
In order to understand the mechanism of proliferation and differentiation of leukemia cells, we investigate the relation between the cytoplasmic regions LIFR alpha-subunit and gp130 and the transcription activator Stat3 in human leukemic U937 cells.The cytoplasmic domain was each truncated from the LIFR alpha-subunit and gp130. The truncated forms of LIFR alpha-subunit(gp190EX) and gp130 (gp130EX) which can compete with the wild type receptor for binding to leukemia inhibitory factor (LIF) were expressed on the membrane of U937 cells. The level of Stat 3 and its phosphorylation were estimated by immunoblotting.The increased level of Stat3 and its decreased tyrosine phosphorylation were detected in each group of gp130EX and gp190EX as compared with that in the wild type receptor subunit group.The cytoplasmic domains of both LIFR alpha subunit and gp130 involve the induction of Stat3 phosphorylation in U937 cells.
STAT3 Transcription Factor, Membrane Glycoproteins, Leukemia Inhibitory Factor Receptor alpha Subunit, Receptors, OSM-LIF, Cell Differentiation, U937 Cells, Lysosomal Membrane Proteins, DNA-Binding Proteins, Antigens, CD, Lysosomal-Associated Membrane Protein 1, Cytokine Receptor gp130, Trans-Activators, Humans, Phosphorylation, Receptors, Cytokine, Cell Division
STAT3 Transcription Factor, Membrane Glycoproteins, Leukemia Inhibitory Factor Receptor alpha Subunit, Receptors, OSM-LIF, Cell Differentiation, U937 Cells, Lysosomal Membrane Proteins, DNA-Binding Proteins, Antigens, CD, Lysosomal-Associated Membrane Protein 1, Cytokine Receptor gp130, Trans-Activators, Humans, Phosphorylation, Receptors, Cytokine, Cell Division
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