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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

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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

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Corresponding author

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

Publication History

Received:
March 7, 2006
Accepted:
May 4, 2006
Published Online:
2006-08-09

Abstract

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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[1]
Jie Zhang and Guo-Ping Shi
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[2]
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Pharmacology & Therapeutics, 2011, Volume 131, Number 3, Page 338
[3]
Sarah E. Ewald, Bettina L. Lee, Laura Lau, Katherine E. Wickliffe, Guo-Ping Shi, Harold A. Chapman, and Gregory M. Barton
Nature, 2008, Volume 456, Number 7222, Page 658
[4]
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