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
-
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
-
neutrophil-mediated
-
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
-
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
ECTree
3.4.21.20 cathepsin GAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.20 - cathepsin G
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SUBSTRATE 
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
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe + norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-Ser-Asp-Lys(Tfa)-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe + Ser-Asp-Lys(Tfa)-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-Ser-Asp-Met(O)-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe + Ser-Asp-Met(O)-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe-norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe + norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe-norvaline-Asp-Met(O)2-Gly-Lys(DNP)-Gly-NH2 + H2O
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe + norvaline-Asp-Met(O)2-Gly-Lys(DNP)-Gly-NH2
-
-
-
-
?
4-(((S)-3-methyl-1-((S)-2-(((S)-1-((4-nitrophenyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamoyl)pyrrolidin-1-yl)-1-oxobutan-2-yl)amino)-4-oxobutanoic acid + H2O
?
-
-
-
-
?
4-carboxybutyryl-Phe-2-naphthyl ester + H2O
4-carboxybutyryrl-Phe + 2-naphthol
-
-
-
ir
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Phe-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2 + H2O
?
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-amino-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-amino-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-carboxy-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-carboxy-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-COOCH3-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-COOCH3-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-cyano-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-cyano-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-guanidyl-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-guanidyl-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-(4-nitro-L-phenylalanyl)-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-4-nitro-L-phenylalanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Arg-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Arg + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Lys-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Lys + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Phe-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Phe + 5-amino-2-nitrobenzamide
-
-
-
-
?
Ac-L-Phe-L-Val-L-Thr-L-Tyr-NH-(3-carbamoyl-4-nitrophenol) + H2O
Ac-L-Phe-L-Val-L-Thr-L-Tyr + 5-amino-2-nitrobenzamide
-
-
-
-
?
acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2 + H2O
?
-
chromogenic cathepsin G substrate
-
-
?
complement component C3 + H2O
complement component C3a + complement component C3b
-
-
-
?
Fibronectin + H2O
?
-
hydrolysis after methionine, leucine, phenylalanine, lysine, or arginine residues
-
?
glycoprotein Ibalpha subunit + H2O
?
-
from the glycoprotein Ib-IX receptor of human platelets
-
-
?
high molecular mass kininogen + H2O
peptide fragments
-
human, 120 kDa
after 1 min reaction: 110, 100, and 75 kDa fragments, after 5 min reaction: 10 to 70 kDa fragments, after 60 min: less than 20 kDa fragments
?
Laminin + H2O
?
-
hydrolysis after methionine, leucine, phenylalanine, lysine, or arginine residues
-
?
MARS123 + H2O
?
-
i.e. bis(4-methoxyphenyl) (1-((S)-1-((5-((3aS,4S,6aR)-3a,6a-dimethyl-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoyl)-L-valyl)pyrrolidine-2-carboxamido)-3-methylbutyl)phosphonate. The reaction occurs in the presence of lactoferrin only
-
-
?
MARS125 + H2O
?
-
i.e. diphenyl(1-((S)-1-((5-((3aS,4S,6aR)-3a,6adimethyl-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoyl)-L-valyl)pyrrolidine-2-carboxamido)-2-methylpropyl)phosphonate. The reaction occurs in the presence of lactoferrin only
-
-
?
N-acetyl-L-phenylalanyl-L-valyl-L-threonyl-N-(5-amino-2-nitrobenzoyl)-3-pyridin-4-yl-L-alaninamide) + H2O
N-acetyl-L-phenylalanyl-L-valyl-L-threonyl-3-pyridin-4-yl-L-alanine + 5-amino-2-nitrobenzamide
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
N-succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
?
-
chromogenic substrate
-
?
N-succinyl-L-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe-L-Pro-L-Phe + 4-nitroaniline
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
N-succinyl-Phe-Leu-Phe-thiobenzyl ester + H2O
?
-
chromogenic substrate
-
?
protease-activated receptor-1 + H2O
?
-
i.e. PAR1, activation of platelets by hydrolysis of the receptor protein
-
?
protease-activated receptor-4 + H2O
?
-
i.e. PAR4, activation of platelets by hydrolysis of the receptor protein
-
?
succinyl-alanyl-alanyl-prolyl-phenylalanyl-aminomethyl-coumarin + H2O
?
-
a fluorogenic substrate
-
-
?
factor VIII + H2O
factor VIIIa + peptide
-
cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, overview
-
-
?
factor VIII + H2O
factor VIIIa + peptide
-
cleavage releases the bound von-Willebrand factor and the corresponding peptide sequence, determination of cleavage sites, overview
-
-
?
factor VIIIa + H2O
factor VIII + peptide
-
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
-
-
?
fibronectin + H2O
fragments of fibronectin
-
degradation, involved in inflammation process
-
ir
fibronectin + H2O
peptide fragments
-
220 kDa substrate in extracellular matrix of human umbilical vein endothelial cells and platelets
162 kDa, 122 kDa, and 92 kDa
?
fibronectin + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
-
i.e. hbrm, cleavage in vitro after induction of apoptosis, cleavage pattern
the 20 kDa fragment contains a bromodomain from the C-terminus of hbrm, the 160 kDa binds less tightly to he nuclear matrix than the full length protein
?
human brm protein + H2O
160 kDa fragment of brm protein + 20 kDa fragment of brm protein
-
i.e. hbrm, nuclear protein in volved in regulation of chromatin conformation
-
?
intercellular adhesion molecule-1 + H2O
fragments
-
i.e. ICAM-1, a membrane glycoprotein consisting of five extracellular Ig-like domains, a transmembrane domain, and a short cytoplasmic tail, all alternate substrate isoforms or mutant substrate forms but the common form, from mouse and human, substrate specificity is influenced by the ability of the ICAM-1 isoforms to form dimers and larger multimeric complexes
-
?
intercellular adhesion molecule-1 + H2O
fragments
-
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
-
?
laminin + H2O
fragments of laminin
-
degradation, involved in inflammation process
-
ir
MARS116 + H2O
?
-
i.e. diphenyl(1-((S)-1-((4-oxo-4-((5-(5-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanamido)pentyl)amino)butanoyl)-L-valyl)pyrrolidine-2-carboxamido)-2-phenylethyl)phosphonate. The reaction occurs in the presence of lactoferrin only
-
-
?
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
-
-
-
-
?
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
-
-
-
-
?
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
-
-
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
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
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
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
-
-
?
myelin basic protein + H2O
myelin basic protein peptide fragments
-
substrate is recombinant purified human myelin basic protein, differential processing patterns, overview
determination of proteolysis products
-
?
N-benzoyl-L-tyrosine ethyl ester + H2O
N-benzoyl-L-tyrosine + ethanol
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
chromogenic substrate
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
assay at pH 7.5, 37°C
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
-
assay at 37°C
-
-
?
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
assay at pH 7.4, 25°C
-
-
?
N-succinyl-L-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Phe-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Phe-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide + H2O
N-succinyl-L-Val-L-Pro-L-Phe + 4-nitroaniline
-
-
-
-
?
RANTES 1-68 + H2O
RANTES 4-68 + peptide
-
cell-associated N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
-
-
?
RANTES 1-68 + H2O
RANTES 4-68 + peptide
-
N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
-
-
?
thrombospondin + H2O
peptide fragments
-
preferred substrate, 180 kDa substrate in extracellular matrix of human umbilical vein endothelial cells and platelets
155 kDa and 25 kDa
?
thrombospondin + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
von Willebrand factor + H2O
peptide fragments
-
280 kDa substrate in extracellular matrix of human umbilical vein endothelial cells and platelets
260-177 kDa and 177-136 kDa
?
von Willebrand factor + H2O
peptide fragments
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
additional information
?
-
-
no activity with PAR1-mutant A2F and PAR4 mutant G1P
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
enzyme is involved in pathological processes of inflammation
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme induces cell proliferation, cytokine productionand IFN-gamma production in normal spleen cells and T lymphocytes from mice
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme probably represents an alternative pathway that modulates the expression of intercellular adhesion molecule-1 on the cell surface
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
cathepsin G controls the processing of myelin basic protein in lysosomes from human B lymphocytes
-
-
?
additional information
?
-
-
cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
in stenotic aortic valves, mast cell-derived cathepsin G may cause adverse valve remodelling and progression of aortic stenosis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme is a chemotactic agonist for G protein-coupled formyl peptide receptor
-
-
?
additional information
?
-
-
cathepsin G acts as a monocyte chemoattractant in rheumatoid arthritis inducing monocyte migration, overview
-
-
?
additional information
?
-
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
-
-
?
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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cathepsin G prefers aromatic or positively charged residues at P1 position, e.g. Phe, Tyr, Lys, or Arg, substrate specificity and active site structure analysis, overview
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cathepsin G prefers aromatic or positively charged residues at P1 position, e.g. Phe, Tyr, Lys, or Arg, substrate specificity and active site structure analysis, overview
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specificity with synthetic fluorogenic/chromogenic substrates, preference for aromatic residues at P1 position, specificity at other positions, overview
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specificity with synthetic fluorogenic/chromogenic substrates, the enzyme prefers Ser at P1' position and Trp at the P2' position, overview
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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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human cathepsin G has broad chymotryptic activity, cleaving after Trp, Phe, and Tyr, with little preference for Tyr versus Phe. It also has substantial Leu-ase and Met-ase activity, with little or no ability to cleave after P1 acidic residues (granzyme B-like Asp-ase activity) and small aliphatic residues (neutrophil elastase-like activity). Its most unique feature, however, is tryptic activity, which is as strong as its Tyr-cleaving chymotryptic activity and is largely Lys-specific
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the enzyme does not hydrolyze high-density lipoprotein
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the enzyme does not hydrolyze high-density lipoprotein
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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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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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lactoferrin is not proteolytically degraded by the enzyme
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no activity with interleukin-4, interleukin-5, or interleukin-10
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no activity with succinyl-AAPI-4-nitroanilide, succinyl-AAPA-4-nitroanilide, succinyl-AAPV-4-nitroanilide, succinyl-VLGR-4-nitroanilide, Z-GPR-4-nitroanilide, acetyl-YVAD-4-nitroanilide, acetyl-VEID-4-nitroanilide, and acetyl-IEPD-4-nitroanilide
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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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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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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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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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the mouse enzyme lacks the tryptic, Leu-ase and Met-ase activity of the human enzyme, and even its chymotryptic profile is narrower, showing preference for Tyr over Phe and little inclination to cleave after Trp
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the enzyme does not hydrolyze high-density lipoprotein
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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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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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