Harmful cells’, such as cancerous cells, growth depends on evasion of apoptosis, which is considered as one of the hallmarks of cancer. Apoptosis is ultimately carried out by the sequential activation of initiator and executioner caspases, which constitute a family of intracellular proteases involved in dismantling the cell in an ordered fashion. In cancer, therefore, one would anticipate caspases to be frequently rendered inactive, either by gene silencing or by somatic mutations. From clinical data, however, there is little evidence that caspase genes are impaired in cancer. Executioner caspases have only rarely been found mutated or silenced, and also initiator caspases are only affected in particular types of cancer. There is experimental evidence from transgenic mice that certain initiator caspases, such as caspase-8 and -2, might act as tumor suppressors. Caspase-2, the most conserved member of the caspase family, has long been recognized as an important protein in the regulation of apoptosis. Caspase-2 is activated upon genotoxic stress in a large protein complex termed the PIDDosome (Tinel and Tschopp, 2004). For this reason, we study and analyzed 2 exons of the human caspase-2 gene, using a strategy combining gene expression based RT-PCR amplification to investigate the associations between prostate cancer and caspase-2 gene expression in 9 individulas with prostate cancer. As a result of working, the level of variant-1 and variant-2 of caspase-2 gene expression in prostate cancer tissues was shown to be lower than in the control specimens and β-actin gene. Expression levels of β-actin were used as internal positive control. It has been demonstrated that the restoration of caspase-2 deficient cancer tissues augments their sensitivity to undergo apoptosis in response to chemotherapeutic agents and to other apoptotic inducers. Consistent