pubmed-article:12171070 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C0229671 | lld:lifeskim |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C0282549 | lld:lifeskim |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C0027280 | lld:lifeskim |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C2825032 | lld:lifeskim |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C1136197 | lld:lifeskim |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:12171070 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:12171070 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12171070 | pubmed:dateCreated | 2002-8-12 | lld:pubmed |
pubmed-article:12171070 | pubmed:abstractText | We have studied changes in plasma membrane NAD(P)H:quinone oxidoreductases of HL-60 cells under serum withdrawal conditions, as a model to analyze cell responses to oxidative stress. Highly enriched plasma membrane fractions were obtained from cell homogenates. A major part of NADH-quinone oxidoreductase in the plasma membrane was insensitive to micromolar concentrations of dicumarol, a specific inhibitor of the NAD(P)H:quinone oxidoreductase 1 (NQOI, DT-diaphorase), and only a minor portion was characterized as DT-diaphorase. An enzyme with properties of a cytochrome b5 reductase accounted for most dicumarol-resistant quinone reductase activity in HL-60 plasma membranes. The enzyme used mainly NADH as donor, it reduced coenzyme Q0 through a one-electron mechanism with generation of superoxide, and its inhibition profile by p-hydroxymercuribenzoate was similar to that of authentic cytochrome b5 reductase. Both NQO1 and a novel dicumarol-insensitive quinone reductase that was not accounted by a cytochrome b5 reductase were significantly increased in plasma membranes after serum deprivation, showing a peak at 32 h of treatment. The reductase was specific for NADH, did not generate superoxide during quinone reduction, and was significantly resistant to p-hydroxymercuribenzoate. The function of this novel quinone reductase remains to be elucidated whereas dicumarol inhibition of NQO1 strongly potentiated growth arrest and decreased viability of HL-60 cells in the absence of serum. Our results demonstrate that upregulation of two-electron quinone reductases at the plasma membrane is a mechanism evoked by cells for defense against oxidative stress caused by serum withdrawal. | lld:pubmed |
pubmed-article:12171070 | pubmed:language | eng | lld:pubmed |
pubmed-article:12171070 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12171070 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12171070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12171070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:12171070 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12171070 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12171070 | pubmed:month | Jun | lld:pubmed |
pubmed-article:12171070 | pubmed:issn | 0145-479X | lld:pubmed |
pubmed-article:12171070 | pubmed:author | pubmed-author:ForthofferNat... | lld:pubmed |
pubmed-article:12171070 | pubmed:author | pubmed-author:Gómez-DíazCon... | lld:pubmed |
pubmed-article:12171070 | pubmed:author | pubmed-author:BelloRosario... | lld:pubmed |
pubmed-article:12171070 | pubmed:author | pubmed-author:BurónMaría... | lld:pubmed |
pubmed-article:12171070 | pubmed:author | pubmed-author:MartínSergio... | lld:pubmed |
pubmed-article:12171070 | pubmed:author | pubmed-author:Rodríguez-Agu... | lld:pubmed |
pubmed-article:12171070 | pubmed:author | pubmed-author:NavasPlácidoP | lld:pubmed |
pubmed-article:12171070 | pubmed:author | pubmed-author:VillalbaJosé... | lld:pubmed |
pubmed-article:12171070 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12171070 | pubmed:volume | 34 | lld:pubmed |
pubmed-article:12171070 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12171070 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12171070 | pubmed:pagination | 209-19 | lld:pubmed |
pubmed-article:12171070 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:12171070 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12171070 | pubmed:articleTitle | A novel plasma membrane quinone reductase and NAD(P)H:quinone oxidoreductase 1 are upregulated by serum withdrawal in human promyelocytic HL-60 cells. | lld:pubmed |
pubmed-article:12171070 | pubmed:affiliation | Departamento de Biología Celular, Fisiología e Immunología, Facultad de Ciencias, Universidad de Córdoba, Spain. | lld:pubmed |
pubmed-article:12171070 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12171070 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:1728 | entrezgene:pubmed | pubmed-article:12171070 | lld:entrezgene |
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