| pubmed-article:534488 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:534488 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:534488 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:534488 | lifeskim:mentions | umls-concept:C2239176 | lld:lifeskim |
| pubmed-article:534488 | lifeskim:mentions | umls-concept:C0001985 | lld:lifeskim |
| pubmed-article:534488 | lifeskim:mentions | umls-concept:C1704711 | lld:lifeskim |
| pubmed-article:534488 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:534488 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:534488 | pubmed:dateCreated | 1980-3-17 | lld:pubmed |
| pubmed-article:534488 | pubmed:abstractText | The subcellular distribution and properties of four aldehyde dehydrogenase isoenzymes (I-IV) identified in 2-acetylaminofluorene-induced rat hepatomas and three aldehyde dehydrogenases (I-III) identified in normal rat liver are compared. In normal liver, mitochondria (50%) and microsomal fraction (27%) possess the majority of the aldehyde dehydrogenase, with cytosol possessing little, if any, activity. Isoenzymes I-III can be identified in both fractions and differ from each other on the basis of substrate and coenzyme specificity, substrate K(m), inhibition by disulfiram and anti-(hepatoma aldehyde dehydrogenase) sera, and/or isoelectric point. Hepatomas possess considerable cytosolic aldehyde dehydrogenase (20%), in addition to mitochondrial (23%) and microsomal (35%) activity. Although isoenzymes I-III are present in tumour mitochondrial and microsomal fractions, little isoenzyme I or II is found in cytosol. Of hepatoma cytosolic aldehyde dehydrogenase activity, 50% is a hepatoma-specific isoenzyme (IV), differing in several properties from isoenzymes I-III; the remainder of the tumour cytosolic activity is due to isoenzyme III (48%). The data indicate that the tumour-specific aldehyde dehydrogenase phenotype is explainable by qualitative and quantitative changes involving primarily cytosolic and microsomal aldehyde dehydrogenase. The qualitative change requires the derepression of a gene for an aldehyde dehydrogenase expressed in normal liver only after exposure to potentially harmful xenobiotics. The quantitative change involves both an increase in activity and a change in subcellular location of a basal normal-liver aldehyde dehydrogenase isoenzyme. | lld:pubmed |
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| pubmed-article:534488 | pubmed:language | eng | lld:pubmed |
| pubmed-article:534488 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:534488 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:534488 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:534488 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:534488 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:534488 | pubmed:author | pubmed-author:LindahlRR | lld:pubmed |
| pubmed-article:534488 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:534488 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:534488 | pubmed:volume | 183 | lld:pubmed |
| pubmed-article:534488 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:534488 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:534488 | pubmed:pagination | 55-64 | lld:pubmed |
| pubmed-article:534488 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:534488 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:534488 | pubmed:articleTitle | Subcellular distribution and properties of aldehyde dehydrogenase from 2-acetylaminofluorene-induced rat hepatomas. | lld:pubmed |
| pubmed-article:534488 | pubmed:publicationType | Journal Article | lld:pubmed |
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