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Publication : Processing and activation of CMH-1 by granzyme B.

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.
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