Abstract
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.
| Original language | English |
|---|---|
| Journal | J Neuroimmunol |
| Volume | 145( 1-2) |
| Publication status | Published - Dec 2003 |
Keywords
- immunology: Alternative Splicing
- Amino Acid Sequence
- Animals
- immunology: Astrocytes
- Base Sequence
- cytology: Brain
- Cells, Cultured
- biosynthesis: Interleukin-18
- Male
- Mice
- immunology: Microglia
- Molecular Sequence Data
- biosynthesis: RNA, Messenger
- Rats
- Rats, Sprague-Dawley
- genetics: Receptors, Interleukin
- Sequence Deletion
- Solubility
- Support, Non-U.S. Gov't