Details

Autor(en) / Beteiligte

• Gu, Y
• Sarnecki, C
• Fleming, M A
• Lippke, J A
• Bleackley, R C
• Su, M S

Titel

Processing and Activation of CMH-1 by Granzyme B

Ist Teil von

• The Journal of biological chemistry, 1996-05, Vol.271 (18), p.10816-10820

Ort / Verlag

United States: American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1996

Quelle

MEDLINE

Beschreibungen/Notizen

• 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-1β-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 Asp -Ser between the p20 and p12 and activates the cysteine protease. Cleavage between p20 and the prosequence of CMH-1 at Asp -Ala is autocatalytic and is not required for CMH-1 activity in vitro . The cleavage and activation of CMH-1 by granzyme B in vitro suggest that, in addition to CPP32, CMH-1 may also play a role in CTL-mediated cell killing.