Previous studies showed that induction of apoptosis by diverse antitumor drugs in various cellular systems was from the induction of Bax translocation. In normal cells, the Bax existed in an inactive form mostly in the cytosol but could be induced to alter conformation and translocate into the mitochondria in reaction to certain apoptotic stimuli. The conformationally transformed Bax protein oligomerized on the outer mitochondrial membrane and caused the release of apoptogenic molecules into the cytoplasm. To ascertain whether Bax translocation was involved with apoptosis, we conducted Western blot analysis and subcellular fractionation on HepG2 cells infected by Ad TIP30 at several time intervals. This conclusion was based on-the subsequent observations: Ad TIP30 therapy causes a Celecoxib solubility translocation of Bax in wild typ-e cells, the HepG2/Baxsi cells prevented TIP30 induced HCC cell death in comparison to HepG2/controlsi cells, and data indicated that membrane translocation of Bax resulted in activation of caspase 3 and PARP. These data suggested that translocation of Bax was necessary and adequate for full control mitochondrial cascade in-the TIP30mediated cell death process. It was more successful in the literature that Bcl xL was highly expressed inmany cell forms, especially inHCC cells. It possesses properties of attenuating cell death in the mitochondrial level, preventing the loss of frm and the release of cytochrome c. Indeed, weight to chemotherapywas associated with increased amounts Meristem of the mitochondria defending meats Bcl 2 and Bcl xL. Previous studies demonstrated that ectopic expression of Bcl xL in cancer cells conferred resistance to apoptosis against a number of death causing agents. Similarly, our data suggested that contaminated by Ad TIP30, Bcl xL protein level decreased in HepG2 cells, implying that overexpression of TIP30 may trigger apoptosis at the least by down regulating Bcl xL in HCC cells. Changes in the frm were retarded by overexpression of Bcl xL, which led to a marked delay in the kinetics of apoptosis. It would be consistent with induction of improvements in Bax by Ad TIP30. In conclusion, overexpression of Bcl xL was associated with suppression of cytochrome c/Smac/DIABLO release. Among the important regulatory steps for apoptosis may be the activation of caspase. Many important intracellular substrates were then cleaved by active p53 ubiquitination caspase, resulting in the characteristic morphological changes connected with apoptotic cells. To determine whether mitochondiral/caspase 9 process was stimulated in AdTIP30 induced apoptosis in HepG2 cells, we reviewed the product of caspase 3, 9 and PARP by western blotting. The result confirmed that in HepG2 cells, both caspases were activated during apoptosis as judged by appearance of cleavage products from procaspase.