| First Author | Enari M | Year | 1998 |
| Journal | Nature | Volume | 391 |
| Issue | 6662 | Pages | 43-50 |
| PubMed ID | 9422506 | Mgi Jnum | J:45015 |
| Mgi Id | MGI:1101626 | Doi | 10.1038/34112 |
| Citation | Enari M, et al. (1998) A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD [see comments]. Nature 391(6662):43-50 |
| abstractText | The homeostasis of animals is regulated not only by the growth and differentiation of cells, but also by cell death through a process known as apoptosis. Apoptosis is mediated by members of the caspase family of proteases, and eventually causes the degradation of chromosomal DNA. A caspase-activated deoxyribonuclease (CAD) and its inhibitor (ICAD) have now been identified in the cytoplasmic fraction of mouse lymphoma cells. CAD is a protein of 343 amino acids which carries a nuclear-localization signal; ICAD exists in a long and a short form. Recombinant ICAD specifically inhibits CAD-induced degradation of nuclear DNA and its DNase activity. When CAD is expressed with ICAD in COS cells or in a cell-free system, CAD is produced as a complex with ICAD: treatment with caspase 3 releases the DNase activity which causes DNA fragmentation in nuclei. ICAD therefore seems to function as a chaperone for CAD during its synthesis, remaining complexed with CAD to inhibit its DNase activity; caspases activated by apoptotic stimuli then cleave ICAD, allowing CAD to enter the nucleus and degrade chromosomal DNA. |
