Granulocyte-macrophage colony-stimulating factor stimulation results in phosphorylation of cAMP response element-binding protein through activation of pp90RSK.

摘要: Granulocyte-macrophage colony-stimulating factor (GM-CSF) activates several kinases and transcription factors through interaction with a heterodimeric receptor complex. We previously demonstrated that phosphorylation of the cyclic adenosine monophosphate (cAMP) response element-binding protein, CREB, occurs protein kinase A-independent pathway is required for GM-CSF‐ induced transcriptional activation immediate early gene, growth response-1 (egr-1). Recent reports indicate tyrosine can induce CREB pp90RSK. performed immune complex assays in human myeloid leukemic cell line, TF-1, which revealed GM-CSF pp90RSK within 5 minutes stimulation. Transfection kinase-defective expression plasmid statistically significant decrease 2116 CAT/egr-1 promoter construct to GMCSF. Furthermore, pp90RSK, egr-1 GM-CSF‐treated cells was inhibited by presence inhibitor, PD98059. In this study, we report induces activating an MEKdependent signaling pathway. (Blood. 2000;95:2552-2558)