We presented that human primary NK cells induce lysis of carcinoma and carcinoma stem cells, while anti-CD16 antibody and monocytes induce functional split anergy by decreasing the cytotoxicfunction of NK cells. In this cell model we demonstrated that the levels of truncated monomeric cystatin F, which is known to inhibit the functions of cathepsins C and H, is significantly elevated in anergized primary NK cells. Furthermore, cystatin F co-localizes with cathepsins C and H in the lysosomal/endosomal vesicles of NK cells. Accordingly, the mature forms of cathepsins C and H, which regulate the activation of effector granzymes in NK cells, are significantly decreased.
COBISS.SI-ID: 3878769
Lectins specifically recognize carbohydrate moeties and thus regulate the action of other biological molecules. They are becoming inportant as regulators of the immune cells. In this study we showed direct interaction between lectins and protease inhibitors as a consequence of similar beta-trefoil structure, which could have an impact on the role of glycosilated protease inhibitors in immune processes.
COBISS.SI-ID: 28421927
Lysosomal cysteine peptidases - cysteine cathepsins - are general intracellular protein-degrading enzymes that control also a variety of specific physiological processes. They can trigger irreversible events leading to signal transduction and activation of signaling pathways, resulting in cell survival and proliferation or cell death. In cancer cells, lysosomal cysteine peptidases are involved in multiple processes during malignant progression.
COBISS.SI-ID: 3908977