| pubmed-article:3365687 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3365687 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:3365687 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:3365687 | lifeskim:mentions | umls-concept:C0001985 | lld:lifeskim |
| pubmed-article:3365687 | lifeskim:mentions | umls-concept:C0010583 | lld:lifeskim |
| pubmed-article:3365687 | lifeskim:mentions | umls-concept:C0332325 | lld:lifeskim |
| pubmed-article:3365687 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:3365687 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:3365687 | pubmed:dateCreated | 1988-6-15 | lld:pubmed |
| pubmed-article:3365687 | pubmed:abstractText | The cytosolic aldehyde dehydrogenase (ALDH) isozyme from cyclophosphamide (CPA) resistant L1210 cells (L1210/CPA) was purified to apparent homogeneity using ternary enzyme complex-dye ligand chromatography. The purified isozyme migrates as a single band at Mr 51,000 in sodium dodecyl sulfate polyacrylamide gel electrophoresis and as a single charge species at isoelectric point = 5.8 in isoelectric focusing. Micromolar Km values were estimated with both propionaldehyde (Km = 5 microM) and 4-hydroxy cyclophosphamide (4-OH CPA) (Km = 4 microM) as substrates, indicating that this isozyme is capable of oxidizing the activated cyclophosphamide intermediate 4-hydroxy CPA/aldophosphamide to carboxyphosphamide. This isozyme is also potently inhibited by disulfiram (Ki = 6 microM) and 4-(diethylamino)benzaldehyde (Ki = 0.04 microM). Both of these inhibitors are capable of sensitizing L1210/CPA cells to activated CPA in clonogenic survival assays. Thus, the increased levels of only the cytosolic ALDH isoform in L1210/CPA cells appear to be the single phenotypic difference necessary for conferring resistance to CPA. Monospecific antibodies to the L1210/CPA isozyme have been used in Western blot analysis to detect nanogram levels of ALDH in cell and tissue extracts. These antibodies cross-react with the cytosolic isozyme in P388/CPA cells, mouse liver, mouse small intestine, and the 1C1C7 hepatoma cell line, whereas no ALDH is detected in sensitive L1210 or P388 cells. Also, these antibodies show little cross-reactivity with the mitochondrial isozyme from mouse liver or 1C1C7 cells. From immunological and inhibitor characterization, the soluble ALDH isozyme in L1210/CPA cells appears identical to the normal mouse tissue isozyme. | lld:pubmed |
| pubmed-article:3365687 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3365687 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3365687 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3365687 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3365687 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3365687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3365687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3365687 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3365687 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3365687 | pubmed:issn | 0008-5472 | lld:pubmed |
| pubmed-article:3365687 | pubmed:author | pubmed-author:HiltonJJ | lld:pubmed |
| pubmed-article:3365687 | pubmed:author | pubmed-author:RussoJ EJE | lld:pubmed |
| pubmed-article:3365687 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3365687 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3365687 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:3365687 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3365687 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3365687 | pubmed:pagination | 2963-8 | lld:pubmed |
| pubmed-article:3365687 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:meshHeading | pubmed-meshheading:3365687-... | lld:pubmed |
| pubmed-article:3365687 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3365687 | pubmed:articleTitle | Characterization of cytosolic aldehyde dehydrogenase from cyclophosphamide resistant L1210 cells. | lld:pubmed |
| pubmed-article:3365687 | pubmed:affiliation | Pharmacology Laboratory, Johns Hopkins Oncology Center, Baltimore, Maryland 21205. | lld:pubmed |
| pubmed-article:3365687 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3365687 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3365687 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3365687 | lld:pubmed |
