First Author | Gu Y | Year | 1996 |
Journal | J Biol Chem | Volume | 271 |
Issue | 18 | Pages | 10816-20 |
PubMed ID | 8631895 | Mgi Jnum | J:32909 |
Mgi Id | MGI:80396 | Doi | 10.1074/jbc.271.18.10816 |
Citation | Gu Y, et al. (1996) Processing and activation of CMH-1 by granzyme B. J Biol Chem 271(18):10816-20 |
abstractText | Granzyme B plays an essential role in cytotoxic T lymphocyte (CTL)-mediated cell killing. Recent studies suggest that granzyme B may exert its effect by cleaving and activating CPP32, a member of the interleukin-1 beta-converting enzyme/Ced-3 family of cysteine proteases. We have examined the processing and activation of CMH-1, a close homologue of CPP32, by granzyme B in vitro. We have found that granzyme B specifically cleaves CMH-1 at Asp198-Ser199 between the p20 and p12 and activates the cysteine protease. Cleavage between p20 and the prosequence of CMH-1 at Asp23-Ala24 is autocatalytic and is not required for CMH-1 activity in vitro. The cleavage and activation of CMH-1 by granzyme B in vitro sugge st that, in addition to CPP32, CMH-1 may also play a role in CTL-mediated cell killing. |