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Licensed Unlicensed Requires Authentication Published by De Gruyter March 23, 2018

Kallikrein-related peptidase 14 is the second KLK protease targeted by the serpin vaspin

  • David Ulbricht , Catherine A. Tindall , Kathrin Oertwig , Stefanie Hanke , Norbert Sträter and John T. Heiker EMAIL logo
From the journal Biological Chemistry


Kallikrein-related peptidases KLK5, KLK7 and KLK14 are important proteases in skin desquamation and aberrant KLK activity is associated with inflammatory skin diseases such as Netherton syndrome but also with various serious forms of cancer. Previously, we have identified KLK7 as the first protease target of vaspin (Serpin A12). Here, we report KLK14 as a second KLK protease to be inhibited by vaspin. In conclusion, vaspin represents a multi-specific serpin targeting the kallikrein proteases KLK7 and KLK14, with distinct exosites regulating recognition of these target proteases and opposing effects of heparin binding on the inhibition reaction.


The vaspin expression plasmid was a kind gift of Dr. J. Wada (Department of Medicine and Clinical Science Okayama University Graduate School of Medicine, Okayama, Japan). This work was funded by grants of the Deutsche Forschungsgemeinschaft SFB1052, ‘Obesity Mechanisms’ (Funder Id: 10.13039/501100001659, C4 NS, C7 JTH).

  1. Conflict of interest statement: The authors declare that they have no conflicts of interest regarding the contents of this article.


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Supplementary Material:

The online version of this article offers supplementary material (

Received: 2018-01-08
Accepted: 2018-02-23
Published Online: 2018-03-23
Published in Print: 2018-09-25

©2018 Walter de Gruyter GmbH, Berlin/Boston

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