The majority of HCC cell lines possess at least one genetic alteration in Fas pathway molecules, which inhibit Fas-mediated apoptosis. For example, Fas ligand interacts with the Fas receptor, causing caspase-8 and caspase-10 activation. Engagement of mFas via the Fas-associated death domain protein is necessary for activation of caspase-8. Active caspase-8 and caspase-10 directly cleave and activate downstream effector proteases, such as caspase-3, causing apoptosis. The present study showed that the expression of the receptor Fas and FADD and the downstream protein of caspase-10 and caspase-8 were activated and led to the release of the caspase-8 active fragments, p18 and p10, which had increased expression in Pokemon-silenced cells after treatment with oxaliplatin. Activated caspase-8 AbMole Trihexyphenidyl HCl cleaves and activates downstream effector caspases, such as caspase-9 and caspase-3, which were up-regulated in the HepG2 si-Pokemon cells compared to the controls. In addition, caspase-8 and caspase10 have the ability to cleave the Bcl-2 family member Bid into truncated Bid, thereby resulting in disruption and release of cytochrome c. Therefore, Pokemon might be a critical mediator of crosstalk between the intrinsic and extrinsic apoptotic pathways in HCC cells. A normal cell maintains its entry and exit into cell cycle by several checkpoints and “licensing” its DNA replication only once per cell cycle. This licensing mechanism includes the formation of pre-replication complexes in late M and early G1 phases and their subsequent activation at the G1-S boundary. The pre-RCs mark the replication origins and control bidirectional DNA synthesis from these origins when S phase is initiated. Pre-RC assembly involves sequential recruitment of several proteins on replication origin. The reaction starts by the initial binding of origin recognition complex. Subsequent binding of CDC6 and CDT1 provide a landing pad for the further recruitment of putative DNA helicases as Minichromosome Maintenance 2-7 complex. Other important members of pre-RC are MCM10 and RECQL4. At the G1-S transition, the activity of two kinases, CDC7 and cyclins E/A-CDK2, recruit additional factors to pre-RCs, resulting in the formation of pre-initiation complexes. Additionally, CDC7 and CDK2 activate the MCM2-7 helicases, which together with formation of pre-IC result in recruitment of DNA polymerases and initiation of DNA replication. Paradoxically, during late S and M phases, high activity of cyclin-dependent kinase results in dissolution of the pre-RCs and destruction of selective pre-RC components, thereby preventing DNA re-replication. MCM proteins were first recognized in the yeast Saccharomyces cerevisiae as mutants defective in the maintenance of mini chromosomes, suggesting a role in plasmid replication and cell cycle. At least 10 homologues, MCM1-10, have been characterized in humans.