Akt activation is also inhibited by the pharmacological inhibitor of PI3 K, resulting in decreased cell growth rate. Consequently, these data imply constitutive activation of PI3 K/Akt results in faster G1 to S cell cycle entry because of increase in cyclin D1 amounts in MCF7As53 cells. In our search to recognize the upstream regulator of activated PI3 K/Akt in MCF 7As53 cells, we probed for Cav 1 together with pCav 1 levels in these cells. Previous studies have suggested that Cav 1 is a potent activator of PI3 K/Akt process. In MCF 7As53 cells, we detected dramatically greater levels of Cav 1 as well as pCav 1 levels in comparison to those within parental MCF 7 cells. The cells were transfected with the wild type p53 expression vector, to confirm whether the upsurge in Cav supplier Hesperidin 1 and pCav 1 is just a direct effect of reduced p53 amounts in MCF 7As53 cells. When p53 was overexpressed in these cells, the Cav1 levels decreased and correspondingly pCav 1 levels also decreased. These results obviously are indicative of a strong relationship between Cav 1 term and p53 amounts, in addition to its service. Furthermore, immunofluorescent studies also confirm that Cav 1 is overexpressed and its superior localization may be detected on the cell membrane in MCF 7As53 cells, in comparison with MCF 7 cells. To analyze whether constitutively upregulated Cav 1 activity is indeed responsible for activation of Akt, we addressed the cells with cholesterol wearing agent MCD that is proven to downregulate Mitochondrion pCav 1 levels without affecting its basal expression. Following MCD therapy, we observed that the decrease in Akt action correlated with the decrease in phosphorylation of Cav 1. Furthermore, to show a direct relationship between Cav 1 and Akt activation, we transfected MCF 7As53 cells with Cav 1 siRNA. Cav 1 levels decreased, when Cav 1 siRNA was introduced in to the cells and correspondingly pAkt levels also decreased. No decline in either Cav 1 level or pAkt level was detected in the cells that were transfected with the control siRNA. Consequently, we also conducted the test in MCF 7 in-which p53 activity was inhibited either by PFT, a inhibitor of p53 treatment, or by silencing the AP26113 p53 information using p53 siRNA. Not surprisingly p53 siRNA phrase decreases p53 protein levels. We discovered that Cav 1 in addition to pAkt levels increased in-the cells in which p53 was inactivated by PFT and also in the cells which were transfected with p53 siRNA, as compared with mock transfected MCF 7 cells. Further to examine the inter connection between p53 status and Cav 1 expression in MCF 7 cells as well as other breast cancer cells, we compared the expression levels of Cav 1 in MCF 7 cells, in MCF 7 cells treated with PFT, MCF 7As53 cells and in other breast cancer cells including MDA MB 231 or MDA MB 468 which express mutant p53.