Puma was referred to as a only protein with extensive binding spectrum to all anti apoptotic proteins. We did not identify any relationship of angiogenesis drugs with anti apoptotic proteins or with Bak during Celecoxib induced apoptosis, even though it is indicated in healthy Jurkat cells. Curiously, Puma is downregulated during Celecoxib induced apoptosis. The downregulation of Puma was caspase dependent as it was blocked by the pancaspase chemical zVAD. Ergo, the decline of Puma is quite a result of apoptosis induction by Celecoxib and of no value for the first mitochondrial permeabilization. Like Puma, Bim was described to truly have a similar broad binding array to other anti apoptotic Bcl 2 household members. Inside our cell system, however, Bim preferred Bcl 2 to Mcl 1 and Bcl xL. While Bim is released from its sequestration by Mcl 1 and BclxL during Celecoxib induced apoptosis, the connection between Bcl 2 and Bim was not changed during the course. Binding of Bim to Bak in response to Celecoxib wasn’t observed in our cell system. Furthermore, siRNA mediated downregulation of Bim and Puma showed convincingly that neither Bim or Puma were required for Celecoxib induced apoptosis. In contrast, silencing of Bim or Puma increased the survival of Jurkat cells after growth factor withdrawal that will be prior to observations made early in the day. Taken together, our data indicate that the BH3 only proteins Puma, Bid, and Bim are dispensable for the original mitochondrial permeabilization all through Celecoxib induced apoptosis. Because the relationship Eumycetoma between anti apoptotic Bcl 2 members of the family and activator BH3 only proteins is of minor importance, we offer the displacement model for Celecoxib induced apoptosis. This model indicates a of multidomain proteins by the anti apoptotic Bcl 2 household members. Binding of the correct BH3 only proteins to anti apoptotic people displaces the Bax/Bak like proteins letting their service. Jurkat T lymphoma cells do not communicate Bax but Bak. Hence, the service of Bak is vital for Celecoxib induced apoptosis. Our data show a connection of Bak with Mcl 1 or Bcl xL in Jurkat Vector as well as in the Bcl 2 and Bcl xLoverexpressing cells. Using slight lysis circumstances, supplier Celecoxib Bcl 2:Bak things were also recognized in Bcl 2 overexpressing cells. However, the association of Mcl 1 or Bcl xL with Bak was certainly not the same as that of Bcl 2 with Bak. In when 0 contrast to Bcl 2, Bcl xL and Mcl 1 type things also under harsher lysis problems. The next day and 2 weeks Triton X 100 was used indicating a stronger relationship between the latter ones and Bak than between Bcl 2 and Bak. The utilization of Triton X 100 isn’t unproblematic.