEuropean Journal of Biochemistry, 1982
- Inhibition of polypeptide synthesis by a factor isolated from ribosomes of resting human lymphocytesFEBS Letters, 1980
- Inhibition of initiation of protein synthesis in rabbit reticulocyte lysates by a factor present in lymphocyte cytoplasmFEBS Letters, 1978
- Initiation of protein synthesis during lymphocyte stimulationNature, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970