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Differentiation of Myeloid Cells is Accompanied by Increased Levels of pp60c-src Protein and Kinase Activity

Connie E. Gee, James Griffin, Leandro Sastre, Linda J. Miller, Timothy A. Springer, Helen Piwnica-Worms and Thomas M. Roberts
Proceedings of the National Academy of Sciences of the United States of America
Vol. 83, No. 14 (Jul. 15, 1986), pp. 5131-5135
Stable URL: http://www.jstor.org/stable/27875
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Differentiation of Myeloid Cells is Accompanied by Increased Levels of pp60c-src Protein and Kinase Activity
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Abstract

We have detected a significant increase in the levels of pp60c-src kinase activity associated with the differentiation of myeloid cell lines HL-60 and U-937. The induction of pp60c-src kinase activity becomes apparent ≈ 14 hr after the addition of phorbol 12-myristate 13-acetate and increases 20-fold by 72 hr. The enhanced kinase activity can be accounted for by elevated levels of c-src protein in the differentiated cells. When nonleukemic bone marrow cells were examined, myeloid progenitor cells exhibited a low level of pp60c-src kinase activity. As these cells are allowed to differentiate in culture, the resulting adherent monocytes are as high in pp60c-src kinase activity as HL-60 cells induced to differentiate into monocytes. A strong correlation is found between the levels of pp60c-src kinase activity and the degree of monocytic differentiation of the cells from patients with acute myeloid leukemia. Our findings suggest that the activation of pp60c-src kinase activity is a normal physiological event associated with myeloid differentiation.

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