In order to make sure Akt activation is preserved by SP600125, we chose to assess several Akt downstream targets. First we studied GSK 3, that is considered to be phosphorylated at 9 by Akt. This phosphorylation MAPK phosphorylation checks GSK 3. S/K withdrawal induced a loss of pGSK 3 levels in CGNs which was avoided by treatment of CGNs with 1-0 M SP600125. Thus, Akt remains when JNK is inhibited after S/K withdrawal activated. The regulation of programmed cell death by Akt might be mediated by two processes: one by direct mechanism through phosphorylation or interactions with cell death proteins or indirectly by controlling transcriptional factors responsible for the expression of professional or antiapoptotic proteins. To discriminate between these possibilities, we investigated if the protective effects of SP600125 target or inhibit indirect signaling of Akt. We studied the expression of Forkhead protein, specifically p FOXO1 and the cyclic AMP response element binding protein, specifically p CREB, which encourages neuronal survival when phosphorylated. Our results suggest that 12 h of CGN S/K withdrawal checks p FOXO1 Ser256 and p CREB Ser133 phosphorylation, while this dephosphorylation mediated inhibition is prevented by treatment with 10 M SP600125. The phosphorylation of both proteins when CGNs Urogenital pelvic malignancy were treated with SP600125 could also explain, simply, the qualities of this drug in this apoptotic design, and again confirms that Akt remains trigger when SP600125 is used to restrict JNK. Regarding CDK5, yet another cyclin dependent kinase that is involved in the means of neuronal apoptosis, Akt has recently been shown to directly regulate CDK5 action through the increase of p35 protein expression, which triggers CDK5. Ergo, the next experiments we completed sought to help investigate whether SP600125 Lu AA21004 can avoid cdk5/p35 break-down and the formation of pro apoptotic cdk5/p25. Here, Western blot analysis showed that SP606125 prevented the breakdown of cdk5/p35 and increased the p35/p25 ratio. Finally, to find out whether Akt is associated with SP600125 mediated neuroprotection, we subjected CGNs to a neuroprotective therapy in-the pres-ence of LY294002, a PI3K/Akt chemical, after S/K withdrawal. The inhibitor, in part, counteracted the antiapoptotic results of SP600125 against S/K withdrawal, this being demonstrated by the significant increase in DNA fragmentation and the amount of condensed nuclei. To further determine if the neuroprotective effects of SP600125 could be mediated by the service of the Akt pathway we investigated the effects of this drug on LY294002 mediated neurotoxicity in CGNs. We first determined the levels of LY294002 that mediated CGN cell loss.