Bcl 2 and Bcl xL have now been proven to inhibit Bax translocation, caspase activation and cytochrome c release induced by Fas or other apoptotic inducing agents. A few recent studies show that overexpressing Bcl 2 or Bcl xL inhibits ceramide deposition during apoptosis induced by chemotherapeutic agents, irradiation, or hypoxia. In contrast, Bax had no e?ect on ceramide creation during etoposide induced apoptosis, but increased etoposide induced apoptosis through acceleration of cytochrome c release and caspases service. These results show that Bax might act downstream o-r independent of ceramide to directly activate the release of cytochrome c. To date=june 2011 the position of Bax in the regulation of ceramide caused apoptosis, we used Bax antisense oligodeoxynucleotides angiogenesis in vitro to diminish intracellular Bax degrees. We demonstrated that treatment of HL 60 cells with Bax antisense avoided PARP cleavage, cytochrome c release and ceramide activated apoptosis. Our data suggest that Bax serves downstream of ceramide to induce cytochrome c release, providing direct evidence for a position of Bax in the apoptotic pathway mediated by ceramide. The mechanism by which ceramide causes Bax dependent apoptosis has not yet been decided. Recent studies suggest that variations in the relation between proapoptotic and antiapoptotic members of the Bcl 2 family, rather than the absolute term level of any single Bcl 2 member, may decide apoptotic sensitivity, which may restrict the supply Mitochondrion and translocation of the Bax protein from the cytoplasm to the mitochondria. It was also noted that overexpression of Bcl 2 or Bcl xL secured against ceramide induced apoptosis. Previously, we noted ceramide enhanced Bax/Bcl 2 ratio in HL 60 cells. Here, we observed decreased Bcl xL term with an upsurge in the Bax/Bcl xL ratio in ceramidetreated HL 60 cells. Consequently, it is proposed that the e?ect of Bax on ceramide mediated apoptosis might be linked to the decreased quantities of proapoptotic members of the Bcl 2 family, thus weakening the death defending signaling during apoptosis. The ratio of Bax and Bcl xL protein levels is vital for cells under-going apoptosis, since Bcl xL and Bax act antagonistically in-the regulation of apoptosis. Current data suggest that ceramide might indicate mitochondrial apoptosis Imatinib solubility by inhibiting the protein kinase Akt, which phosphorylates Bad. Phosphorylation of Bad via growth factor receptor signaling and the Akt kinase releases Bcl xL to a target mitochondria. Ergo, inhibition of Akt by ceramide results in inhibition of antiapoptotic protein Bcl xL by Bad. Depending on these observations, it’s postulated that ceramide may induce apoptosis by decreasing antiapoptotic signaling and improving proapoptotic signaling, ultimately causing disruption of the balance of proapoptotic and antiapoptotic signaling within the cell.