Abstract
AbstractWe investigated the expression, degree of phosphorylation, and activation of the proto-oncogene c-kitproduct before and after stimulation with the c-kitligand in a human factor-dependent myeloid leukemia cell line, M07E. The culture supernatant of the BALB/3T3 fibroblast cell line, which contains the ligand for the murine c-kitproduct, was found to stimulate proliferation of the M07E cell line in a dose-dependent manner. The proliferation was significantly inhibited by a tyrosine kinase inhibitor, genistein. An immunoblot technique with a monoclonal antibody specific for phosphotyrosine, showed that there was rapid, dose-dependent tyrosine-phosphorylation of the c-kitproduct in response to murine c-kitligand. Furthermore, the murine c-kitligand increased autokinase activity of the c-kitproduct in vitro. Similar results were obtained with human stem cell factor (SCF), a recombinant human ligand for the c-kitproduct. These results suggest that the phosphorylation and activation of the c-kit product are involved in proliferative signals of some human leukemia cells, as well as of normal hematopoietic cells.
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