previous studies have noted that calcium signaling stimulates Akt through NMDA receptors. But, our results utilizing MK 801, an receptor antagonist, suggest that the NMDA receptor is not involved in SP600125 neuroprotective effects. On the other hand, there’s growing evidence that neurotrophins act on CGNs through binding to tyrosine kinase receptors and that phosphorylation of Akt by BDNF is mediated by TrkB receptors. Here we showed that the TrkB receptors order Canagliflozin didn’t play a prominent part in Akt activation mediated by SP600125, because K252a, an antagonist of these receptors, didn’t exert any effect in terms of counteracting the protective effects of SP600125. PTEN is really a lipid phosphatase that performs a in cell survival and apoptosis by negatively regulating phosphoproteins in the PI3K/Akt path. Certainly, PTEN is known to be considered a important negative regulator of the PI3K/Akt signaling pathway that acts by catalyzing the degradation of phosphatidylinositol 3,4,5 triphosphate to PI 4,5 diphosphate. Here, since SP600125 didn’t cause changes in PTEN expression, we obviously show that increasing Akt Ser473 phosphorylation isn’t mediated by changes in PTEN expression. Still another regulator of the Akt pathway may be the Src family tyrosine kinases. Our results show the neuroprotective effects of SP600125 are not mediated through the activation of Src. Our hypothesis is founded on the fact the particular Src household tyrosine kinase inhibitor PP2 and its control PP3 were not able to attenuate the neuroprotective effects of SP600125. The outcomes presented here vary from those described in previous studies, which suggested that CEP 1347 in PC12 cells modulates Akt service via Src. Still another finding of the study is that JNK inhibition prevents the method of cell cycle re access in CGNs by a novel procedure PF299804 solubility that involves the inhibition of GSK 3 and p Rb. Because a common characteristic in all neurodegenerative disorders may be the enhanced expression of cell cycle proteins, which therefore has detrimental effects on neuronal survival studying the process by which JNK inhibition stops re entry into the cell cycle is important. Moreover, in response to apoptotic insults, post mitotic neurons may attempt to re enter the cell cycle and failure to perform the cell cycle leads to the demise of neurons. Although much of the idea remains to be tested, samples of increased levels of proteins in damaged neurons and upregulation of cell cycle genes have already been widely reported. Even though process underlying neuronal cell cycle re entry is defectively understood it has been proposed that DNA damage will be the cause. More over, a recent study shows that the increase in cell cycle proteins takes its mechanism of DNA repair.