3.4.18.1 malfunction cathepsin X prevents an effective immune response against Helicobacter pylori infection of THP-1 cells, overview 708373 3.4.18.1 malfunction more profilin 1-clathrin complexes are present in PC-3 cells when cathepsin X is inhibited by its specific inhibitor AMS36 or silenced by siRNA. As a consequence, the endocytosis of FITC-labeled dextran and transferrin conjugate is significantly increased 755099 3.4.18.1 metabolism there is a significant release of cathepsin X from activated BV2 and EOC 13.31 cells following a lipopolysaccharide stimulus that coincides with reduced release of the active form of gamma-enolase 754902 3.4.18.1 physiological function 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 ?2 integrin receptor, LFA-1, 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. Role of cathepsin X in cell signaling, detailed overview 708023 3.4.18.1 physiological function cathepsin B2 is expressed only in early stages of the parasite and may be involved in digestion of host connective tissues and evasion of the host immune system during their penetration and migration 731770 3.4.18.1 physiological function cathepsin X cleaves profilin 1 C-terminal Tyr1391, affecting binding of poly-L-proline ligands and, consequently, tumor cell migration and invasion. Tyr139 is important for proper function of profilin 1 as a tumor suppressor. Cleaving off Tyr139 prevents the binding of clathrin, a poly-L-proline ligand involved in endocytosis 755099 3.4.18.1 physiological function cathepsin X generates peptide receptor agonists and acts as a type I kininase. It is a cysteine-type carboxypeptidase and able to modulate the kallikrein–kinin system through carboxyterminal processing of the small peptide hormones bradykinin and kallidin. Cathepsin X as an alternative possible link between the kallikrein–kinin system and the renin–angiotensin system in that it not only cleaves kinins C-terminally, but also converts angiotensin I to angiotensin II, reaction of EC 3.6.15.1 708738 3.4.18.1 physiological function cathepsin X plays an important role in the pathogenes of atherosclerosis. It aids in the migration of T-lymphocytes and the release of cytokines. Cathepsin X may aid in the migration of immune cells within the lesion and is predominately implicated in T-lymphocyte signaling and secretion of cytokines that stimulate the proliferation of smooth muscle cells. It may also play a role in localizing inflammatory cells to the shoulder of unstable plaques 752431 3.4.18.1 physiological function cathepsin X, a cysteine protease, regulates T-cell migration by interaction with lymphocyte function associated antigen-1, LFA-1. Gradual cleavage of LFA-1 by cathepsin X enables the transition between intermediate and high affinity LFA-1, an event that is crucial for effective T-cell migration, overview 708379 3.4.18.1 physiological function cathepsin X-mediated beta2 integrin activation results in membrane nanotube outgrowth, nanotube structures and mechanism of membrane nanotube formation in T cells through LFA-1 integrin activation by the cysteine protease cathepsin X, mechanism of nanotube formation follows homotypic T cell contact formation,mechanism pf LFA-1 iuntegrin activation, overview 708056