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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2000-11-28
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pubmed:abstractText |
Michael adducts of ascorbic acid with alpha,beta-unsaturated carbonyl compounds have been shown to be potent inhibitors of protein phosphatase 1 (PP1) without affecting cell viability at the respective concentrations. Here we were able to show that higher concentrations can partially inhibit PP2A activity and concomitantly induce apoptotic cell death. A nitrostyrene adduct of ascorbic acid proved to be a more potent and effective inhibitor of PP2A as well as a stronger inducer of apoptosis. These adducts only slightly lost their cytotoxic potential in multidrug resistant cells that were 10-fold less sensitive to apoptosis induction by okadaic acid and vinblastine.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0960-894X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1605-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10915062-Animals,
pubmed-meshheading:10915062-Apoptosis,
pubmed-meshheading:10915062-Ascorbic Acid,
pubmed-meshheading:10915062-Caspase 3,
pubmed-meshheading:10915062-Caspases,
pubmed-meshheading:10915062-Cell Line,
pubmed-meshheading:10915062-Cricetinae,
pubmed-meshheading:10915062-DNA Fragmentation,
pubmed-meshheading:10915062-Drug Design,
pubmed-meshheading:10915062-Enzyme Activation,
pubmed-meshheading:10915062-Enzyme Inhibitors,
pubmed-meshheading:10915062-Indicators and Reagents,
pubmed-meshheading:10915062-Kinetics,
pubmed-meshheading:10915062-Molecular Structure,
pubmed-meshheading:10915062-Phosphoprotein Phosphatases,
pubmed-meshheading:10915062-Protein Phosphatase 1,
pubmed-meshheading:10915062-Protein Phosphatase 2,
pubmed-meshheading:10915062-Structure-Activity Relationship
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pubmed:year |
2000
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pubmed:articleTitle |
Michael adducts of ascorbic acid as inhibitors of protein phosphatase 2A and inducers of apoptosis.
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pubmed:affiliation |
Institut für Pharmakologie, Universität Göttingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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