TY - JOUR
T1 - Identification of a truncated IL-18Rβ mRNA: A putative regulator of IL-18 expressed in rat brain
AU - Andre, Ralph
AU - Wheeler, Rachel D.
AU - Collins, Peter D.
AU - Luheshi, Giamal N.
AU - Pickering-Brown, Stuart
AU - Kimber, Ian
AU - Rothwell, Nancy J.
AU - Pinteaux, Emmanuel
PY - 2003/12
Y1 - 2003/12
N2 - 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. © 2003 Elsevier B.V. All rights reserved.
AB - 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. © 2003 Elsevier B.V. All rights reserved.
KW - Cytokine receptors
KW - EAE
KW - IL-18
KW - Interleukins
U2 - 10.1016/j.jneuroim.2003.09.005
DO - 10.1016/j.jneuroim.2003.09.005
M3 - Article
C2 - 14644029
SN - 0165-5728
VL - 145
SP - 40
EP - 45
JO - Journal of neuroimmunology
JF - Journal of neuroimmunology
IS - 1-2
ER -