Polygalasaponin F inhibits neuronal apoptosis induced by oxygen-glucose deprivation and reoxygenation through the PI3K/Akt pathway
- Basic Clin Pharmacol Toxicol. 2020 Sep;127(3):196-204. doi: 10.1111/bcpt.13408.
- 1. Department of Physiology, Baotou Medical College, Baotou, China.
- 2. Institute of Neuroscience, Baotou Medical College, Baotou, China.
- 3. Inner Mongolia Key Laboratory of Hypoxic Translational Medicine, Baotou Medical College, Baotou, China.
- 4. Department of Pharmacy, Inner Mongolia International Mongolian Hospital, Hohhot, China.
- 5. Department of Traditional Chinese Medical Science, Baotou Medical College, Baotou, China.
- 6. Institute of Materia Medica, Chinese Academy of Medical Sciences, Beijing, China.
Cerebral ischaemia is a common cerebrovascular disease and often induces neuronal Apoptosis, leading to brain damage. Polygalasaponin F (PGSF) is one of the components in Polygala japonica Houtt, and it is a triterpenoid saponin monomer. This research focused on anti-apoptotic effect of PGSF during oxygen-glucose deprivation and reoxygenation (OGD/R) injury in rat adrenal pheochromocytoma cells (PC12) and primary rat cortical neurons. OGD/R treatment reduced viability of PC12 cells and primary neurons. This reduced viability was prevented by PGSF, as shown by MTT assay. OGD/R insult decreased expression of Bcl-2/Bax both in PC12 cells and primary neurons but elevated levels of Caspase-3 in primary neurons. However, PGSF may up-regulate expression of Bcl-2/Bax and down-regulate Caspase-3 in these particular cells. Furthermore, Bcl-2/Bax and the ratio between phosphorylated Akt and total Akt were decreased in PC12 cells treated with OGD/R, and both were increased by PGSF. Moreover, increase in the ratios of Bcl-2/Bax and phosphorylated Akt/total Akt in PC12 cells was suppressed by phosphatidylinositol 3-kinase (PI3K) inhibitor. Data suggest PGSF might prevent OGD/R-induced injury via activation of PI3K/Akt signalling. The ability of PGSF to block the effects of OGD/R appears to involve regulation of Bcl-2, Bax and Caspase-3, which are related to Apoptosis.
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