pubmed-article:2848721 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2848721 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:2848721 | lifeskim:mentions | umls-concept:C2239176 | lld:lifeskim |
pubmed-article:2848721 | lifeskim:mentions | umls-concept:C2717940 | lld:lifeskim |
pubmed-article:2848721 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:2848721 | lifeskim:mentions | umls-concept:C0079189 | lld:lifeskim |
pubmed-article:2848721 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:2848721 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:2848721 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:2848721 | pubmed:dateCreated | 1989-1-25 | lld:pubmed |
pubmed-article:2848721 | pubmed:abstractText | The regulation of the synthesis of alpha-2-HS glycoprotein (AHSG) by inflammatory mediators from activated monocytes was studied on the human hepatoma cell line HepG2 and compared to that of albumin. Monocyte-conditioned medium, recombinant human interleukin-6 (rhIL6) and interleukin-1 beta (rhIL1 beta) all down-regulated the synthesis of AHSG. This decrease was found both at the protein and the mRNA level. The most efficient mediator was the monocyte-conditioned medium, when rhIL1 beta was found to be less efficient than rhIL6. The combination of rhIL6 and rhIL1 beta resulted in an additive down-regulation of the AHSG mRNA levels. Similar results were obtained with albumin. These data indicate that AHSG is a negative acute-phase protein whose synthesis is regulated by cytokines in a manner similar to that of albumin. | lld:pubmed |
pubmed-article:2848721 | pubmed:language | eng | lld:pubmed |
pubmed-article:2848721 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2848721 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2848721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2848721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2848721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2848721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2848721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2848721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2848721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2848721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2848721 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2848721 | pubmed:month | Dec | lld:pubmed |
pubmed-article:2848721 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:2848721 | pubmed:author | pubmed-author:ArnaudPP | lld:pubmed |
pubmed-article:2848721 | pubmed:author | pubmed-author:LebretonJ PJP | lld:pubmed |
pubmed-article:2848721 | pubmed:author | pubmed-author:HironMM | lld:pubmed |
pubmed-article:2848721 | pubmed:author | pubmed-author:DaveauMM | lld:pubmed |
pubmed-article:2848721 | pubmed:author | pubmed-author:JulesKK | lld:pubmed |
pubmed-article:2848721 | pubmed:author | pubmed-author:Christian-Dav... | lld:pubmed |
pubmed-article:2848721 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2848721 | pubmed:day | 5 | lld:pubmed |
pubmed-article:2848721 | pubmed:volume | 241 | lld:pubmed |
pubmed-article:2848721 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2848721 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2848721 | pubmed:pagination | 191-4 | lld:pubmed |
pubmed-article:2848721 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
pubmed-article:2848721 | pubmed:meshHeading | pubmed-meshheading:2848721-... | lld:pubmed |
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pubmed-article:2848721 | pubmed:meshHeading | pubmed-meshheading:2848721-... | lld:pubmed |
pubmed-article:2848721 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:2848721 | pubmed:articleTitle | The synthesis of human alpha-2-HS glycoprotein is down-regulated by cytokines in hepatoma HepG2 cells. | lld:pubmed |
pubmed-article:2848721 | pubmed:affiliation | INSERM Unité 78, Bois-Guillaume, France. | lld:pubmed |
pubmed-article:2848721 | pubmed:publicationType | Journal Article | lld:pubmed |
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