Ginsenoside Rg1 activated CaMKⅡα mediated extracellular signal-regulated kinaselmitogen activated protein kinase signaling pathway  被引量:5

Ginsenoside Rg1 activated CaMKⅡα mediated extracellular signal-regulated kinaselmitogen activated protein kinase signaling pathway

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作  者:Jin-feng HU Wei XUE Na NING Yu-he YUAN Jun-tian ZHANG Nai-hong CHEN 

机构地区:[1]Department of Pharmacology, Institute of Materia Medica, Chinese Academy of Medical Sciences & Peking Union Medical College, Beo'ing 100050, China

出  处:《Acta Pharmacologica Sinica》2008年第9期1119-1126,共8页中国药理学报(英文版)

摘  要:Aim: We carried out this study to investigate the effect of ginsenoside Rg1 on the extracellular signal-regulated kinase/mitogen activated protein kinase (ERK/ MAPK) pathway for understanding its effect on synaptic platicity. Methods: Western blotting and immunostaining were used to examine the phosphorylation of ERK1/2, CaMKⅡα and cAMP response element binding protein (CREB) in PC 12 cells and synaptosomes. The confocal microscopy and fluorescent indicator Fluo-3 was applied to observe the intracellular calcium ion flux. Results: The phosphorylation of ERK1/2 in PC 12 cells and synaptosomes incubated with Rg1 was increased and reached maximum at 4 min. Rg1 also promoted the transient enhancement of upstream calcium ion and activated CaMKⅡα, which reached maximum at 2 min. CREB, the downstream protein, was phosphorylated within 8 min in PC12 cells after being incubated with Rg1. Moreover, KN93 partially inhibited the activation of ERK1/2, and PD98059 also partially blocked the phosphorylation of CREB. Conclusions: Rg1 activated ERK/MAPK pathway by CaMKⅡα, and the activation of CREB was not only dependent on ERK induced by Rg1, which may provide an explanation for the effect of Rg1 on long-term potentiation.Aim: We carried out this study to investigate the effect of ginsenoside Rg1 on the extracellular signal-regulated kinase/mitogen activated protein kinase (ERK/ MAPK) pathway for understanding its effect on synaptic platicity. Methods: Western blotting and immunostaining were used to examine the phosphorylation of ERK1/2, CaMKⅡα and cAMP response element binding protein (CREB) in PC 12 cells and synaptosomes. The confocal microscopy and fluorescent indicator Fluo-3 was applied to observe the intracellular calcium ion flux. Results: The phosphorylation of ERK1/2 in PC 12 cells and synaptosomes incubated with Rg1 was increased and reached maximum at 4 min. Rg1 also promoted the transient enhancement of upstream calcium ion and activated CaMKⅡα, which reached maximum at 2 min. CREB, the downstream protein, was phosphorylated within 8 min in PC12 cells after being incubated with Rg1. Moreover, KN93 partially inhibited the activation of ERK1/2, and PD98059 also partially blocked the phosphorylation of CREB. Conclusions: Rg1 activated ERK/MAPK pathway by CaMKⅡα, and the activation of CREB was not only dependent on ERK induced by Rg1, which may provide an explanation for the effect of Rg1 on long-term potentiation.

关 键 词:ginsenoside Rg1 ERK1/2 CaMKⅡα CREB 

分 类 号:R96[医药卫生—药理学]

 

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