J1-5449 — Annual report 2015
1.
Fast profiling of protease specificity reveals similar substrate specificities for cathepsins K, L and S

In this report we presented a fast and straightforward approach for profiling of protease specificity. This method was applied for the profiling of cathepsins K, S.

COBISS.SI-ID: 28342823
2.
Proteomic identification of cysteine cathepsin substrates shed from the surface of cancer cell

In this report we haver shown that cysteine cathepsins can act like shedases and cleave protein ectodomains from the cell surface. Proteomic analysis of various cell types has shown that cysteine cathepsins can shed structurally closely related group of cell adhesion molecules and membrane receptors. Observed substrate cleavages were confirmed also in vivo in murine cancer model.

COBISS.SI-ID: 28696103