It’s been proven that growth factors including GDNF block neurological apoptosis after transient ischemia through Akt activation in rat. Regarding about astrocytes, it has been noted that the activation of PI3 kinase/Akt pathway suppresses apoptosis of rat cortical astrocytes and reveals cell survival after hypoxia. FGF 2 is generally proven to stimulate the PI3 kinase/Akt process in a number sort of cells. Additionally, PF 573228 FGF 2 supposedly reveals neuroprotective effects against glutamate through GDNF synthesis in rat nerves. It’s also been found that heme oxygenase 1 triggers phrase through Akt activation in rat glial cells. Nevertheless, the function of PI3 kinase/Akt pathway in FGF 2induced GDNF launch fromastrocytes remains to be elucidated. Thus, we investigated if the PI3 kinase/Akt process is involved in FGF 2 induced GDNF release from C6 glioma cells and the partnership with the MAP kinase superfamily. It is known that FGFs cause PI3 kinase activation in various types of cells. The activated PI3 kinase converts the plasma membrane lipid PI4,5 bisphosphate to PI 3,4,5 trisphosphate. Accumulation Lymphatic system with this lipid contributes to recruitment of Akt from cytosol to the plasma membrane, therefore activated by phosphorylation on Thr308 and Ser473 remains. Akt phosphorylates many different substrates including glycogen synthase kinase 3B. First, we confirmed that FGF 2 markedly aroused GSK3B in a time dependent manner and phosphorylation Akt at Ser473 and Thr308 residues in C6 glioma cells. FGF 2 induced phosphorylation of Akt and GSK3B reached its peak at 10 min following the pleasure and continued as much as 90 min. To be able to investigate whether the PI3 kinase/Akt process is involved with FGF 2 induced GDNF release from C6 glioma cells, we examined the results of PI3 kinase inhibitors on FGF 2 induced GDNF release. Wortmannin, a kinase inhibitor, dramatically suppressed the FGF GDC-0068 clinical trial 2 induced GDNF release as well as the basal levels of GDNF. Wortmannin incredibly attenuated FGF 2 induced Akt phosphorylation at Ser473 and Thr308 derivatives and GSK3B phosphorylation. The viability of cells stimulated by FGF 2 after 3-6 h with pretreatment of 7 uM wortmannin or 20 uM LY294002 was above 98% compared to that of cells without pretreatment by trypan blue staining. LY294002, yet another PI3 kinase inhibitor, also somewhat paid down the FGF 2 induced GDNF release. LY294002 truly suppressed FGF 2 caused Akt phosphorylation at Thr308 and Ser473 deposits and GSK3B phosphorylation. Therefore, it is suggested that the PI3 kinase/Akt process is associated with FGF 2 induced GDNF release from cells.