| pubmed-article:12623073 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12623073 | lifeskim:mentions | umls-concept:C0525410 | lld:lifeskim |
| pubmed-article:12623073 | lifeskim:mentions | umls-concept:C0743223 | lld:lifeskim |
| pubmed-article:12623073 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:12623073 | lifeskim:mentions | umls-concept:C2697585 | lld:lifeskim |
| pubmed-article:12623073 | lifeskim:mentions | umls-concept:C0048297 | lld:lifeskim |
| pubmed-article:12623073 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12623073 | pubmed:dateCreated | 2003-3-7 | lld:pubmed |
| pubmed-article:12623073 | pubmed:abstractText | 4-hydroxynonenal (4HNE) is a major product of peroxidative membrane lipid destruction and exerts a variety of deleterious actions through formation of covalent adducts with cellular nucleophiles. Consequently, a number of cellular enzyme systems exist that are capable of detoxifying this reactive aldehyde by oxidation, reduction, or conjugation with glutathione. In this investigation we characterize the multidrug resistance-associated protein 2 (MRP2) as the primary transmembrane transport protein in hepatocytes responsible for extracellular export of 4HNE-glutathione conjugate (HNE-SG) from the intracellular site of its formation. Suspensions of freshly isolated hepatocytes (10(6) cells/ml) prepared from either wild-type (WT) Wistar rats or TR(-) rats possessing a mutated Mrp2 gene were incubated with 4HNE (50 nmol/10(6) cells). The formation of 4HNE metabolites, 4-hydroxynonenoic acid (HNA) and HNE-SG, was quantified in the intracellular and extracellular fractions. These studies demonstrated that freshly isolated hepatocytes from both WT and TR(-) rats formed and exported the oxidized metabolite (HNA) to similar extents. Likewise, both populations of hepatocytes displayed nearly identical rates of glutathione conjugation with 4HNE. However, the rate of HNE-SG export from TR(-) hepatocytes was approximately fourfold less than that of WT hepatocytes. In TR(-) hepatocytes, HNE-SG accumulated and remained predominantly intracellular throughout the time course, suggesting an absence of compensatory export by other hepatocellular transporters. In conclusion, these data demonstrate that although WT and TR(-) hepatocytes are similar in their conjugative and oxidative metabolism of 4HNE, export of 4HNE-SG is mediated by the MRP2 transporter, a transport system distinct from that involved in HNA efflux. | lld:pubmed |
| pubmed-article:12623073 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12623073 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12623073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12623073 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12623073 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12623073 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:12623073 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:12623073 | pubmed:author | pubmed-author:PetersenDenni... | lld:pubmed |
| pubmed-article:12623073 | pubmed:author | pubmed-author:DoornJonathan... | lld:pubmed |
| pubmed-article:12623073 | pubmed:author | pubmed-author:ReichardJohn... | lld:pubmed |
| pubmed-article:12623073 | pubmed:author | pubmed-author:SimonFranzF | lld:pubmed |
| pubmed-article:12623073 | pubmed:author | pubmed-author:TaylorMelinda... | lld:pubmed |
| pubmed-article:12623073 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12623073 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:12623073 | pubmed:volume | 411 | lld:pubmed |
| pubmed-article:12623073 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12623073 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12623073 | pubmed:pagination | 243-50 | lld:pubmed |
| pubmed-article:12623073 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12623073 | pubmed:meshHeading | pubmed-meshheading:12623073... | lld:pubmed |
| pubmed-article:12623073 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12623073 | pubmed:articleTitle | Characterization of multidrug resistance-associated protein 2 in the hepatocellular disposition of 4-hydroxynonenal. | lld:pubmed |
| pubmed-article:12623073 | pubmed:affiliation | Department of Pharmaceutical Sciences, University of Colorado Health Sciences Center, Denver, CO 80262, USA. | lld:pubmed |
| pubmed-article:12623073 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12623073 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:25303 | entrezgene:pubmed | pubmed-article:12623073 | lld:entrezgene |
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