Nuclear changes in apoptosis.
Specific proteinases of the Ced-3/interleukin-1 beta converting enzyme family trigger a multi-enzyme cascade that drives apoptotic events. Studies with newly developed cell-free systems have begun to identify the substrates of these and other proteinases in apoptosis. Studies with intact cells have revealed that cleavage of the genome into domain-sized fragments precedes the activation of a second nuclease that fragments the DNA into nucleosome-sized pieces.
Earnshaw
W C
WC
Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D029742:Caenorhabditis elegans Proteins; D020170:Caspase 1; D020169:Caspases; D002467:Cell Nucleus / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D004950:Esterases / Q000378:metabolism; D015801:Helminth Proteins / Q000378:metabolism; D006801:Humans; D008938:Mitosis / Q000502:physiology
D029742:Caenorhabditis elegans Proteins; D015801:Helminth Proteins; D004950:Esterases; D010450:Endopeptidases; D020169:Caspases; D003546:Cysteine Endopeptidases; C089223:ced-3 protein, C elegans; D020170:Caspase 1