apoptotic process requires permeabilization of the outer mitochondrial membrane and the dissipation of mitochondrial membrane potential. Apoptogenic factors which are within the mitochondrial intermembrane space of healthier cells are introduced into the cytosol where they facilitate the activation of caspases, the executers of the apoptotic death program. Members of the Bcl 2 protein family are the gate keepers of the mitochondrial homeostasis regulating the release of pro apoptotic elements from the mitochondrial intermembrane space into the cytosol. The Bcl 2 protein family includes professional and antiapoptotic members which Imatinib STI-571 have the ability to form heterodimers. Among others, the anti apoptotic team entails Bcl 2, Bcl xL, Mcl 1, and A1 which are often observed to be over expressed in tumor cells. The pro apoptotic group is split in numerous domain proteins which reveal three Bcl 2 homologous domains and the BH3 only proteins which have only the BH3 domain in common. The activation of the multi domain proteins is absolutely essential for mitochondrial permeabilization and apoptosis induction. Currently, two ideas exist which describe the contribution of the various anti apoptotic and BH3 only proteins leading to activation of Bak/Bax like proteins. In the model, the multidomain proteins are neutralized by the antiapoptotic Bcl Lymphatic system 2 family members in healthy cells. Upon apoptosis induction, BH3 only proteins bind to the anti apoptotic ones therefore displacing Bax or Bak allowing them to be stimulated through spontaneous self oligomerization. The direct activation or hierarchical model discernes BH3 only protein activators and sensitizers. The former bind to all anti apoptotic proteins with similar affinity as well as to the pro apoptotic multidomain proteins while the latter do not interact with Bax/ Bak like proteins. Furthermore, sensitizer BH3 only meats display specific binding tastes to the anti apoptotic ones. Therefore associates Noxa with Mcl 1 and A1 only while Bad interacts with Bcl 2 and Bcl xL. In healthy cells, the activators are sequestered by the anti apoptotic proteins. A specific PFI-1 clinical trial apoptotic stimulation activates a distinct set of sensitizer proteins which, in turn, bind their favored anti apoptotic partners. The activator proteins, when produced from their sequestration, bind to the Bax/Bak like proteins to induce their oligomerization. Our previous investigations demonstrate that Celecoxib induced apoptosis through the Noxa/Mcl 1 axis in Jurkat T cell lymphoma cells ultimately causing downregulation of Mcl 1. The destruction of Mcl 1 protein levels was adequate to induce apoptosis in this cell system. Interestingly, overexpression of Bcl xL although not Bcl 2 can avoid induction of apoptosis in a reaction to Celecoxib.