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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 387, Issue 8 (Aug 2006)

Issues

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

Jon Mallen-St. Clair
  • Department of Medicine and Cardiovascular Research Institute, University of California, San Francisco, CA 94143-0111, USA
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/ Guo-Ping Shi
  • Department of Medicine and Cardiovascular Research Institute, University of California, San Francisco, CA 94143-0111, USA
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/ Rachel E. Sutherland
  • Department of Medicine and Cardiovascular Research Institute, University of California, San Francisco, CA 94143-0111, USA
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/ Harold A. Chapman
  • Department of Medicine and Cardiovascular Research Institute, University of California, San Francisco, CA 94143-0111, USA
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/ George H. Caughey
  • Department of Medicine and Cardiovascular Research Institute, University of California, San Francisco, CA 94143-0111, USA
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/ Paul J. Wolters
  • Department of Medicine and Cardiovascular Research Institute, University of California, San Francisco, CA 94143-0111, USA
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Published Online: 2006-08-09 | DOI: https://doi.org/10.1515/BC.2006.141

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

About the article

Corresponding author


Received: March 7, 2006

Accepted: May 4, 2006

Published Online: 2006-08-09

Published in Print: 2006-08-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.141.

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