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rdf:type |
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lifeskim:mentions |
umls-concept:C0020792,
umls-concept:C0205245,
umls-concept:C0666963,
umls-concept:C1167231,
umls-concept:C1511545,
umls-concept:C1514562,
umls-concept:C1880022,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2003941
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pubmed:issue |
12
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pubmed:dateCreated |
2003-12-9
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pubmed:abstractText |
Steady state mRNA levels in various human tissues reveal that the proinflammatory cytokine IL-18 is constitutively and ubiquitously expressed. However, limited IL-18R alpha-chain (IL-18Ralpha) expression in tissues may restrict ligand-acting sites and contribute to a specific response for IL-18. To study the IL-18R complex, [(125)I]IL-18 was studied for binding to the cell surface receptors of IL-18-responsive NK and macrophagic KG-1 cells. After cross-linking, [(125)I]IL-18 formed three IL-18R complexes with sizes of approximately 93, 160, and 220 kDa. In KG-1 cells, Scatchard analysis revealed the presence of 135 binding sites/cell, with an apparent dissociation constant (K(d)) of 250 pM; in NK cells, there were 350 binding sites per cell with an apparent K(d) of 146 pM. Each domain of extracellular IL-18Ralpha was cloned and individually expressed in Escherichia coli. An mAb specifically recognized the membrane-proximal third domain; this mAb blocked IL-18-induced IFN-gamma production in NK cells. Furthermore, deletion of the membrane-proximal third domain of IL-18Ralpha prevented the formation of IL-18R ternary complex with IL-18R beta-chain. The present studies demonstrate that the biologically active IL-18R complex requires the membrane-proximal third Ig-like domain in IL-18Ralpha for the formation of IL-18R ternary complex as well as for signal transduction involved in IL-18-induced IFN-gamma in NK cells.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/IL18R1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-18,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-18 Receptor alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Iodine Radioisotopes,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-18
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
171
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6574-80
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:14662859-Cell Line,
pubmed-meshheading:14662859-Cell Line, Tumor,
pubmed-meshheading:14662859-Humans,
pubmed-meshheading:14662859-Immunoglobulins,
pubmed-meshheading:14662859-Interleukin-18,
pubmed-meshheading:14662859-Interleukin-18 Receptor alpha Subunit,
pubmed-meshheading:14662859-Iodine Radioisotopes,
pubmed-meshheading:14662859-Killer Cells, Natural,
pubmed-meshheading:14662859-Macromolecular Substances,
pubmed-meshheading:14662859-Membrane Proteins,
pubmed-meshheading:14662859-Organ Specificity,
pubmed-meshheading:14662859-Protein Binding,
pubmed-meshheading:14662859-Protein Structure, Tertiary,
pubmed-meshheading:14662859-Protein Subunits,
pubmed-meshheading:14662859-RNA, Messenger,
pubmed-meshheading:14662859-Receptors, Interleukin,
pubmed-meshheading:14662859-Receptors, Interleukin-18,
pubmed-meshheading:14662859-Sequence Deletion,
pubmed-meshheading:14662859-Structure-Activity Relationship
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pubmed:year |
2003
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pubmed:articleTitle |
Identification of a critical Ig-like domain in IL-18 receptor alpha and characterization of a functional IL-18 receptor complex.
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pubmed:affiliation |
University of Colorado Health Sciences Center, Denver, CO 80262, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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