pubmed-article:1729592 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0312738 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0024027 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0025723 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C0596260 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C1956128 | lld:lifeskim |
pubmed-article:1729592 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:1729592 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:1729592 | pubmed:dateCreated | 1992-2-10 | lld:pubmed |
pubmed-article:1729592 | pubmed:abstractText | We show that both the lipopolysaccharide (LPS)-induced activation of NF-kappa DNA binding and kappa gene expression are blocked by treating murine pre-B lymphocyte 70Z/3 cells with 5'-methylthioadenosine (MTA), an inhibitor of several S-adenosylmethionine-dependent methylation reactions. We further show that the LPS-induced incorporation of radioactivity from [methyl-3H]methionine into methyl ester-like linkages on a group of membrane polypeptides is also inhibited by MTA treatment, suggesting the involvement of protein methylation reactions in the LPS signal transduction pathway. We also find that NF-kappa B and kappa gene activation in LPS-treated 70Z/3 cells is blocked by mevinolin, an inhibitor that prevents protein isoprenylation. Interestingly, mevinolin-treated cells also exhibited a marked reduction in the methylation of membrane proteins. Neither MTA nor mevinolin significantly inhibited NF-kappa B activation by phorbol myristate acetate, suggesting that these agents act early in signal transduction. These results provide the first evidence that carboxyl methylated and/or isoprenylated proteins play an essential role in the LPS-signaling pathway. | lld:pubmed |
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pubmed-article:1729592 | pubmed:language | eng | lld:pubmed |
pubmed-article:1729592 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1729592 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1729592 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:1729592 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1729592 | pubmed:month | Jan | lld:pubmed |
pubmed-article:1729592 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:1729592 | pubmed:author | pubmed-author:WallRR | lld:pubmed |
pubmed-article:1729592 | pubmed:author | pubmed-author:CarterCC | lld:pubmed |
pubmed-article:1729592 | pubmed:author | pubmed-author:LawR ERE | lld:pubmed |
pubmed-article:1729592 | pubmed:author | pubmed-author:ClarkeSS | lld:pubmed |
pubmed-article:1729592 | pubmed:author | pubmed-author:StimmelJ BJB | lld:pubmed |
pubmed-article:1729592 | pubmed:author | pubmed-author:DamoreM AMA | lld:pubmed |
pubmed-article:1729592 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1729592 | pubmed:volume | 12 | lld:pubmed |
pubmed-article:1729592 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1729592 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1729592 | pubmed:pagination | 103-11 | lld:pubmed |
pubmed-article:1729592 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |