![]() The activities of eIF4E are regulated at multiple levels, one of which is through its phosphorylation at Serine 209 by the mitogen-activated protein kinase-interacting kinases (MNKs, including MNK1 and MNK2). Translation initiation is thought to be the rate-limiting step in protein synthesis, and the mRNA 5′ cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) is a pivotal factor that initiates translation. Western blots were performed to determine the effects of rapamycin on MNK1 protein levelsĭysregulated protein synthesis is frequently involved in oncogenesis and cancer progression. HL60 cells were exposed to rapamycin at the indicated concentrations for 24 h. ( d ) Cell cycle inhibition does not influence MNK1 expression in myeloid cells. ATRA-exposed cells no longer had detectable MNK1 protein after a 12 h exposure to cycloheximide, but nonexposed NB4 cells still had detectable MNK1 levels after 24 h. Then, cycloheximide was added and MNK1 protein levels were monitored by Western blotting. ( c ) To analyse the effects of ATRA on MNK1 protein half-life, NB4 cells were exposed to ATRA (10 À 6 M ) for 24 h. Cells were harvested after 24 h and Western blot analysis for MNK1 protein was performed. ( b ) In a dose–response study, NB4 cells were exposed to different concentrations of ATRA. For densitometry analyses, we used an INTAS camera (Epichem 3 Darkroom) and the programme GelPro Analyser (1D-Gel ToolBar). The bar diagram on the right indicates the average MNK1 protein level of the two independent experiments. Cells were harvested at the indicated time points and analysed for MNK1 protein levels to determine the protein half-life. ( a ) U937 PMT control cells or U937-PML-RAR a cells were zinc-induced for 24 h before cycloheximide was added in order to block protein synthesis. MNK1 protein half-life regulation by PML-RAR a and ATRA. ![]()
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