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
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proteinases
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granule
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polymorphonuclear
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myeloperoxidase
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chymase
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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
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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
-
anti-cathepsin
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neutrophil-mediated
-
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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General Information
General Information on EC 3.4.21.20 - cathepsin G
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malfunction
physiological function
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inhibition of CatG reduces the presentation of antigens to CD4+ T cells
malfunction
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inhibition of cathepsin G reduces active TGF-beta at the tumor-bone interface
malfunction
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abrogation of CatG activity results in functional inhibition of proinsulin-reactive T cells
malfunction
both pharmacologic inhibition of cathepsin G and its congenital absence prolonge the time for platelet thrombus to form in ferric chloride-injured mouse mesenteric arterioles. In a vaso-occlusive model of ischemic stroke, inhibition of cathepsin G and its congenital absence improves cerebral blood flow, reduces histologic brain injury, and improves neurobehavioral outcome
malfunction
the absence of cathepsin G reduces arterial wall elastin degradation and attenuates early atherosclerosis when mice consume a Western diet for 3 months
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acts as a major histocompatibility complex calls II-degrading protease, involved in major histocompatibility complex class II turnover
physiological function
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cathepsin G is activating pro-MMP9, involved in enhanced TGF-betra signaling
physiological function
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clearance of internalized pathogens, proteolytic modification of chemokines and cytokines, activation and shedding of cell surface receptors, apoptosis, CatG at the surface of mononuclear cells digest cell surface proteins
physiological function
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clearance of internalized pathogens, proteolytic modification of chemokines and cytokines, activation and shedding of cell surface receptors, apoptosis, CatG at the surface of mononuclear cells digest cell surface proteins
physiological function
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induces contact inhibition of cell movement and cell condensation in MCF-7 cells, prmotes E-cadherin/catenin complex foramtion in MCF-7 cells, increases PKD1/E-cadherin complexes in MCF-7 cells
physiological function
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at a concentration of 60 nM, cathepsin G induces a statistically significant acceleration of thrombin generation in blood plasma. With increasing concentrations of cathepsin G, endogenous thrombin potential and thrombin peak decrease also. A statistically significant decrease in all three thrombogram parameters is found at 240 nM. Cathepsin G is not able to induce thrombin generation in factor V- or factor X-depleted plasma
physiological function
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CatG plays a critical role in proinsulin processing and is important in the activation process of diabetogenic T cells
physiological function
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Tamm-Horsfall glycoprotein adheres to surface-expressed lactoferrin and cathepsin G on polymorphonuclear neutrophils and transduces signaling via the MAP kinase pathway to enhance polymorphonuclear neutrophil phagocytosis
physiological function
cathepsin G activity lowers plasma low-density lipoprotein and reduces atherosclerosis. The enzyme promotes early atherogenesis through its elastinolytic activity, but suppresses late progression of atherosclerosis by degrading low-density lipoprotein without affecting high-density lipoprotein or triglycerides
physiological function
cathepsin G activity lowers plasma low-density lipoprotein and reduces atherosclerosis. The enzyme promotes early atherogenesis through its elastinolytic activity, but suppresses late progression of atherosclerosis by degrading low-density lipoprotein without affecting high-density lipoprotein or triglycerides
physiological function
cathepsin G originating from primed peripheral polymorphonuclear leukocytes of hemodialysis patients can initiate endothelial dysfunction
physiological function
cathepsin G regulates the release and proteolysis of annexin A1 and cathelin-related antimicrobial peptide, which act on neutrophil cell surface receptors to modulate the level of cellular activation. Cathepsin G is required for the release of neutrophil-derived inflammatory mediators
physiological function
neutrophil cathepsin G is a physiologic modulator of platelet thrombus formation in vivo
physiological function
neutrophil cathepsin G is a physiologic modulator of platelet thrombus formation in vivo
physiological function
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the enzyme can increase the permeability of vascular endothelial cells and the chemotaxis of inflammatory cells. The enzyme plays an important role in muscle inflammatory cells infiltration by increasing the permeability of vascular endothelial cells. Serum enzyme induces the expression of protease activated receptor 2, interleukin-6, and interleukin-8 in human dermal microvascular endothelial cells
physiological function
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the enzyme cleaves and activates recombinant human full length interleukin-36gamma to promote CXCL-1 and CXCL-8 expression by human keratinocytes
physiological function
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the enzyme functions in regulating excessive inflammation