| pubmed-article:1370076 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1370076 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
| pubmed-article:1370076 | lifeskim:mentions | umls-concept:C0017837 | lld:lifeskim |
| pubmed-article:1370076 | lifeskim:mentions | umls-concept:C0028195 | lld:lifeskim |
| pubmed-article:1370076 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:1370076 | lifeskim:mentions | umls-concept:C0006506 | lld:lifeskim |
| pubmed-article:1370076 | lifeskim:mentions | umls-concept:C1551336 | lld:lifeskim |
| pubmed-article:1370076 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:1370076 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1370076 | pubmed:dateCreated | 1992-1-17 | lld:pubmed |
| pubmed-article:1370076 | pubmed:abstractText | These studies concern the initial steps in 4-nitroquinoline 1-oxide (4NQO) metabolism in relation to mechanisms of anticarcinogenesis. Butylated hydroxyanisole (BHA) administration by a protocol known to inhibit the pulmonary tumorigenicity of 4NQO in A/HeJ mice enhanced hepatic and pulmonary activities for 4NQO metabolism by two major pathways, conjugative detoxification and nitroreductive activation. High-performance liquid chromatography analysis showed approximate doubling of two types of glutathione transferase subunits with 4NQO-conjugating activity in livers of BHA-treated mice. Similar increases were observed in hepatic 4NQO-conjugating activity and in Vmax, while Km for 4NQO was 39 to 43 microM. Pulmonary 4NQO-glutathione transferase activity increased 24 to 29%. DT diaphorase activity toward 4NQO was elevated 3.3-fold in livers and 2.7-fold in lungs of BHA-treated mice. However, the predominant 4NQO reductase of liver and lung was dicumarol resistant, had a strong preference for NADH, and showed little if any response to BHA. This Mr 200,000 enzyme, partially purified from livers of Swiss mice, exhibited the stoichiometry of 2-NADH/4NQO expected for reduction of 4NQO to 4-hydroxyaminoquinoline 1-oxide. Its high affinity for 4NQO (Km, 15 microM) signified a much greater influence on 4NQO metabolism than DT diaphorase (Km, 208 microM). The dicumarol-resistant 4NQO reductase differed from several known cytosolic nitroreductases. The results suggest that protection by BHA may result from alteration of the balance between 4NQO activation and conjugation. | lld:pubmed |
| pubmed-article:1370076 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1370076 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1370076 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1370076 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1370076 | pubmed:issn | 0008-5472 | lld:pubmed |
| pubmed-article:1370076 | pubmed:author | pubmed-author:BensonA MAM | lld:pubmed |
| pubmed-article:1370076 | pubmed:author | pubmed-author:YorkJ LJL | lld:pubmed |
| pubmed-article:1370076 | pubmed:author | pubmed-author:StanleyJ SJS | lld:pubmed |
| pubmed-article:1370076 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1370076 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1370076 | pubmed:volume | 52 | lld:pubmed |
| pubmed-article:1370076 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1370076 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1370076 | pubmed:pagination | 58-63 | lld:pubmed |
| pubmed-article:1370076 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:1370076 | pubmed:meshHeading | pubmed-meshheading:1370076-... | lld:pubmed |
| pubmed-article:1370076 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1370076 | pubmed:articleTitle | Nitroreductases and glutathione transferases that act on 4-nitroquinoline 1-oxide and their differential induction by butylated hydroxyanisole in mice. | lld:pubmed |
| pubmed-article:1370076 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock 72205-7199. | lld:pubmed |
| pubmed-article:1370076 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1370076 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1370076 | lld:pubmed |
