Source:http://linkedlifedata.com/resource/pubmed/id/16264266
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2005-11-2
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pubmed:abstractText |
Phospholipase D (PLD) activity is known to be related to oxidant-induced cellular signaling and membrane disturbance. Previously, an induction of PLD activity in various cell lines by X-ray irradiation was observed. In this study, we examined the effect of UVC radiation on the PLD activity in Vero 76 cells. At a dose of 10 kJ/m2 of UVC irradiation, the PLD activity was stimulated approximately 10-fold over the basal activity. This UVC-induced PLD activity was found to be dependent on the presence of extracellular calcium and was inhibited by catalase as well as amifostine-an intracellular thiol antioxidant. Pretreatments with Ro32-0432-a selective inhibitor of protein kinase C (PKC)-and downregulation of PKC by preincubation of phorbol 12-myristate 13-acetate significantly inhibited the UVC-induced PLD activity. UVC-stimulated PLD activity was observed only in murine PLD2 (mPLD2)-transfected Vero 76 cells and not in human PLD1 (hPLD1)-transfected cells. Transient incorporation of PKC with mPLD2 and the phosphorylation of mPLD2 by a and b forms of PKC by UVC irradiation were observed. These results suggest that the UVC-stimulated PLD activity in Vero 76 cells is mediated through transient phosphorylation of PLD2 by the translocation of PKC to PLD2.
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Chelating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/phospholipase D2
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1226-3613
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
418-26
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16264266-Animals,
pubmed-meshheading:16264266-Antioxidants,
pubmed-meshheading:16264266-Calcium,
pubmed-meshheading:16264266-Cercopithecus aethiops,
pubmed-meshheading:16264266-Chelating Agents,
pubmed-meshheading:16264266-Enzyme Activation,
pubmed-meshheading:16264266-Mice,
pubmed-meshheading:16264266-Phospholipase D,
pubmed-meshheading:16264266-Protein Isoforms,
pubmed-meshheading:16264266-Protein Kinase C,
pubmed-meshheading:16264266-Protein Kinase Inhibitors,
pubmed-meshheading:16264266-Reactive Oxygen Species,
pubmed-meshheading:16264266-Signal Transduction,
pubmed-meshheading:16264266-Ultraviolet Rays,
pubmed-meshheading:16264266-Vero Cells
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pubmed:year |
2005
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pubmed:articleTitle |
Involvement of protein kinase C pathway in UVC-stimulated phospholipase D2 activity in Vero 76 cells.
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pubmed:affiliation |
School of Chemistry, Seoul National University, Seoul 151-747, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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