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Institut fuer Physiologie und Experimentelle Pathophysiologie, Friedrich-Alexander Universitaet, 91054 Erlangen, Germany; and
* Institut fuer Anatomie und Zellbiologie, Justus-Liebig Universitaet, Giessen, Germany
1Correspondence: Institut fuer Physiologie und Experimentelle Pathophysiologie, Universitaetsstr. 17, D-91054 Erlangen, Germany. E-mail: kress{at}physiologie1.uni-erlangen.de
Interleukin 1ß (IL-1ß) is a proinflammatory cytokine that maintains thermal hyperalgesia and facilitates the release of calcitonin gene-related peptide from rat cutaneous nociceptors in vivo and in vitro. Brief applications of IL-1ß to nociceptive neurons yielded a potentiation of heat-activated inward currents (Iheat) and a shift of activation threshold toward lower temperature without altering intracellular calcium levels. The IL-1ß-induced heat sensitization was not dependent on G-protein-coupled receptors but was mediated by activation of protein kinases. The nonspecific protein kinase inhibitor staurosporine, the specific protein kinase C inhibitor bisindolylmaleimide BIM1, and the protein tyrosine kinase inhibitor genistein reduced the sensitizing effect of IL-1ß whereas negative controls were ineffective. RT-PCR and in situ hybridization revealed IL-1RI but not RII expression in neurons rather than surrounding satellite cells in rat dorsal root ganglia. IL-1ß acts on sensory neurons to increase their susceptibility for noxious heat via an IL-1RI/PTK/PKC-dependent mechanism.—Obreja, O., Rathee, P. K., Lips, K. S., Distler, C., Kress, M. IL-1ß potentiates heat-activated currents in rat sensory neurons: involvement of IL-1RI, tyrosine kinase, and protein kinase C.
Key Words: hyperalgesia • inflammation • cytokines • nociceptor
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