作者: Masatoshi Ichihara , Takahiko Hara , Heejung Kim , Takashi Murate , Atsushi Miyajima
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摘要: Oncostatin M (OSM) and leukemia inhibitory factor (LIF ) are members of the interleukin-6 (IL-6) subfamily cytokines that use a common signal transducer gp130. Human OSM (hOSM) LIF share functional high-affinity receptor is composed gp130 β subunit (LIFRβ). A second for hOSM was recently found to be formed by subunit. However, nature murine (mOSM) its receptors has remained unknown. Using cloned mOSM cDNA, we produced recombinant studied biological activity structure. Murine hematopoietic cell lines M1 DA1.a, an embryonic stem line CCE, Ba/F3 transfectants expressing LIFRβ responded (mLIF equally well, while these cells only at 30-fold 100-fold higher concentration than those mLIF hOSM. In contrast, NIH3T3 mOSM, but not Scatchard plot analyses showed bound with low-affinity (kd = 2.8 4.2 nmol/L) binding affinity did increase in presence LIFRβ. 660 pmol/L), whereas bind all. These results indicate unlike hOSM, do same receptor, delivers signals through specific complex. Further studies mice will define physiological roles OSM.