Source:http://linkedlifedata.com/resource/pubmed/id/12171070
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2002-8-12
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome-B(5) Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Dicumarol,
http://linkedlifedata.com/resource/pubmed/chemical/NAD(P)H Dehydrogenase (Quinone),
http://linkedlifedata.com/resource/pubmed/chemical/Quinone Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Uncoupling Agents
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0145-479X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
209-19
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:12171070-Animals,
pubmed-meshheading:12171070-Cell Membrane,
pubmed-meshheading:12171070-Culture Media, Serum-Free,
pubmed-meshheading:12171070-Cytochrome Reductases,
pubmed-meshheading:12171070-Cytochrome-B(5) Reductase,
pubmed-meshheading:12171070-Dicumarol,
pubmed-meshheading:12171070-Enzyme Induction,
pubmed-meshheading:12171070-HL-60 Cells,
pubmed-meshheading:12171070-Humans,
pubmed-meshheading:12171070-Models, Biological,
pubmed-meshheading:12171070-NAD(P)H Dehydrogenase (Quinone),
pubmed-meshheading:12171070-Oxidative Stress,
pubmed-meshheading:12171070-Quinone Reductases,
pubmed-meshheading:12171070-Swine,
pubmed-meshheading:12171070-Uncoupling Agents,
pubmed-meshheading:12171070-Up-Regulation
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pubmed:year |
2002
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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.
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pubmed:affiliation |
Departamento de Biología Celular, Fisiología e Immunología, Facultad de Ciencias, Universidad de Córdoba, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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