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      • Oncostatin M signaling
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      • Oncostatin M (OSM) is a member of the multifunctional cytokine interleukin 6 (IL6) - type cytokine family. It is mainly produced in activated T lymphocytes, macrophages, monocytes, neutrophils, and microglial cells. OSM signaling is initiated by the interaction of the cytokine to either: the type I LIFR-gp130 receptor complex, or to the type II OSMR-gp130 receptor (O’Hara et al). The major downstream signaling pathways that are activated in OSM signaling are JAK/STAT, Ras/Raf/MAPK and PI3K pathways (Halfter, Halfter, Stross, Brantley). As the receptors lack intrinsic tyrosine kinase activity, associated JAKs (JAK1, JAK2, JAK3 and TYK2) phosphorylate OSM receptor complex and STATs (STAT1, STAT3, STAT5A, STAT5B, STAT6) (O’Hara, Fritz, Migita, Hintzen). Phosphorylated STATs form homodimeric complexes (STAT1, STAT3, STAT5B) or heterodimeric complex (STAT1-STAT3) and translocate to the nucleus. Once inside nucleus STAT proteins bind to regulatory elements in the promoter of OSM-responsive genes and regulate the gene expression (O’Hara, Halfter, Halfter, Hintzen). Alternatively, OSM induced phosphorylation of PTPN11, GRB2, SHC1, Ras/Raf molecules can bring about the activation of ERK1/2 signaling module (O’Hara). Oncostatin M -through ERK1/2 signaling module induces the phosphorylation of CEBPB, both CEBPB and EGR1 stimulates the transcription of genes involved in lipid metabolism (Zhang). Although OSM also causes induced phosphorylation in MAPK family members (MAPK8/9/14) the functional importance of this is at present not well understood (O’Hara, Li). OSM mediated signaling cascade is negatively regulated by JAK1 inhibition by SOCS3 and STAT3 inhibition by PIAS3 (Stross, Brantley, Chung). OSM also induces the activation of caspase family members (CASP3, CASP7, CASP9) through the JAK2 module and regulates apoptosis (Auernhammer, Tiffen, Chipoy). In osteosarcoma cells, OSM mediates apoptosis through a less understood STAT5B signaling module (Chipoy).
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