Apoptosis, programmed cell death, has been shown to play a major role in maintaining normal cellular and tissue physiology and morphology. As such, an altered state of apoptosis has been linked to several biological and pathological conditions. Elucidating the underlying mechanisms of programed cell death, consequently, may one day facilitate cures for a myriad of disorders ranging from Parkinsons Disease to cancer, lymphomas to auto immune deficiency syndrome (AIDS). Among the many mechanisms for the signal transduction of apoptosis that have been proposed, the ceramide-induced pathway has emerged as a strong candidate. Phosphatases and mitochondria have recently been implicated in ceramide-induced programmed cell death. The precise mechanism by which they impose their effects, however, remain unclear. To further elucidate the role of the phosphatases and mitochondria in apoptotic pathways, we treated molt-4 leukemia cells with ceramide, calyculin A (a phosphatase inhibitor), and rotenone (a mitochondrial inhibitor of complex 1 of the electron transport chain). Western blot analysis illuminanted the release of proteolysis and cytochrome c in treated cells. Consequently, 

Introduction 

Programmed cell death, apoptosis, has been the subject of intense research due to the elucidation of its role in a myriad of biological and pathological conditions. Distinguished from necrosis, the process by which accidental cell death occurs due to acute injury (mechanical or chemical), by Kerr et al. (1972), apoptosis has been shown to play a central role in normal developmental and cellular processes. In tissues, apoptosis affects scattered individual cells in contrast to the tracts of contiguous cells affected by necrosis (McKenna, 1996). Consequently, the potential importance of apoptosis is immense. Defective apoptotic machinery may contribute to numerous diseases. Specifically, loss or degregulation of apoptotic pathways may be a causal factor in cancer proliferation and a multitude of autoimmune disorders, whereas