3.4.21.20: cathepsin G
This is an abbreviated version!
For detailed information about cathepsin G, go to the full flat file.
Word Map on EC 3.4.21.20
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3.4.21.20
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elastase
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neutrophil
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leukocyte
-
proteinases
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granule
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polymorphonuclear
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myeloperoxidase
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chymase
-
granulocyte
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thrombin
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platelet
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mast
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azurophilic
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serpins
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plasmin
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lactoferrin
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collagenase
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neutrophil-derived
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granzyme
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kallikrein
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1-proteinase
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degranulation
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tryptase
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antineutrophil
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1-antichymotrypsin
-
eglin
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drug development
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nsp4
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antiproteinases
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2-macroglobulin
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fmlp
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hne
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alpha-chymotrypsin
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wegener
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chediak-higashi
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antiprotease
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elastolytic
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chymostatin
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slpi
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elastase-like
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p-anca
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procollagenase
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alpha1-proteinase
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pharmacology
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pmn-derived
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elafin
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1-antitrypsin
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medicine
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granulomatosis
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alpha1-antichymotrypsin
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anti-cathepsin
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neutrophil-mediated
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anca-positive
- 3.4.21.20
- elastase
- neutrophil
- leukocyte
- proteinases
- granule
-
polymorphonuclear
- myeloperoxidase
- chymase
- granulocyte
- thrombin
- platelet
-
mast
-
azurophilic
- serpins
- plasmin
- lactoferrin
- collagenase
-
neutrophil-derived
-
granzyme
- kallikrein
-
1-proteinase
-
degranulation
- tryptase
-
antineutrophil
-
1-antichymotrypsin
- eglin
- drug development
- nsp4
-
antiproteinases
-
2-macroglobulin
- fmlp
- hne
- alpha-chymotrypsin
-
wegener
-
chediak-higashi
-
antiprotease
-
elastolytic
- chymostatin
- slpi
-
elastase-like
-
p-anca
- procollagenase
- alpha1-proteinase
- pharmacology
-
pmn-derived
- elafin
-
1-antitrypsin
- medicine
-
granulomatosis
- alpha1-antichymotrypsin
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anti-cathepsin
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neutrophil-mediated
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anca-positive
Reaction
specificity similar to chymotrypsin C =
Synonyms
alpha-protease, cat G, Cat-G, Cat.G, CatG, Cath G, cathepsin G, chymotrypsin-like proteinase, CTSG, More, neutral proteinase, serine protease cathepsin G, Vimentin-specific protease, VSP
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3.4.21.20 cathepsin GAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.21.20 - cathepsin G
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
factor VIII + H2O
factor VIIIa + peptide
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cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, overview
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?
factor VIIIa + H2O
factor VIII + peptide
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cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, inactivation occurs due to decreased stability by subsequent dissociation of the A2 subunit following proteolytic cleavage by cathepsin G, overview
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-
?
fibronectin + H2O
peptide fragments
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proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
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?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
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i.e. hbrm, nuclear protein in volved in regulation of chromatin conformation
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?
intercellular adhesion molecule-1 + H2O
fragments
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i.e. ICAM-1, the substrate plays an important role in inflammation and immune response, e.g. to sustain neutrophil infiltration and to confer susceptibility to septic shock, all alternate substrate isoforms but the common form, in model mouse mutants, and in cystic fibrosis patients
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?
laminin + H2O
fragments of laminin
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degradation, involved in inflammation process
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ir
RANTES 1-68 + H2O
RANTES 4-68 + peptide
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cell-associated N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
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-
?
thrombospondin + H2O
peptide fragments
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proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
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?
von Willebrand factor + H2O
peptide fragments
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proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
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?
fibronectin + H2O
fragments of fibronectin
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degradation, involved in inflammation process
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ir
myelin basic protein + H2O
myelin basic protein peptide fragments
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the serine protease cathepsin G dominates the proteolytic processing of the multiple sclerosis-associated autoantigen myelin basic protein in lysosomes from primary B cells and dendritic cells, overview
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-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
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when microglia are treated with interferon-gamma to mimic a T helper type 1-biased cytokine milieu in multiple sclerosis, CatG is drastically down-regulated resulting in significantly increased stability of myelin basic protein and a selective lack of CatG-derived proteolytic fragments
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?
additional information
?
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enzyme causes platelet secretion and aggregation mediated by protease-activated receptor-4, i.e. PAR4, triggers calcium mobilization in PAR4-transfected fibroblasts, PAR4-expressing Xenopus oocytes, and washed human platelets, enzyme might mediate platelet-neutrophil interaction at sites of vascular injury or inflammation, regulation of enzyme activity on platelets and protease-activated receptors-1 and -4
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?
additional information
?
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enzyme is involved in pathological processes of inflammation
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?
additional information
?
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the enzyme can directly alter platelet function and/or participate in coagulation cascade reactions on the platelet or neutrophil surface to enhance fibrin formation, coagulation pathway overview
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?
additional information
?
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the enzyme induces cell proliferation, cytokine productionand IFN-gamma production in normal spleen cells and T lymphocytes from mice
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?
additional information
?
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the enzyme induces chemotaxis and production of proinflammatory cytokines by macrophages but not by CD4+ T cells, pretreatment of macrophages, but not CD4+ T cells, increases susceptibility to acute HIV-infection, the enzyme has mutiple activities in HIV-type1 infection of macrophages, long-term exposure to cathepsin G suppresses HIV infection of macrophages, the effect is neutralized by serine protease inhibitors
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?
additional information
?
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the enzyme probably represents an alternative pathway that modulates the expression of intercellular adhesion molecule-1 on the cell surface
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?
additional information
?
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cathepsin G and neutrophil elastase are involved in responses of polymorphonucleocytes to various stimuli. When released at sites of inflammation, they participate in the degradation of numerous proteins involved in the regulation of the immune response. the ability of cathepsin G and neutrophil elastase to modulate levels of membrane and soluble forms of tumor necrosis factor alpha may contribute to the proinflammatory activity of neutrophils
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?
additional information
?
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cathepsin G controls the processing of myelin basic protein in lysosomes from human B lymphocytes
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?
additional information
?
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cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
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?
additional information
?
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hypochlorous acid, a specific product of myeloperoxidase, potently inactivates cathepsin G by a pathway that involves oxidation of a specific methionine residue, which in turn may disrupt the catalytic charge relay system and introduce proteolytic cleavage sites into the enzyme. This finding raises the possibility that myeloperoxidase might restrain the activity of cathepsin G near the surface of neutrophils
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-
?
additional information
?
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in stenotic aortic valves, mast cell-derived cathepsin G may cause adverse valve remodelling and progression of aortic stenosis
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?
additional information
?
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Mycobacterium tuberculosis infection results in a cathepsin switch with down-regulation of cathepsin G rendering Mycobacterium tuberculosis bacilli more viable. Downregulation of cathepsin G in macrophages is advantageous to Mycobacterium tuberculosis bacilli and possibly is an important mechanism by which Mycobacterium tuberculosis is able to evade the host immune defense
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?
additional information
?
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neutrophil elastase and cathepsin G induce the formation of highly aggregated multicellular 3-D spheroids of MCF-7 cells. Neutrophil elastase and cathepsin G might be involved in the dissemination of tumor clumps and formation of emboli in tumor metastasis
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-
?
additional information
?
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release of leukocyte elastase or cathepsin G from neutrophils specifically down-regulates the responsiveness of neutrophils to C5a. Elastase and cathepsin G may therefore play an important role in the down-regulation of acute inflammation
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-
?
additional information
?
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the enzyme is a chemotactic agonist for G protein-coupled formyl peptide receptor
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?
additional information
?
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cathepsin G acts as a monocyte chemoattractant in rheumatoid arthritis inducing monocyte migration, overview
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-
?
additional information
?
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the enzyme is one of the major components of the neutrophil primary granules that participate in the non-oxidative pathway of intracellular pathogen destruction, it helps kill bacterial cells and is involved in the degradation of extracellular matrix components during acute and chronic inflammation, the enzyme is important in regulation of immune response, control of cellular signaling through the procession of cytokines and modulation of the cytokine network, biological functions and roles in diseases of cathepsin G, overview
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-
?
additional information
?
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the enzyme is one of the major components of the neutrophil primary granules that participate in the non-oxidative pathway of intracellular pathogen destruction, it helps kill bacterial cells and is involved in the degradation of extracellular matrix components during acute and chronic inflammation, the enzyme is important in regulation of immune response, control of cellular signaling through the procession of cytokines and modulation of the cytokine network, biological functions and roles in diseases of cathepsin G, overview
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-
?
additional information
?
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cathepsin G shows a concentration-dependent induction of monocyte chemotaxis. At the highest concentrations, it induced chemotaxis similar to MCP-1, a known monocyte chemoattractant
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?
additional information
?
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the enzyme does not hydrolyze high-density lipoprotein
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?
additional information
?
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the enzyme does not hydrolyze high-density lipoprotein
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-
?
additional information
?
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The enzyme has a dual specificity consisting of chymase and tryptase-type activities. Phe, Tyr, Trp and Leu are preferred in the P1 position. The enzyme has a preference for negatively charged amino acids in the P2A position of substrates and a preference for aliphatic amino acids both upstream and downstream of the cleavage site
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-
?
additional information
?
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the extended cleavage sites for the enzyme contain about 8 amino acids, and cleavage normally occurs after an aromatic amino acid (phenylalanine, tyrosine and tryptophan or leucine) in the P1 substrate position
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?
additional information
?
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cathepsin G as a critical component sustaining neutrophil-mediated acute tissue pathology and subsequent fibrosis after renal ischemia/reperfusion injury, cathepsin G is required for sustained inflammation and tissue injury after reperfusion of ischemic kidneys, overview
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-
?
additional information
?
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the neutrophil-derived serine protease cathepsin G inhibits the murine hosts ability to clear Pseudomonas aeruginosa, an infection in cystic fibrosis airways causing intense inflammation, from the lung, murine model of endobronchial inflammation, overview
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-
?
additional information
?
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cathepsin G shows a concentration-dependent induction of monocyte chemotaxis. At the highest concentrations, it induced chemotaxis similar to MCP-1, a known monocyte chemoattractant
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?
additional information
?
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enzyme enhances mammary tumor-induced osteolysis by generating soluble receptor activator of nuclear factor-KB ligand. It is significantly up-regulated at the tumor-bone interface and is capable of generating sRANKL, which potentially enhances osteoclast activation and osteolysis
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?
additional information
?
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the enzyme does not hydrolyze high-density lipoprotein
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-
?
additional information
?
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enzyme enhances mammary tumor-induced osteolysis by generating soluble receptor activator of nuclear factor-KB ligand. It is significantly up-regulated at the tumor-bone interface and is capable of generating sRANKL, which potentially enhances osteoclast activation and osteolysis
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?
additional information
?
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the neutrophil-derived serine protease cathepsin G induces neonatal cardiomyocyte detachment and apoptosis by anoikis, which requires matrix metalloproteinase-dependent membrane shredding of epidermal growth factor, signaling induction by the enzyme via epidermal growth factor receptor induction and transactivation, mechanism, overview
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-
?
