| First Author | Sarin A | Year | 1997 |
| Journal | Immunity | Volume | 6 |
| Issue | 2 | Pages | 209-15 |
| PubMed ID | 9047242 | Mgi Jnum | J:38709 |
| Mgi Id | MGI:86091 | Doi | 10.1016/s1074-7613(00)80427-6 |
| Citation | Sarin A, et al. (1997) Target cell lysis by CTL granule exocytosis is independent of ICE/Ced-3 family proteases. Immunity 6(2):209-15 |
| abstractText | Activation of ICE/Ced-3 family proteases (caspases) has been proposed to mediate both the granule exocytosis and Fas-Fas ligand pathways of rapid target cell death by cytotoxic T lymphocytes. In agreement with this model, two peptide fluoromethyl ketone caspase inhibitors and baculovirus p35 blocked apoptotic nuclear damage and target cell lysis by the CTL-mediated Fas-Fas ligand pathway. The peptide caspase inhibitors also blocked drug-induced apoptotic cell death in tumor cells. In contrast, the caspase inhibitors blocked CTL granule exocytosis-induced target apoptotic nuclear damage, but did not inhibit target lysis. These results are consistent with recent demonstrations that granzyme B can activate caspases leading to apoptotic nuclear damage, but show that target cell lysis by CTL granule exocytosis occurs by a caspase-independent pathway. |
