rdf:type |
|
lifeskim:mentions |
umls-concept:C0020792,
umls-concept:C0021764,
umls-concept:C0033684,
umls-concept:C0123771,
umls-concept:C0218229,
umls-concept:C0332120,
umls-concept:C1414557,
umls-concept:C1522642,
umls-concept:C1749467,
umls-concept:C1880022,
umls-concept:C1998793
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pubmed:issue |
14
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pubmed:dateCreated |
1997-5-8
|
pubmed:abstractText |
Interleukin-4 (IL-4) and interleukin-13 (IL-13) are structurally and functionally related cytokines which play an important role in the regulation of the immune response to infection. The functional similarity of IL-4 and IL-13 can be explained, at least in part, by the common components that form their cell surface receptors, namely the IL-4 receptor alpha-chain (IL-4Ralpha) and the IL-13 receptor alpha-chain (IL-13Ralpha). Soluble forms of the IL-4Ralpha have also been described and implicated in modulating the effect of IL-4. In this paper we describe the presence of a 45,000-50,000 Mr IL-13-binding protein (IL-13BP) in the serum and urine of mice. This protein binds IL-13 with a 100-300-fold higher affinity (KD = 20-90 pM) than does the cloned IL-13Ralpha (KD = 3-10 nM). In addition to this functional difference, the IL-13BP appears to be structurally and antigenically distinct from the IL-13Ralpha. Finally, unlike the cloned receptor, the IL-13BP acts as a potent inhibitor of IL-13 binding to its cell surface receptor, raising the possibility that it may be used to modulate the effects of IL-13 in vivo.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Il13ra1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-13,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-13 Receptor alpha1...,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-13,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/glutamyl endopeptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
|
pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
4
|
pubmed:volume |
272
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
9474-80
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9083087-Animals,
pubmed-meshheading:9083087-Antigens, CD,
pubmed-meshheading:9083087-Chromatography, Affinity,
pubmed-meshheading:9083087-Chromatography, Gel,
pubmed-meshheading:9083087-Cloning, Molecular,
pubmed-meshheading:9083087-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9083087-Glycosylation,
pubmed-meshheading:9083087-Interleukin-13,
pubmed-meshheading:9083087-Interleukin-13 Receptor alpha1 Subunit,
pubmed-meshheading:9083087-Interleukin-4,
pubmed-meshheading:9083087-Mice,
pubmed-meshheading:9083087-Molecular Weight,
pubmed-meshheading:9083087-Rabbits,
pubmed-meshheading:9083087-Receptors, Interleukin,
pubmed-meshheading:9083087-Receptors, Interleukin-13,
pubmed-meshheading:9083087-Receptors, Interleukin-4,
pubmed-meshheading:9083087-Serine Endopeptidases
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pubmed:year |
1997
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pubmed:articleTitle |
Identification, purification, and characterization of a soluble interleukin (IL)-13-binding protein. Evidence that it is distinct from the cloned Il-13 receptor and Il-4 receptor alpha-chains.
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pubmed:affiliation |
Walter and Eliza Hall Institute of Medical Research and the Cooperative Research Centre for Cellular Growth Factors, P.O. Royal Melbourne Hospital, Victoria 3050, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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