| pubmed-article:9536002 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9536002 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9536002 | lifeskim:mentions | umls-concept:C0227525 | lld:lifeskim |
| pubmed-article:9536002 | lifeskim:mentions | umls-concept:C0205112 | lld:lifeskim |
| pubmed-article:9536002 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:9536002 | lifeskim:mentions | umls-concept:C0069535 | lld:lifeskim |
| pubmed-article:9536002 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:9536002 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9536002 | pubmed:dateCreated | 1998-5-12 | lld:pubmed |
| pubmed-article:9536002 | pubmed:abstractText | The effects of oncostatin M on the expression of different cytochrome P450 (CYP) isozymes has been investigated in human hepatocytes. The dose-response and time-course analyses of effects on CYP1A2 and CYP3A4 isozymes revealed that maximal inhibition was reached after 48 hr of exposure of human hepatocytes to 25 units/ml oncostatin M. Reductions in CYP1A2 and CYP3A4 activity produced by oncostatin M correlated with decreases in protein content, de novo protein synthesis and specific mRNA levels, thus suggesting that oncostatin M could down-regulate CYP expression at the transcriptional level. The inhibitory potency of oncostatin M on CYP expression was compared with that of other cytokines belonging to the interleukin-6 receptor family (interleukin-6, interleukin-11 and leukemia inhibitory factor), and interferon-gamma, which is recognized to inhibit human CYP expression, and granulocyte colony-stimulating factor, a cytokine that shares structural homology with the interleukin-6 family but has a different transduction signal. Maximal reductions in CYP1A2 activity were reached after 48 hr of treatment with cytokines. At that time, oncostatin M showed the highest inhibitory effects on CYP1A2 activity (38% of control), followed by interferon (49% of control) and interleukin-6 (60% of control), whereas minor effects were produced by the other cytokines (74-80%). Comparable decreases were observed for CYP2A6, CYP2B6 and CYP3A4 activities. Enzymatic activity and de novo protein synthesis of 3-methylcholanthrene-induced CYP1A2 and dexamethasone-induced CYP3A4 were also reduced to a much greater extent by oncostatin M than by other cytokines. The results show that oncostatin M is the most effective cytokine in down-regulating CYP isozymes in human hepatocytes, and its effects were evident even after removal of the cytokine from the culture medium. | lld:pubmed |
| pubmed-article:9536002 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9536002 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9536002 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9536002 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9536002 | pubmed:issn | 0022-3565 | lld:pubmed |
| pubmed-article:9536002 | pubmed:author | pubmed-author:CastellJ VJV | lld:pubmed |
| pubmed-article:9536002 | pubmed:author | pubmed-author:Gómez-LechónM... | lld:pubmed |
| pubmed-article:9536002 | pubmed:author | pubmed-author:JoverRR | lld:pubmed |
| pubmed-article:9536002 | pubmed:author | pubmed-author:FabraRR | lld:pubmed |
| pubmed-article:9536002 | pubmed:author | pubmed-author:TrullenqueRR | lld:pubmed |
| pubmed-article:9536002 | pubmed:author | pubmed-author:DonatoM TMT | lld:pubmed |
| pubmed-article:9536002 | pubmed:author | pubmed-author:GuillénM IMI | lld:pubmed |
| pubmed-article:9536002 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9536002 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:9536002 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9536002 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9536002 | pubmed:pagination | 127-34 | lld:pubmed |
| pubmed-article:9536002 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:9536002 | pubmed:meshHeading | pubmed-meshheading:9536002-... | lld:pubmed |
| pubmed-article:9536002 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9536002 | pubmed:articleTitle | Oncostatin M down-regulates basal and induced cytochromes P450 in human hepatocytes. | lld:pubmed |
| pubmed-article:9536002 | pubmed:affiliation | Unidad de Hepatolog-ia Experimental, Centro de Investigaci-on, Hospital Universitario La Fe, Valencia, Spain. | lld:pubmed |
| pubmed-article:9536002 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9536002 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9536002 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9536002 | lld:pubmed |
