Abstract
To explore the modulation of phosphorylation and/or kinase activity of cellular proteins in interferon-α (IFN-α) treated Daudi cells, experiments were performed to determine the effect of IFN-α on the ability of cellular proteins to undergo autophosphorylation reaction in-vitro. Treatment of cells with IFN-α significantly inhibited the amount of phosphorylation of a nuclear protein of about 60 kDa [±3000 KDa, (P60)]. Results of phosphoamino acids analysis indicated that the nuclear P60 was a phosphotyrosine containing protein and was predominantly phosphorylated on threonine and serine in the absence of IFN-α. Treatment with IFN-α had a dual effect on relative phosphoamino acids content of P60: inhibited the phosphorylation on threonine residue, and enhanced the phosphorylation on serine and tyrosine residues. The nuclear P60 is not one of earlier described IFN-responsive signaling protein as it was not translocated from the cytosol.
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