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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Natural Substrates Products on EC 3.4.18.1 - cathepsin X
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REACTION DIAGRAM
alpha-enolase + H2O
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cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
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bradykinin + H2O
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the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
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CXCL-12 + H2O
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CXCL-12 is a physiological substrate for secreted cathepsin X
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gamma-enolase + H2O
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cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase abolishing their neurotrophic activity
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kallidin + H2O
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the peptide is converted from a bradykinin B2 receptor ligand to a bradykinin B1 receptor specific ligand
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lymphocyte function associated antigen-1 + H2O
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cathepsin X cleaves the beta2 cytoplasmic tail of LFA-1 inducing the intermediate affinity form of LFA-1 and alpha-actinin-1 binding. Cleavage by cathepsin X of the amino acid residues S769, E768 and A767 from the C-terminal of the b2 cytoplasmic tail of LFA-1 promotes binding of the actin-binding protein a-actinin-1
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profilin + H2O
L-tyrosine + ?
cathepsin X cleaves profilin 1 C-terminal Tyr139 and influences clathrin-mediated endocytosis. 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
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profilin 1 + H2O
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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
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active cathepsin X mediates the function of beta2 integrin receptors during cell adhesion. It could also be involved in other processes associated with beta2 integrin receptors such as phagocytosis and T cell activation
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additional information
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cathepsin X plays a role not only in the chronic inflammation of gastric mucosa but also in the tumourigenesis of gastric cancer
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additional information
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cathespin X is involved in phagocytosis and regulation of immune response, not involved in degradation of extracellular matrix, a proteolytic event leading to tumor cell invasion and metastasis
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additional information
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cathepsin X binds to the membrane lectin endoplasmic reticulum Golgi intermediate compartment protein-53, ERGIC-53, involving the soluble luminal interaction partner multiple coagulation factor deficiency protein 2, MCFD2, which form a cargo receptor complex in the early secretory pathway, but is dispensable for enzyme binding, overview
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additional information
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luminal protein-protein interactions between components of the cargo system in the endoplasmic reticulum for secretion of cargo proteins, e.g. cathepsin C or cathepsin Z, involve the cargo transport receptor ERGIC-53, i.e. endoplasmic reticulum-Golgi intermediate compartment protein of 53 kDa, with its luminal interaction partner MCFD2, i.e. multiple coagulation factor deficiency protein 2, MCFD2 is not required for the binding of cathepsin Z and cathepsin C to ERGIC-53 in vivo, overview
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additional information
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procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
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additional information
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procathepsin X supports integrin alphavbeta3-dependent attachment and spreading of umbilical vein endothelial cells, overvie
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additional information
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the enzyme is associated with plaques in Alzheimer patients, overview
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additional information
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the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
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additional information
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the enzyme plays a role in immunity to pathogens including Mycobacterium tuberculosis, variation in the melanocortin 3 receptor and cathepsin Z genes play a role in the pathogenesis of tuberculosis in West African populations
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additional information
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the enzyme stimulates macrophage antigen-1 receptor-dependent adhesion and phagocytosis via interaction with integrin beta2 subunit. It plays a role in regulating lymphocyte proliferation via Mac-1 and the other b2 integrin receptor, lymphocyte function-associated antigen-1. Cathepsin X has been shown to suppress proliferation of peripheral blood mononuclear cells, by activation of Mac-1, known as a suppressive factor for lymphocyte proliferation, co-localization of cathepsin X and LFA-1 enhances lymphocyte proliferation, overview
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additional information
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cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
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additional information
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cathepsin X acts as a monocarboxypepidase and has a strict positional and narrower substrate specificity relative to the other human cathepsins
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additional information
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cathepsin X is an important regulator of LFA-1 activity, and cathepsin X-upregulated Jurkat T cells exhibit increased homotypic aggregation, cathepsin X induces polarized migration-associated morphology in Jurkat T cells, overview
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additional information
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co-localization of alpha or gamma enolase and cathepsin X. Cathepsin X impairs survival and neuritogenesis of neuronal cells, e.g. it reduces PC12 cell survival and neuritogenesis
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additional information
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CATX is an important player in the spinal mechanisms involved in chronic pain induction and maintenance
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additional information
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CATX is widely expressed in the brain and is implicated in several neurological conditions such as Alzheimer's disease, amyotrophic lateral sclerosis and age-related inflammation
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