Cathepsin S is a cysteine protease responsible for many pathological conditions and diseases, including cancer. It is also known as one of the proteases capable of cleaving CD74 in endosomes. CD74 is a chaperone participating in MHC class II assembly. As a receptor in plasma membrane, it functions as a binding site for MIF, with different signalling pathways, including NF-κB and kinase cascades, such as ERK, PI3K-Akt, and AMPK, which play a role in inflammation. Cathepsin S and CD74 are expressed in numerous types of cells, including macrophages and monocytes. This thesis compares the expression of cahtepsin S and CD74 in macrophages M0 and monocytes THP-1 and describes the effect of substance P. The expression of cathepsin S is higher than that of CD74. The expression levels of both proteins were higher in monocytes, with substance P having no effect. In macrophages, the expression increased with prolonged treatment of cells with substance P. These results provide the basis for future analysis of cathepsin S and CD74 expression, as well as the effects of substance P.
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