In this report we have shown cysteine cathepsins can act like sheddases 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
In this report we presented a fast and straightforward approach for profiling of protease specificity. The method was applied for the profiling of cysteine cathepsins K, L and S.
COBISS.SI-ID: 28342823
In this review article we presented the latest methodologies for identification of protease substrates and profiling of protease specificity.
COBISS.SI-ID: 29060647
Cysteine cathepsins are among the major proteases involved in ECM remodeling and their role is not limited to degradation only. In this review we focused in their extracellular functions linked to ECM degradation and discussed their importance in pathologies and treatment of ECM related diseases.
COBISS.SI-ID: 27616039
In this study we have performed proteomic analysis of cancer cell secretome of murine model of mammarian gland cancer. We have identified cathepsin B as the most abundant protease in the secretome.
COBISS.SI-ID: 27932455