BAX-induced cell death does not require interleukin 1β-converting enzyme (ICE)-like proteases. Expression of BAX alone is sufficient to induce apoptosis, involving the activation of ICE-like proteases and cleavage of substrates such as poly(ADP ribose) polymerase (PARP) and D4-GDI. However, inhibition of these proteases with zVAD-fmk prevented PARP and D4-GDI cleavage and DNA fragmentation but did not block BAX-induced cell death. This suggests that while ICE-like proteases are involved in some aspects of BAX-induced apoptosis, they are not essential for the overall process. BAX, a member of the Bcl-2 family, functions as a death agonist in a common apoptotic pathway. It forms homodimers and heterodimers with BCL-2 and BCL-XL. The ratio of BCL-2 family death agonists to antagonists determines cell susceptibility to apoptosis. BAX can induce apoptosis in the absence of other death signals, as shown in Bax-deficient mice. ICE-like proteases are activated in apoptosis and are required for certain aspects of cell death. In mammals, several ICE-like proteases, including CPP32, MCH2, and ICH-1, are involved in apoptosis. However, BAX-induced apoptosis does not require these proteases for cell death, as evidenced by the fact that zVAD-fmk, an inhibitor of ICE-like proteases, did not prevent BAX-induced cell death. BAX-induced apoptosis involves changes in mitochondrial function, including a decrease in mitochondrial membrane potential and the production of reactive oxygen species (ROS). These changes occur independently of ICE-like protease activity, suggesting that BAX may initiate apoptosis through a non-proteolytic pathway involving mitochondrial dysfunction. The study highlights that while ICE-like proteases are involved in some aspects of apoptosis, BAX-induced cell death can proceed through a pathway that does not require these proteases. This suggests that BAX may initiate apoptosis through a distinct mechanism involving mitochondrial dysfunction.BAX-induced cell death does not require interleukin 1β-converting enzyme (ICE)-like proteases. Expression of BAX alone is sufficient to induce apoptosis, involving the activation of ICE-like proteases and cleavage of substrates such as poly(ADP ribose) polymerase (PARP) and D4-GDI. However, inhibition of these proteases with zVAD-fmk prevented PARP and D4-GDI cleavage and DNA fragmentation but did not block BAX-induced cell death. This suggests that while ICE-like proteases are involved in some aspects of BAX-induced apoptosis, they are not essential for the overall process. BAX, a member of the Bcl-2 family, functions as a death agonist in a common apoptotic pathway. It forms homodimers and heterodimers with BCL-2 and BCL-XL. The ratio of BCL-2 family death agonists to antagonists determines cell susceptibility to apoptosis. BAX can induce apoptosis in the absence of other death signals, as shown in Bax-deficient mice. ICE-like proteases are activated in apoptosis and are required for certain aspects of cell death. In mammals, several ICE-like proteases, including CPP32, MCH2, and ICH-1, are involved in apoptosis. However, BAX-induced apoptosis does not require these proteases for cell death, as evidenced by the fact that zVAD-fmk, an inhibitor of ICE-like proteases, did not prevent BAX-induced cell death. BAX-induced apoptosis involves changes in mitochondrial function, including a decrease in mitochondrial membrane potential and the production of reactive oxygen species (ROS). These changes occur independently of ICE-like protease activity, suggesting that BAX may initiate apoptosis through a non-proteolytic pathway involving mitochondrial dysfunction. The study highlights that while ICE-like proteases are involved in some aspects of apoptosis, BAX-induced cell death can proceed through a pathway that does not require these proteases. This suggests that BAX may initiate apoptosis through a distinct mechanism involving mitochondrial dysfunction.