st-638 has been researched along with Leukemia--Erythroblastic--Acute* in 2 studies
2 other study(ies) available for st-638 and Leukemia--Erythroblastic--Acute
| Article | Year |
|---|---|
Synergistic induction of erythroid differentiation of mouse erythroleukemia (MEL) cells by inhibitors of topoisomerases and protein tyrosine kinases.
In vitro erythroid differentiation of mouse erythroleukemia (MEL) cells was induced by combinations of topoisomerase and protein kinase inhibitors. Neither inhibitor alone exhibited inducing activity. Although inhibitors of topoisomerases I and II were equally effective in the synergistic induction of erythroid differentiation, only inhibitors of tyrosine kinases, not of serine/threonine kinases, exhibited synergistic activity. The erythroid differentiation induced by the combination of topoisomerase and protein tyrosine kinase inhibitors was distinguished from that induced by typical erythroid inducing agents such as DMSO or HMBA by (1) earlier hemoglobin accumulation in the cells and (2) insensitivity to specific inhibitors (dexamethasone and sodium orthovanadate) of MEL cell differentiation. Topics: Acetamides; Amsacrine; Animals; Blotting, Western; Camptothecin; Cell Differentiation; Cinnamates; Dimethyl Sulfoxide; Hemoglobins; Leukemia, Erythroblastic, Acute; Mice; Mitomycin; Protein-Tyrosine Kinases; Sulfides; Topoisomerase I Inhibitors; Topoisomerase II Inhibitors; Tumor Cells, Cultured; Vanadates | 1992 |
Inhibitors for protein-tyrosine kinases, ST638 and genistein: induce differentiation of mouse erythroleukemia cells in a synergistic manner.
In order to investigate the biochemical nature of intracellular cascades leading to cellular differentiation in vitro, we examined the effect of inhibitors of protein phosphorylation on terminal erythroid differentiation of mouse erythroleukemia (MEL) cells. We have found that specific inhibitors of protein phosphorylation at tyrosine residues, ST638 and genistein, effectively induce differentiation in a synergistic manner with an agent which blocks DNA replication such as mitomycin C (MMC). Based upon these findings, the possible involvement of protein phosphorylation (and dephosphorylation) at tyrosine residues in differentiation is discussed. Topics: Animals; Cell Differentiation; Cell Line; Cinnamates; Drug Synergism; Flavonoids; Genistein; Globins; Isoflavones; Kinetics; Leukemia, Erythroblastic, Acute; Mice; Protein-Tyrosine Kinases; Sulfides; Transcription, Genetic | 1989 |