Abstract
The interleukin-6 (IL-6) family of cytokines and their receptors all require dimerization of one receptor subunit with gp130 to trans-duce an intracellular signal (for reviews see refs. 1 and 2). Leukemia inhibitory factor (LIFR) binds LW that is converted to high affinity binding by heterodimerization with gp130. Other ligands that use the LIFR are oncostatin M (OSM) and cardiotrophin-1 (CT-1). CT-1 utilizes LIFR although all the receptor components for CT-1 have not been elucidated (3), whereas OSM binds directly to gp130 and can use either LIFR (4) or another receptor (alternate OSMR; B. Mosley, personal communication) for dimerization and signal transduction. Ciliary neurotrophic factor (CNTF) also requires LIFR for biological activity, but first binds CNTF receptor (CNTFR) and this complex then interacts with LIFR and gp130 (5). Therefore, of the known ligands, the absence of LIFR would completely disrupt activity of LIF, CNTF, and CT-1, and would affect some OSM activity.
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