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

  
@article{APS6155,
	author = {Jin-feng Hu and Wei Xue and Na Ning and Yu-he Yuan and Jun-tian Zhang and Nai-hong Chen},
	title = {Ginsenoside Rg1 activated CaMKIIα mediated extracellular signal-regulated kinase/mitogen activated protein kinase signaling pathway},
	journal = {Acta Pharmacologica Sinica},
	volume = {29},
	number = {9},
	year = {2016},
	keywords = {},
	abstract = {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 PC12 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 PC12 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.},
	issn = {1745-7254},	url = {http://www.chinaphar.com/article/view/6155}
}