Source:http://linkedlifedata.com/resource/pubmed/id/15331324
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-8-27
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pubmed:abstractText |
Mycobacterium leprae lipoprotein, LpK, induced IL-12 production from human monocytes. To determine the components essential for cytokine production and the relative role of lipidation in the activation process, we produced lipidated and non-lipidated truncated forms of LpK. While 0.5nM of lipidated LpK-a having N-terminal 60 amino acids of LpK produced more than 700pg/ml IL-12 p40, the non-lipidated LpK-b having the same amino acids as that of LpK-a required more than 20nM of the protein to produce an equivalent dose of cytokine. Truncated protein having the C-terminal 192 amino acids of LpK did not induce any cytokine production. Fifty nanomolar of the synthetic lipopeptide of LpK produced only about 200pg/ml IL-12. Among the truncated LpK, only LpK-a and lipopeptide stimulated NF-kB-dependent reporter activity in TLR-2 transfectant. However, when monocytes were stimulated with lipopeptide in the presence of non-lipidated protein, they produced IL-12 synergistically. Therefore, both peptide regions of LpK and lipid residues are necessary for efficient IL-12 production.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-12,
http://linkedlifedata.com/resource/pubmed/chemical/LpK protein, Mycobacterium leprae,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/TLR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0008-8749
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
229
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15331324-Bacterial Proteins,
pubmed-meshheading:15331324-Humans,
pubmed-meshheading:15331324-Interleukin-12,
pubmed-meshheading:15331324-Membrane Glycoproteins,
pubmed-meshheading:15331324-Membrane Proteins,
pubmed-meshheading:15331324-Mycobacterium leprae,
pubmed-meshheading:15331324-Receptors, Cell Surface,
pubmed-meshheading:15331324-Toll-Like Receptor 2,
pubmed-meshheading:15331324-Toll-Like Receptors
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pubmed:year |
2004
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pubmed:articleTitle |
Role of the polypeptide region of a 33kDa mycobacterial lipoprotein for efficient IL-12 production.
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pubmed:affiliation |
Department of Microbiology, Leprosy Research Center,National Institute of Infectious Diseases, 4-2-1 Aobacho,Higashimurayama, Tokyo 189-0002, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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