p67K kinase in different tissues and plasma of control and interferon-treated mice

Interferon-treated mouse cells show an enhanced level of protein kinase activity which is manifested by the phosphorylation of an endogenous 67,000-molecular weight protein (p67K kinase). This kinase activity can be assayed efficiently after its partial purification on poly(I) · poly(C)-Sepharose. We have previously shown that the p67K kinase is present in the liver, spleen and plasma (heparinized) of mice with high levels of circulating interferon. Here we confirm these results by treatment of mice with interferon and furthermore show that besides the liver and spleen, the level of p67K kinase is enhanced in several other tissues such as thymus, brain, pancreas, heart, and lung. The action of interferon in mice was further monitored by the assay of pppA(2′p5′A)n synthetase (2–5A synthetase) in different tissues. The level of 2-5A synthetase was enhanced several fold in the following tissues: heart, pancreas, thymus, liver, and spleen. The detection of 2–5A synthetase and p67K kinase activities in the different tissues of mice provides suitable markers for the response of each individual tissue toward treatment with interferon. The phosphorylated 67K protein (pp67K) from control and interferon-treated mouse L-929 cells and from the plasma and different tissues of control and interferontreated mice was characterized by two-dimensional gel electrophoresis. The isoelectric point (pl) of pp67K from the different tissues and L-929 cells was 8 to 8.5. On the other hand the pI of pp67K from the plasma had a range of 7.5 to 8. These results indicated that the presence of p67K kinase in the plasma of mice is not due to lysis of tissue cells.