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lüll The role of cathepsin X in cell signaling Kos J; Jevnikar Z; Obermajer NCell Adh Migr 2009[Apr]; 3 (2): 164-6Cathepsin X is a lysosomal cysteine protease, found predominantly in cells of monocyte/macrophage lineage. It acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins. In our recent studies we identified-beta(2) subunit of integrin receptors and alpha and gamma enolase as possible substrates for cathepsin X carboxypeptidase activity. In both cases cathepsin X is capable to cleave regulatory motifs at C-terminus affecting the function of targeted molecules. We demonstrated that via activation of beta(2) integrin receptor Mac-1 (CD11b/CD18) active cathepsin X enhances adhesion of monocytes/macrophages to fibrinogen and regulates the phagocytosis. By activation of Mac-1 receptor cathepsin X may regulate also the maturation of dendritic cells, a process, which is crucial in the initiation of adaptive immunity. Cathepsin X activates also the other beta(2) integrin receptor, LFA-1 (CD11a/CD18) which is involved in the proliferation of T lymphocytes. By modulating the activity of LFA-1 cathepsin X causes cytoskeletal rearrangements and morphological changes of T lymphocytes enhancing ameboid-like migration in 2-D and 3-D barriers and increasing homotypic aggregation. The cleavage of C-terminal amino acids of alpha and gamma enolase by cathepsin X abolishes their neurotrophic activity affecting neuronal cell survival and neuritogenesis.|Cathepsin K[MESH]|Cathepsins/*physiology[MESH]|Humans[MESH]|Macrophage-1 Antigen/physiology[MESH]|Phagocytosis/physiology[MESH]|Signal Transduction/*physiology[MESH] |