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The cysteine protease dipeptidyl peptidase I (DPPI) activates granule-associated immune-cell serine proteases. The  in vivo  activator of DPPI itself is unknown; however, cathepsins L and S are candidates because they activate pro-DPPI  in vitro . In this study, we tested whether cathepsins L and S activate pro-DPPI  in vivo  by characterizing DPPI activity and processing in cells lacking cathepsins L and S. DPPI activity, and the relative size and amounts of DPPI heavy and light chains, were identical in mast cells from wild-type and cathepsin L/S double-null mice. Furthermore, the activity of DPPI-dependent chymase was preserved in tissues of cathepsin L/S double-null mice. These results show that neither cathepsin L nor S is required for activation of DPPI and suggest that one or more additional proteases is responsible.

Cathepsins L and S are not required for activation of dipeptidyl peptidase I (cathepsin C) in mice