pubmed-article:10821856 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10821856 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
pubmed-article:10821856 | lifeskim:mentions | umls-concept:C1417701 | lld:lifeskim |
pubmed-article:10821856 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
pubmed-article:10821856 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:10821856 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
pubmed-article:10821856 | lifeskim:mentions | umls-concept:C0311404 | lld:lifeskim |
pubmed-article:10821856 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:10821856 | pubmed:issue | 21 | lld:pubmed |
pubmed-article:10821856 | pubmed:dateCreated | 2000-6-30 | lld:pubmed |
pubmed-article:10821856 | pubmed:abstractText | Electrophiles and reactive oxygen species have been implicated in the pathogenesis of many diseases. Transcription factor Nrf2 was recently identified as a general regulator of one defense mechanism against such havoc. Nrf2 regulates the inducible expression of a group of detoxication enzymes, such as glutathione S-transferase and NAD(P)H:quinone oxidoreductase, via antioxidant response elements. Using peritoneal macrophages from Nrf2-deficient mice, we show here that Nrf2 also controls the expression of a group of electrophile- and oxidative stress-inducible proteins and activities, which includes heme oxygenase-1, A170, peroxiredoxin MSP23, and cystine membrane transport (system x(c)(-)) activity. The response to electrophilic and reactive oxygen species-producing agents was profoundly impaired in Nrf2-deficient cells. The lack of induction of system x(c)(-) activity resulted in the minimum level of intracellular glutathione, and Nrf2-deficient cells were more sensitive to toxic electrophiles. Several stress agents induced the DNA binding activity of Nrf2 in the nucleus without increasing its mRNA level. Thus Nrf2 regulates a wide-ranging metabolic response to oxidative stress. | lld:pubmed |
pubmed-article:10821856 | pubmed:language | eng | lld:pubmed |
pubmed-article:10821856 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10821856 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10821856 | pubmed:month | May | lld:pubmed |
pubmed-article:10821856 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10821856 | pubmed:author | pubmed-author:TakahashiSS | lld:pubmed |
pubmed-article:10821856 | pubmed:author | pubmed-author:SatoHH | lld:pubmed |
pubmed-article:10821856 | pubmed:author | pubmed-author:IshiiTT | lld:pubmed |
pubmed-article:10821856 | pubmed:author | pubmed-author:YamamotoMM | lld:pubmed |
pubmed-article:10821856 | pubmed:author | pubmed-author:ItohKK | lld:pubmed |
pubmed-article:10821856 | pubmed:author | pubmed-author:KatohYY | lld:pubmed |
pubmed-article:10821856 | pubmed:author | pubmed-author:YanagawaTT | lld:pubmed |
pubmed-article:10821856 | pubmed:author | pubmed-author:BannaiSS | lld:pubmed |
pubmed-article:10821856 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10821856 | pubmed:day | 26 | lld:pubmed |
pubmed-article:10821856 | pubmed:volume | 275 | lld:pubmed |
pubmed-article:10821856 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10821856 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10821856 | pubmed:pagination | 16023-9 | lld:pubmed |
pubmed-article:10821856 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:10821856 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10821856 | pubmed:articleTitle | Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. | lld:pubmed |
pubmed-article:10821856 | pubmed:affiliation | Institute of Basic Medical Sciences and Center for Tsukuba Advanced Research Alliance, University of Tsukuba, 1-1-1 Tennoudai, Tsukuba 305-8577, Japan. | lld:pubmed |
pubmed-article:10821856 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10821856 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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