pubmed-article:11248074 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C0383327 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C0205216 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C0765701 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C1446680 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:11248074 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
pubmed-article:11248074 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:11248074 | pubmed:dateCreated | 2001-3-15 | lld:pubmed |
pubmed-article:11248074 | pubmed:abstractText | IL-18 can be considered a proinflammatory cytokine mediating disease as well as an immunostimulatory cytokine that is important for host defense against infection and cancer. The high-affinity, constitutively expressed, and circulating IL-18 binding protein (IL-18BP), which competes with cell surface receptors for IL-18 and neutralizes IL-18 activity, may act as a natural antiinflammatory as well as immunosuppressive molecule. In the present studies, the IL-18 precursor caspase-1 cleavage site was changed to a factor Xa site, and, after expression in Escherichia coli, mature IL-18 was generated by factor Xa cleavage. Mature IL-18 generated by factor Xa cleavage was fully active. Single point mutations in the mature IL-18 peptide were made, and the biological activities of the wild-type (WT) IL-18 were compared with those of the mutants. Mutants E42A and K89A exhibited 2-fold increased activity compared with WT IL-18. A double mutant, E42A plus K89A, exhibited 4-fold greater activity. Unexpectedly, IL-18BP failed to neutralize the double mutant E42A plus K89A compared with WT IL-18. The K89A mutant was intermediate in being neutralized by IL-18BP, whereas neutralization of the E42A mutant was comparable to that in the WT IL-18. The identification of E42 and K89 in the mature IL-18 peptide is consistent with previous modeling studies of IL-18 binding to IL-18BP and explains the unusually high affinity of IL-18BP for IL-18. | lld:pubmed |
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pubmed-article:11248074 | pubmed:language | eng | lld:pubmed |
pubmed-article:11248074 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11248074 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11248074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11248074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:11248074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11248074 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11248074 | pubmed:month | Mar | lld:pubmed |
pubmed-article:11248074 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:11248074 | pubmed:author | pubmed-author:DinarelloC... | lld:pubmed |
pubmed-article:11248074 | pubmed:author | pubmed-author:RubinsteinMM | lld:pubmed |
pubmed-article:11248074 | pubmed:author | pubmed-author:MOER ERE | lld:pubmed |
pubmed-article:11248074 | pubmed:author | pubmed-author:NovickDD | lld:pubmed |
pubmed-article:11248074 | pubmed:author | pubmed-author:YoonD YDY | lld:pubmed |
pubmed-article:11248074 | pubmed:author | pubmed-author:ReznikovL LLL | lld:pubmed |
pubmed-article:11248074 | pubmed:author | pubmed-author:AzamTT | lld:pubmed |
pubmed-article:11248074 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11248074 | pubmed:day | 13 | lld:pubmed |
pubmed-article:11248074 | pubmed:volume | 98 | lld:pubmed |
pubmed-article:11248074 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11248074 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11248074 | pubmed:pagination | 3304-9 | lld:pubmed |
pubmed-article:11248074 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:11248074 | pubmed:meshHeading | pubmed-meshheading:11248074... | lld:pubmed |
pubmed-article:11248074 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11248074 | pubmed:articleTitle | Site-specific mutations in the mature form of human IL-18 with enhanced biological activity and decreased neutralization by IL-18 binding protein. | lld:pubmed |
pubmed-article:11248074 | pubmed:affiliation | University of Colorado Health Sciences Center, Denver, CO 80262, USA. | lld:pubmed |
pubmed-article:11248074 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11248074 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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