Abstract
THERE have been a number of reports1–10 which indicate that an experimentally induced elevation in the intracellular level of adenosine-3′,5′-monophosphate (cyclic AMP) in mouse neuroblastoma cells induces and increases the expression of many differentiated functions that are characteristic of the mature neurone. The irreversibility of cyclic AMP-induced “differentiation”3 was attributed to the increased level of proteins which bind cyclic AMP thereby protecting the newly synthesised cyclic nucleotide from hydrolysis11,12. However, the mechanisms by which cyclic AMP initiates the observed morphological1–3 and biochemical3–10 alterations remain unclear since the activity of cyclic AMP-dependent protein kinase did not change in differentiated cells13. We have investigated the phosphorylation of specific proteins in control and ‘differentiated’ neuroblastoma cells. We report here that the cyclic AMP-dependent phosphorylation of a specific protein in the cytosol of ‘differentiated’ cells increased while the cyclic AMP-independent phosphorylation of another protein in this cell fraction decreased. These selective alterations may represent intermediate steps in a series of events which ultimately lead to the expression of differentiated functions.
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EHRLICH, Y., BRUNNGRABER, E., SINHA, P. et al. Specific alterations in phosphorylation of cytosol proteins from differentiating neuroblastoma cells grown in culture. Nature 265, 238–240 (1977). https://doi.org/10.1038/265238a0
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DOI: https://doi.org/10.1038/265238a0
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