Apoptosis, the process of programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms and involves dramatic changes in cellular structure. Disruption of apoptosis may contribute to cancer and to autoimmune and degenerative diseases. Apoptosis is induced by a family of cell death receptors and their corresponding ligands. Cell death signals are then transduced by adapter molecules and members of the caspase (ICE/CED-3) family of cysteine proteases that eventually lead to the degradation of chromosomal DNA by activated DNase. Recently identified was a mouse DNase that causes apoptotic DNA fragmentation and was designated CAD (for caspase activated deoxyribonuclease) (1,2). The human homologue of mouse CAD was recently identified by two groups independently and termed CPAN (caspase activated nuclease) and DFF40 (DNA fragmentation fragment 40) (3,4). Human DFF45 and its mouse homologue ICAD are the inhibitors of DFF40 and CAD, respectively (5). DFF is composed of two subunits, DFF40/CAD and DFF45/ICAD. Cleavage of DFF45/ICAD, which is mediated by caspase-3, leads to DFF40/CADís activation as a nuclease (1–4). Activation of DFF40/CAD, which causes DNA degradation, is the hallmark of apoptotic cell death. DFF40 mRNA is expressed in limited number of human tissues; pancreas, spleen, prostate, and ovary (6).
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