Kallikrein-related proteases (KLKs) play a critical role in epidermis physiology and have been implicated in skin pathologies such as Netherton syndrome. The contribution of individual KLKs to skin proteolysis is poorly understood. Monitoring of their activities in skin proteome is hampered by overlapping substrate specificities, and there is a need for novel assays. Here, we present a platform of selective and sensitive fluorogenic substrates and inhibitors for profiling KLK5, KLK7 and KLK14. These chemical tools were evaluated using recombinant KLKs and tissue from a unique set of mice deficient in eight combinations of KLKs and their natural regulator LEKTI.

Czech Centre for Phenogenomics Institute of Molecular Genetics of the ASCR Prumyslova 595 252 50 Vestec Czech Republic

Department of Biochemistry Faculty of Science Charles University Hlavova 2030 8 128 00 Prague Czech Republic

Institute of Organic Chemistry and Biochemistry The Czech Academy of Sciences Flemingovo n 2 166 10 Prague Czech Republic

Laboratory of Transgenic Models of Diseases Institute of Molecular Genetics of the ASCR Prumyslova 595 252 50 Vestec Czech Republic

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Structural studies of complexes of kallikrein 4 with wild-type and mutated forms of the Kunitz-type inhibitor BbKI

Crystal structures of the complex of a kallikrein inhibitor from Bauhinia bauhinioides with trypsin and modeling of kallikrein complexes