| First Author | Korfali N | Year | 2004 |
| Journal | J Biol Chem | Volume | 279 |
| Issue | 2 | Pages | 1030-9 |
| PubMed ID | 14583630 | Mgi Jnum | J:87720 |
| Mgi Id | MGI:3027461 | Doi | 10.1074/jbc.M306277200 |
| Citation | Korfali N, et al. (2004) Caspase-7 gene disruption reveals an involvement of the enzyme during the early stages of apoptosis. J Biol Chem 279(2):1030-9 |
| abstractText | Caspases play a key role during apoptotic execution. In an attempt to elucidate the specific role of caspase-7 we generated a chicken DT40 cell line in which both alleles of the gene were disrupted. Viability assays showed that caspase-7-/- clones are more resistant to the common apoptosis-inducing drugs etoposide and staurosporine. Caspase-7-/- cells show a delay in phosphatidylserine externalization and DNA fragmentation as well as cleavage of the caspase substrates poly(ADP-ribose) polymerase 1 and lamins B1 and B2. Caspase affinity labeling and activity assays indicated that deficient cells exhibit a delay in caspase activation compared with wild type DT40 cells, providing an explanation for the differences in apoptotic execution between caspase-7 null and wild type DT40 cells. These results strongly suggest that caspase-7 is involved earlier than other effector caspases in the apoptotic execution process in DT40 B lymphocytes. |
