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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1992-12-8
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pubmed:databankReference | |
pubmed:abstractText |
IL-1 beta is a potent modulator of immune and inflammatory responses. Murine IL-1 beta is initially synthesized as an inactive 33-kDa pro-molecule that is activated by proteolytic cleavage between Asp-117 and Val-118 to generate the 17-kDa mature IL-1 beta protein. This cleavage is catalyzed by a specific protease that has been designated the IL-1 beta converting enzyme (or IL-1 beta convertase). We have used a human IL-1 beta convertase cDNA to isolate murine convertase cDNA from a WEHI-3 library. These cDNA predicted that the murine convertase is a 402-residue protein. Overall, the murine convertase showed 71% nucleotide and 62% predicted amino acid sequence identity with the human convertase. Southern blot analysis of interspecific backcross mice indicated that the murine IL-1 beta convertase is encoded by a single copy gene located on murine chromosome 9. The murine convertase showed broad constitutive expression, being detected in mononuclear phagocyte and T lymphocyte cell lines as well as in spleen, heart, brain, and adrenal glands. The expression of the murine convertase in mononuclear phagocytes was up-regulated by treatment with LPS or rIFN-gamma. These studies establish that the IL-1 beta convertase is an evolutionarily conserved, widely expressed enzyme that can be regulated at a pretranslational level.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
149
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3254-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1431103-Amino Acid Sequence,
pubmed-meshheading:1431103-Animals,
pubmed-meshheading:1431103-Base Sequence,
pubmed-meshheading:1431103-Cloning, Molecular,
pubmed-meshheading:1431103-Endopeptidases,
pubmed-meshheading:1431103-Female,
pubmed-meshheading:1431103-Interferon-gamma,
pubmed-meshheading:1431103-Interleukin-1,
pubmed-meshheading:1431103-Lipopolysaccharides,
pubmed-meshheading:1431103-Macrophages,
pubmed-meshheading:1431103-Mice,
pubmed-meshheading:1431103-Mice, Inbred Strains,
pubmed-meshheading:1431103-Molecular Sequence Data,
pubmed-meshheading:1431103-RNA, Messenger,
pubmed-meshheading:1431103-Up-Regulation
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pubmed:year |
1992
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pubmed:articleTitle |
Molecular cloning of the murine IL-1 beta converting enzyme cDNA.
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pubmed:affiliation |
Department of Internal Medicine, Washington University School of Medicine, St. Louis, MO 63110.
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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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