The bcr‐c‐abl tyrosine kinase activity is extinguished by TPA in K562 leukemia cells

FEBS Letters

Alitalo, Riitta¹ 

[1] Transplantation Laboratory and Department of Virology, University of Helsinki, Haartmaninkatu 3, 00290 Helsinki, Finland

关键词: Chronic myeloid leukemia;    Oncoprotein;    Philadelphia chromosome;    Phosphotyrosine;    Tyrosine kinase;    CML;    chronic myeloid leukemia;    DMSO;    dimethyl sulfoxide;    TBRS;    tumor-bearing rabbit serum;    TPA;    12-O-tetradecanoyl phorbol-13-acetate;   

DOI  :  10.1016/0014-5793(87)80389-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tyrosine kinase activity is associated with the transforming potential of several oncogenes. Human chronic myeloid leukemia (CML) cells and cell lines have been shown to contain an active bcr-c-abl p210 tyrosine kinase as a consequence of the Philadelphia chromosomal translocation. In the present work the activity of the c-abl and c-src oncogene-encoded tyrosine kinases was investigated during phorbol diester (TPA) induced differentiation of the K562 CML cells. The high tyrosine kinase activity of p210 ^bcr -c- ^abl is strongly reduced during the initial 24 h of TPA treatment. In contrast, the activity of the c-src tyrosine kinase is not changed. No change occurs in the expression of the c-abl-specific RNAs during this period. Following the reduction of bcr-c-abl kinase activity, cell proliferation is arrested and megakaryoblastic antigens appear on the cells. Sodium butyrate caused a slight decrease in growth rate and of bcr-c-abl kinase activity during erythroid differentiation whereas no changes in c-src or c-abl tyrosine kinase activities were seen in DMSO-treated control cells.

【 授权许可】

Unknown