Journal
JOURNAL OF NEUROIMMUNOLOGY
Volume 145, Issue 1-2, Pages 40-45Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jneuroim.2003.09.005
Keywords
interleukins; IL-18; cytokine receptors; EAE
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Interleukin (IL)-18, a member of the IL-1 family, is a key mediator of peripheral inflammation and host defense responses, and has been implicated in inflammatory and neurodegenerative diseases in the brain. IL-18 acts via a receptor complex that closely resembles that of IL-1, consisting of a ligand binding protein, IL-18Ralpha, and an accessory protein, IL-18Rbeta. Here, we describe the presence of a splice variant of IL-18Rbeta that is predicted to encode a truncated soluble protein, consisting of only the first immunoglobulin-like domain of IL-18Rbeta (EMBL/ Genbank accession number AJ550893). Both forms of IL-18Rbeta were expressed in rat cortex, striatum, hypothalamus, hippocampus, and also liver, and were detected in pure cultures of microglia, astrocytes and neurons. This novel splice variant is up-regulated rapidly in microglial cells by bacterial lipopolyssacharide (LPS). We propose that this putative truncated form of IL-18Rbeta is analogous to the soluble form of IL-1R accessory protein, and could act as an important regulator of IL-18 actions. (C) 2003 Elsevier B.V. All rights reserved.
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