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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Cathepsins L and S are not required for activation of dipeptidyl peptidase I (cathepsin C) in mice. Mallen-St Clair, J., Shi, G.P., Sutherland, R.E., Chapman, H.A., Caughey, G.H., Wolters, P.J. Biol. Chem. (2006) [Pubmed]
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