3.4.18.1: cathepsin X
This is an abbreviated version!
For detailed information about cathepsin X, go to the full flat file.
Word Map on EC 3.4.18.1
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3.4.18.1
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cathepsins
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papain-like
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procathepsins
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saitoi
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diagnostics
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galactosialidosis
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medicine
- 3.4.18.1
- cathepsins
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papain-like
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procathepsins
- saitoi
- diagnostics
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galactosialidosis
- medicine
Reaction
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity =
Synonyms
acid carboxypeptidase, cathepsin B2, cathepsin IV, cathepsin P, cathepsin X, cathepsin Z, CATX, CTPZ, CTSX, CTSZ, cysteine-type carboxypeptidase, lysosomal carboxypeptidase B, mopre, PoCtX
ECTree
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General Information
General Information on EC 3.4.18.1 - cathepsin X
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malfunction
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
physiological function
cathepsin X prevents an effective immune response against Helicobacter pylori infection of THP-1 cells, overview
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
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
physiological function
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cathepsin X generates peptide receptor agonists and acts as a type I kininase. It is a cysteine-type carboxypeptidase and able to modulate the kallikreinkinin system through carboxyterminal processing of the small peptide hormones bradykinin and kallidin. Cathepsin X as an alternative possible link between the kallikreinkinin system and the reninangiotensin 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
physiological function
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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
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
physiological function
cysteine cathepsin proteases are primarily involved in endolysosomal degradation, but also function extracellularly and in the nucleus. Cathepsin X is secreted by human osteoblasts, digests CXCL-12 and impairs adhesion of hematopoietic stem and progenitor cells, i.e. HSPC s, to osteoblasts. Cathepsin X can influence HSPC trafficking in the bone marrow
physiological function
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synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice, overview
physiological function
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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
physiological function
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downregulation of cathepsin X expression by siRNA attenuates the neuronal death caused by 6-hydroxydopamine. Treatment with specific cathepsin X inhibitor AMS36 protects cells against 6-hydroxydopamine mediated cytotoxicity, resulting in reduced cell death and apoptosis.Inhibitor AMS36 reverses 6-hydroxydopamine-induced loss of tyrosine hydroxylase and attenuates 6-hydroxydopamine-induced activation of caspase-3. Cathepsin X may be responsible for dopamine neuron death, involved in the pathogenic cascade event for the neurodegenerative disorders, such as Parkinson's disease
physiological function
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RNAi for cathepsins L and Z confirms that they are critical in degrading polyglutamine-rich proteins (expanded huntingtin exon 1) but not other types of aggregation-prone proteins
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
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
physiological function
cathepsins X promotes epithelial-mesenchymal transition of tumor cells
physiological function
the molecular target of cathepsin X in tumor cells is profilin 1, a known tumor suppressor and regulator of actin cytoskeleton dynamics. Cathepsin X cleaves off the C-terminal Tyr139 of profilin 1, 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
physiological function
up-regulated expression and increased release and activity of microglial cathepsin X leads to microglia activation-mediated neurodegeneration