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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1998-5-21
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pubmed:abstractText |
RRR-alpha-Tocopherol, but not RRR-beta-tocopherol, negative regulates proliferation of vascular smooth muscle cells at physiological concentrations. At the same concentrations RRR-alpha-tocopherol inhibits protein kinase C activity, whereas RRR-beta-tocopherol is ineffective. Furthermore, RRR-beta-tocopherol prevents the inhibition of cell growth and of protein kinase C activity caused by RRR-alpha-tocopherol. The negative regulation by RRR-alpha-tocopherol of protein kinase C activity appears to be the cause of smooth muscle cell growth inhibition. RRR-alpha-Tocopherol does not act by binding to protein kinase C directly but presumably by preventing protein kinase C activation. A second RRR-alpha-tocopherol effect has been found at the level of AP 1, the latter becoming activated by RRR-alpha-tocopherol under condition of protein kinase C inhibition or down regulation. AP-1 inhibition by RRR-alpha-tocopherol is seen, however, under condition of protein kinase C stimulation. Compositional changes of AP-1 have been found to be at the basis of the RRR-alpha-tocopherol effects. RRR-beta-tocopherol, provided with similar antioxidant properties, not only it does not affect AP 1 but it prevents the effects of RRR-alpha-tocopherol. Moreover, it has been observed that RRR-alpha-tocopherol is able to affect TRE regulated gene transcription. It is concluded that RRR-alpha-tocopherol acts specifically in vascular smooth muscle cells, by controlling a signal transduction pathway leading to cell proliferation by a non-antioxidant mechanism.
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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/Antioxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Chloramphenicol O-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin E
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pubmed:status |
MEDLINE
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pubmed:issn |
0044-264X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37 Suppl 1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9558725-Animals,
pubmed-meshheading:9558725-Antioxidants,
pubmed-meshheading:9558725-Aorta,
pubmed-meshheading:9558725-Cell Division,
pubmed-meshheading:9558725-Cell Survival,
pubmed-meshheading:9558725-Cells, Cultured,
pubmed-meshheading:9558725-Chloramphenicol O-Acetyltransferase,
pubmed-meshheading:9558725-DNA,
pubmed-meshheading:9558725-Gene Expression Regulation,
pubmed-meshheading:9558725-Muscle, Smooth, Vascular,
pubmed-meshheading:9558725-Protein Kinase C,
pubmed-meshheading:9558725-Rats,
pubmed-meshheading:9558725-Recombinant Proteins,
pubmed-meshheading:9558725-Stereoisomerism,
pubmed-meshheading:9558725-Tetradecanoylphorbol Acetate,
pubmed-meshheading:9558725-Thymidine,
pubmed-meshheading:9558725-Transcription, Genetic,
pubmed-meshheading:9558725-Transcription Factor AP-1,
pubmed-meshheading:9558725-Transfection,
pubmed-meshheading:9558725-Vitamin E
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pubmed:year |
1998
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pubmed:articleTitle |
RRR-alpha-tocopherol regulation of gene transcription in response to the cell oxidant status.
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pubmed:affiliation |
Institut für Biochemie und, Molekularbiologie, Universität Bern, Schweiz.
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pubmed:publicationType |
Journal Article
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