Identification of a truncated IL-18Rβ mRNA: a putative regulator of IL-18 expressed in rat brain

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 ligan...

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Bibliographic Details
Published in:Journal of neuroimmunology 2003-12, Vol.145 (1), p.40-45
Main Authors: Andre, Ralph, Wheeler, Rachel D., Collins, Peter D., Luheshi, Giamal N., Pickering-Brown, Stuart, Kimber, Ian, Rothwell, Nancy J., Pinteaux, Emmanuel
Format: Article
Language:English
Subjects:
Alternative Splicing - immunology
Amino Acid Sequence
Animals
Astrocytes - immunology
Astrocytes - metabolism
Base Sequence
Brain - cytology
Brain - immunology
Brain - metabolism
Cells, Cultured
Cytokine receptors
EAE
IL-18
Interleukin-18 - biosynthesis
Interleukin-18 - metabolism
Interleukin-18 Receptor beta Subunit
Interleukins
Male
Mice
Microglia - immunology
Microglia - metabolism
Molecular Sequence Data
Rats
Rats, Sprague-Dawley
Receptors, Interleukin - genetics
Receptors, Interleukin - isolation & purification
Receptors, Interleukin - physiology
RNA, Messenger - biosynthesis
Sequence Deletion
Solubility
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Summary: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-18Rα, and an accessory protein, IL-18Rβ. Here, we describe the presence of a splice variant of IL-18Rβ that is predicted to encode a truncated soluble protein, consisting of only the first immunoglobulin-like domain of IL-18Rβ (EMBL/Genbank accession number AJ550893). Both forms of IL-18Rβ 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-18Rβ is analogous to the soluble form of IL-1R accessory protein, and could act as an important regulator of IL-18 actions.
ISSN:0165-5728
1872-8421
DOI:10.1016/j.jneuroim.2003.09.005