A unique family of cysteine proteases has been described that differs in sequence, structure and substrate specificity from any previously described protease family. This family, termed CED-3/ICE, is comprised of ICE, CPP32, ICH-1/Nedd-2, Tx, Mch2, Mch3 (ICE-LAP3 or CMH-1), Mch4 and ICE-LAP6. Ced-3/ICE family members function as key components of the apoptotic machinery and act to destroy specific target proteins which are critical to cellular longevity. Nuclear lamins are critical to maintaining the integrity of the nuclear envelope and cellular morphology. The nuclear Lamin A is cleaved by Mch2, but not CPP32. Nuclear Lamin B is fragmented as a consequence of apoptosis by an unidentified member of the ICE family. Lamin C is a splice variant of Lamin A, differing only at the carboxy-terminus. Lamins A and C are identical for the first 566 amino acids, with Lamin C differing only in six unique carboxy-terminal amino acids.