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Buchner, Johannes

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

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

Jon Mallen-St. Clair1 / Guo-Ping Shi2 / Rachel E. Sutherland3 / Harold A. Chapman4 / George H. Caughey5 / Paul J. Wolters6







Corresponding author

Citation Information: Biological Chemistry. Volume 387, Issue 8, Pages 1143–1146, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.141, August 2006

Publication History

March 7, 2006
May 4, 2006
Published Online:


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.

Keywords: chymase; cysteine protease; mast cell; papain

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