| pubmed-article:12106824 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12106824 | lifeskim:mentions | umls-concept:C2717940 | lld:lifeskim |
| pubmed-article:12106824 | lifeskim:mentions | umls-concept:C0332157 | lld:lifeskim |
| pubmed-article:12106824 | lifeskim:mentions | umls-concept:C0596691 | lld:lifeskim |
| pubmed-article:12106824 | lifeskim:mentions | umls-concept:C0205217 | lld:lifeskim |
| pubmed-article:12106824 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
| pubmed-article:12106824 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12106824 | pubmed:dateCreated | 2002-7-10 | lld:pubmed |
| pubmed-article:12106824 | pubmed:abstractText | Chronic ethanol consumption is associated with increased protein oxidation and decreased proteolysis in the liver. We tested the hypothesis that even single-dose treatment with ethanol or bromotrichloromethane causes increased protein oxidation and a distinct proteolytic response in cultured hepatocytes. HepG2 cells were treated for 30 min with ethanol, H(2)O(2) and bromotrichloromethane at various nontoxic concentrations. Protein degradation was measured in living cells using [35S]-methionine labeling. Protein oxidation, and 20S proteasome activity were measured in cell lysates. Oxidized proteins increased immediately after ethanol, H(2)O(2), and bromotrichloromethane exposure, but a further significant increase 24-h after exposure was observed only following ethanol and bromotrichloromethane treatment. All three reagents caused a significant increase of the overall intracellular proteolysis at rather low concentrations, which could be suppressed by the proteasome inhibitor lactacystin. A decline of proteolysis observed at higher-subtoxic-concentrations was not related to decreased proteasome activity. Preincubation with ketoconazole or 4-methylpyrazole completely prevented the ethanol- and bromotrichloromethane-induced but not the H(2)O(2)-induced protein oxidation and proteolysis, suggesting strongly an enzyme-mediated generation of reactive oxygen species. In conclusion single-dose exposure with ethanol or haloalkanes causes increased protein oxidation followed by an increased proteasome-dependent protein degradation in human liver cells. | lld:pubmed |
| pubmed-article:12106824 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12106824 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12106824 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12106824 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:12106824 | pubmed:issn | 0891-5849 | lld:pubmed |
| pubmed-article:12106824 | pubmed:author | pubmed-author:LochsHerbertH | lld:pubmed |
| pubmed-article:12106824 | pubmed:author | pubmed-author:GruneTilmanT | lld:pubmed |
| pubmed-article:12106824 | pubmed:author | pubmed-author:PirlichMatthi... | lld:pubmed |
| pubmed-article:12106824 | pubmed:author | pubmed-author:JakstadtManue... | lld:pubmed |
| pubmed-article:12106824 | pubmed:author | pubmed-author:MüllerCorneli... | lld:pubmed |
| pubmed-article:12106824 | pubmed:author | pubmed-author:SandigGritG | lld:pubmed |
| pubmed-article:12106824 | pubmed:author | pubmed-author:SitteNicolleN | lld:pubmed |
| pubmed-article:12106824 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12106824 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:12106824 | pubmed:volume | 33 | lld:pubmed |
| pubmed-article:12106824 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12106824 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12106824 | pubmed:pagination | 283-91 | lld:pubmed |
| pubmed-article:12106824 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:12106824 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12106824 | pubmed:articleTitle | Increased proteolysis after single-dose exposure with hepatotoxins in HepG2 cells. | lld:pubmed |
| pubmed-article:12106824 | pubmed:affiliation | Department of Gastroenterology and Hepatology, University Hospital Charité, Humboldt-University Berlin, Germany. | lld:pubmed |
| pubmed-article:12106824 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12106824 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12106824 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12106824 | lld:pubmed |
