TAILIEUCHUNG - Báo cáo khóa học: Phospholipase C, protein kinase C, Ca 2+ /calmodulin-dependent protein kinase II, and redox state are involved in epigallocatechin gallate-induced phospholipase D activation in human astroglioma cells

We show that epigallocatechin-3 gallate (EGCG), a major component of green tea, stimulates phospholipase D (PLD) activity in U87 human astroglioma cells. EGCG-induced PLD activation was abolished by the phospholipase C (PLC) inhibitor and a lipase inactive PLC-c1mutant, which is dependent on intracellular or extracellular Ca 2+ ,withthe possible involvement of Ca 2+ /calmodulin-dependent pro-teinkinase II (CaMkinase II). | Eur. J. Biochem. 271 3470-3480 2004 FEBS 2004 doi Phospholipase C protein kinase C Ca2 calmodulin-dependent protein kinase II and redox state are involved in epigallocatechin gallate-induced phospholipase D activation in human astroglioma cells Shi Yeon Kim1 Bong-Hyun Ahn1 Joonmo Kim1 Yoe-Sik Bae2 Jong-Young Kwak2 Gyesik Min3 Taeg Kyu Kwon4 Jong-Soo Chang5 Young Han Lee6 Shin-Hee Yoon1 and Do Sik Min1 1 Department of Physiology College of Medicine The Catholic University of Korea Seoul Korea 2Medical Research Center for Cancer Molecular Therapy and Department of Biochemistry College of Medicine Dong-A University Busan Korea 3 Department of Microbiological Engineering Jinju National University Korea 4Department of Immunology School of Medicine Keimyung University Daegu Korea 5Department of Life Science Daejin University Kyeongggido Korea 6Division of Molecular and Life Science College of Science and Technology Hanyang University Ansan Korea We show that epigallocatechin-3 gallate EGCG a major component of green tea stimulates phospholipase D PLD activity in U87 human astroglioma cells. EGCG-induced PLD activation was abolished by the phospholipase C PLC inhibitor and a lipase inactive PLC-y1 mutant which is dependent on intracellular or extracellular Ca2 with the possible involvement of Ca2 calmodulin-dependent protein kinase II CaM kinase II . EGCG induced translocation of PLC-y1 from the cytosol to the membrane and PLC-y1 interaction with PLD1. EGCG regulates the activity of PLD by modulating the redox state of the cells and antioxidants reverse this effect. Moreover EGCG-induced PLD activation was reduced by PKC inhibitors or down-regulation of PKC. Taken together these results show that in human astroglioma cells EGCG regulates PLD activity via a signaling pathway involving changes in the redox state that stimulates a PLC-y1 Ins 1 4 5 P3-Ca2 -CaM kinase II-PLD pathway and a PLC-- 1 diacylglycerol -PKC-PLD pathway. Keywords Ca2 .

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