Activation Mechanism of Phospholipase D Involved in the Generation of Lipid Mediators in Cultured Madin-Darby Canine Kidney Cells
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概要
- 論文の詳細を見る
Addition of 100 nM phorbol 12-myristate 13-acetate (PMA), an active phorbol diester, to quiescent cultured Madin-Darby canine kidney (MDCK) cells caused a maximal stimulation of phosphatidylethanol formation within 1-2 h in the presence of 1% ethanol, indicating the activation of phospholipase D (PLD). The specificity of phorbol diesters for the activation of PLD activation was confirmed by the fact that phorbol 12,13-dibutyrate (PDBu) was effective, whereas 4α-phorbol 12,13-didecanoate (4α-PDD) was without effect. Down-regulation caused by the long-term pretreatment of the cells with active phorbol diesters significantly decreased the production of phosphatidylethanol. Staurosporine, a well known protein kinase (PK)C inhibitor at 1μM, decreased the activation of PLD. Taken together, these observations suggested the involvement of PKC in the activation of PLD. The cellular PLD activity was found to be selectively localized in the particulate fraction by centrifugation at 12,000×g. The particulate PLD showed the selective substrate specificity for phosphatidylcholine rather than phosphatidyl-ethanolamine. In response to the addition of 100 nM PMA, 1,2-diacylglycerol (DG) increased in a biphasic fashion. In view of the time course of the activation of PLD, the second increase in the 1,2-DG around 20 min was contributed by the activation of PLD. In reponse to the simultaneous addition of 100 nM PMA and 100 nM A23187, the cultured MDCK cells activated the arachidonate cascades to form prostaglandin (PG)E_2 and PGF_<2α> as major products, requiring slower 24h to reach maximal levels. The pretreatment of the cells with 1% ethanol caused a significant drop in the synthesis of PGE_2 rather than PGF_<2α>. The results indicated that either phosphatidic acid (PA) or 1, 2-DG from the hydrolysis of PA served as an activator of cellular response or a direct source of free arachidonic acid as substrates for phospholipases.
- 社団法人日本農芸化学会の論文
- 1995-07-23
著者
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Yokota K
Department Of Bacteriology Okayama University Graduate School Of Medicine And Dentistry
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Yokota K
Laboratory Of Applied Microbiology Department Of Molecular And Cell Biology Graduate School Of Agric
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Yokota Kenji
Department Of Bacteriology Okayama University Graduate School Of Medicine And Dentistry
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Jisaka M
Shimane Univ. Shimane Jpn
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Jisaka Mitsuo
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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Yokota Kenji
Okayama Univ. Graduate School Of Medicine And Dentistry Okayama Jpn
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YOKOTA Kazushige
Department of Life Science and Biotechnology, Shimane University
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Jisaka Mitsuo
Department Of Food Science And Technology Faculty Of Agriculture Kyoto University
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Takinami K
Kansai Univ. Osaka Jpn
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TAKINAMI Koichi
Research Institute of Molecular Genetics, Shimane University
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Takinami Koichi
Research Institute Of Molecular Genetics Shimane University
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Takeuchi Jun-Ichi
Department of Bioresource Chemistry, Faculty of Agriculture, Shimane University
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Takinami Koichi
Department of Bioresource Chemistry, Faculty of Agriculture, Shimane University
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Jozuka Michiyo
Dep. Of Nutritional Sci. Fac. Of Health And Welfare Sci. Okayama Prefectural Univ.
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Yokota Kenji
Department Of Bacteriology Okayama University Graduate School Of Medicine Dentistry And Pharmaceutic
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Takeuchi Jun-ichi
Department Of Bioresource Chemistry Faculty Of Agriculture Shimane University
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Oguma Keiji
Department Of Bacteriology Okayama University Graduate School Of Medicine Dentistry And Pharmaceutic
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YOKOTA Kazushige
Department of Life Science and Biotechnology, Faculty of Life and Environmental Science, Shimane University
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