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Oncostatin M (OSM) is a member of the interleukin-6 cytokine family and regulates eg. gene activation, cell survival, proliferation and differentiation. OSM binds to a receptor complex consisting of the ubiquitously expressed signal transducer gp130 and the ligand binding OSM receptor subunit, which is expressed on a specific subset of primary afferent neurons. In the present study, the effect of OSM on heat nociception was investigated in nociceptor-specific gp130 knock-out ( SNS-gp130 -/-  ) and gp130 floxed ( gp130 fl/fl  ) mice.  Subcutaneous injection of pathophysiologically relevant concentrations of OSM into the hind-paw of  C57BL6J   wild type  mice significantly reduced paw withdrawal latencies to heat stimulation. In contrast to  gp130 fl/fl   mice, OSM did not induce heat hypersensitivity  in vivo  in  SNS-gp130 -/-   mice. OSM applied at the receptive fields of sensory neurons in  in vitro  skin-nerve preparations showed that OSM significantly increased the discharge rate during a standard ramp-shaped heat stimulus. The capsaicin- and heat-sensitive ion channel TRPV1, expressed on a subpopulation of nociceptive neurons, has been shown to play an important role in inflammation-induced heat hypersensitivity. Stimulation of cultured dorsal root ganglion neurons with OSM resulted in potentiation of capsaicin induced ionic currents. In line with these recordings, mice with a null mutation of the TRPV1 gene did not show any signs of OSM-induced heat hypersensitivity  in vivo .  The present data suggest that OSM induces thermal hypersensitivity by directly sensitizing nociceptors via OSMR-gp130 receptor mediated potentiation of TRPV1.

Oncostatin M Induces Heat Hypersensitivity by gp130-Dependent Sensitization of TRPV1 in Sensory Neurons