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Information on EC 3.4.21.20 - cathepsin G and Organism(s) Homo sapiens and UniProt Accession P08311
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3.4.21.20 cathepsin GSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cathepsin g, neutral proteinase, cat g, chymotrypsin-like proteinase, cat.g, cat-g, serine protease cathepsin g, alpha-protease, cath g, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CatG
-
-
cathepsin G
chymotrypsin-like proteinase
-
-
-
-
neutral proteinase
-
-
-
-
Vimentin-specific protease
-
-
-
-
VSP
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
56645-49-9
-
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
N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide + H2O
N-succinyl-Ala-Ala-Pro-Phe + p-nitroaniline
assay at pH 7.4, 25°C
-
-
?
(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
-
-
?
methoxy succinyl-L-alanine-L-alanine-L-proline-L-valine-p-nitroanilide + H2O
?
-
-
-
-
?
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
-
?
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
-
-
?
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
-
-
?
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-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
-
-
?
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
?
-
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
?
-
-
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
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
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
?
-
-
specificity with synthetic fluorogenic/chromogenic substrates, preference for aromatic residues at P1 position, specificity at other positions, overview
-
-
?
additional information
?
-
-
specificity with synthetic fluorogenic/chromogenic substrates, the enzyme prefers Ser at P1' position and Trp at the P2' position, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
lactoferrin is not proteolytically degraded by the enzyme
-
-
?
additional information
?
-
-
no activity with interleukin-4, interleukin-5, or interleukin-10
-
-
?
additional information
?
-
-
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
-
-
?
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
-
cathepsin G activates coagulation factor VIII to apartially active form, while having only a minor inactivating effect on thrombin-activated factor VIIIa, 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
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, nuclear protein in volved in regulation of chromatin conformation
-
?
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
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
-
-
?
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
-
-
?
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
-
proteolysis causes no change in endothelial cell morphology, involved in release of extracellular matrix components during inflammation
-
?
fibronectin + H2O
fragments of fibronectin
-
degradation, involved in inflammation process
-
ir
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
?
-
-
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
?
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
additional information
?
-
-
the enzyme does not hydrolyze high-density lipoprotein
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Na+
-
enhances the ionic interaction and binding affinity and thereby increases the inhibitory effect of glycosaminiglycans and heparin-like dextran derivatives depending on the nature of chemical groups substituted to the dextran
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11-oxo-beta-boswellic acid
0.01 mM, 30% cathepsin G activity compared to control
3-O-acetyl-11-oxo-beta-boswellic acid
0.01 mM, 15% cathepsin G activity compared to control
3-O-acetyl-beta-boswellic acid
0.01 mM, 5% cathepsin G activity compared to control
beta-boswellic acid
0.01 mM, 30% cathepsin G activity compared to control
glut-11-oxo-beta-boswellic acid
0.01 mM 20% cathepsin G activity compared to control
JNJ-10311795
inhibitor of cathepsin G and chymase. The possibility to inhibit both cathepsin G and chymase with a single molecule suggests an opportunity in the treatment of asthma and chronic obstructive pulmonary disease
N-succinyl-L-Ala-L-Ala-L-Pro-L-Phe-chloromethylketone
irreversible inhibitor
[2-(3-[methyl[1-(2-naphthoyl)piperidin-4-yl]amino]carbonyl]-2-naphthyl)-1-(1-naphthyl)-2-oxoethyl]phosphonic acid
0.0005 mM, 10% cathepsin G activity compared to control
2-amino-3,1-benzoxazin-4-ones
-
non-covalent complex formation, hydrophobic and basic residues at position 2, kinetics of acylation and desacylation, binding at the enzyme's active site
6-((1'R,2'S,5'R)-menthyloxycarbonyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-((1'S)-camphanyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
selective inhibition
6-((1'S,2'R,5'S)-menthyloxycarbonyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
6-(benzoyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
selective inhibition
6-(N-tosyl-L-phenylalanyl)amino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-dione
-
-
bis(4-ethylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis(4-methoxyphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
bis(4-methylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis(4-tert-butylphenyl) [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis-naphthyl beta-ketophosphoric acid
-
moderately potent, competitive, reversible, the R-isomer occupies the active site of the enzyme
bis[4-(1,1,3,3-tetramethylbutyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
3% inhibition, 115 microM
bis[4-(1-methylethyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] ([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][(O-tert-butyl-L-threonyl)amino]methyl)phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] [[4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl]([O-tert-butyl-N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-threonyl]amino)methyl]phosphonate
-
-
bis[4-(methylsulfanyl)phenyl] [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
dermatan sulfate
-
25 kDa, protection of laminin and fibronectin against degradation by cathepsin G
dinaphthalen-2-yl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
-
diphenyl (1-[[(benzyloxy)carbonyl]amino]-3-carbamimidamidopropyl)phosphonate
-
-
diphenyl (4-amino-1-[[(benzyloxy)carbonyl]amino]butyl)phosphonate
-
5% inhibition, 221 microM
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidamidophenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
diphenyl [[[(benzyloxy)carbonyl]amino](4-carbamimidoylphenyl)methyl]phosphonate
-
30% inhibition, 112 microM
diphenyl [[[(benzyloxy)carbonyl]amino](6-carbamimidoylnaphthalen-2-yl)methyl]phosphonate
-
5% inhibition, 112 microM
diphenyl [[[(benzyloxy)carbonyl]amino](phenyl)methyl]phosphonate
-
more potent inhibitor for related proteases than cathepsin G
heparan sulfate
-
60 kDa, protection of laminin and fibronectin against degradation by cathepsin G
heparin
-
12 kDa, 1:1 binding stoichiometry with cathepsin G, protection of laminin and fibronectin against degradation by cathepsin G
high molecular mass kininogen
-
i.e. HK, human, competitive, inhibits platelet activation by the enzyme completely by complex formation with the enzyme
-
L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
L-valyl-N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
-
N-acetyl-L-phenylalanyl-L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
N-acetyl-L-phenylalanyl-L-valyl-N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
-
N-tosyl-L-phenylalanine chloromethyl ketone
-
TPCK, inhibitor of the proteolytic activity of cathepsin G, effectively eliminated cathepsin G-induced chemotaxis of monocytes
N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-valyl-N-([4-[bis(tert-butoxycarbonyl)carbamimidamido]phenyl][bis[4-(methylsulfanyl)phenoxy]phosphoryl]methyl)-O-tert-butyl-L-threoninamide
-
-
N-[[bis[4-(methylsulfanyl)phenoxy]phosphoryl](4-carbamimidamidophenyl)methyl]-L-threoninamide
-
two times more active against cathepsin G than against trypsin
RG1150
-
i.e. carboxymethyl-benzylamide-dextran derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
RG1192
-
i.e. carboxymethyl-benzylamide-dextran sulfate derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
RG1503
-
i.e. carboxymethyl-dextran sulfate derivative, protection of laminin and fibronectin against degradation by cathepsin G
-
[2-(3-methylcarbamoyl-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
[2-(3-[(3-benzoylamino-propyl)-methyl-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
[2-(3-[(piperidin-4-yl)-methyl-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
reversible, selective, competitive inhibition
[2-(3-[methyl-(diphenyl-ethylcarbamoyl-methyl)-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
strong inhibition
[2-(3-[methyl-(phenethylcarbamoyl-methyl)-carbamoyl]-naphthalen-2-yl)-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
[2-[3-(benzyl-methyl-carbamoyl)-naphthalen-2-yl]-1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
alpha1-Aantichymotrypsin
-
acute phase reactant which is up-regulated during inflammation episodes to compensate for the excess of enzymes released from the actvated neutrophils
-
benzyloxycarbonyl-Gly-Leu-Phe-chloromethyl ketone
-
i.e. CK-08, specific for cathepsin G
additional information
-
5kD heparin fragment protects against inhibition by alpha1-antichymotrypsin inhibitor, eglin c and alpha1-proteinase inhibitor
-
additional information
-
inhibition mechanism and kinetics, effect of ionic strength
-
additional information
-
structural features of inhibition, high-throughput screening of a diverse chemical library, lead structure is bis-naphthyl beta-ketophosphoric acid
-
additional information
-
no inhibitory effect: diphenyl (1-[[(benzyloxy)carbonyl]amino]-4-carbamimidamidobutyl)phosphonate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lactoferrin
-
allosteric enhancer of the proteolytic activity of the enzyme with highest enhancing capacity under acidic (pH 5.0) conditions at 0.0025-0.25 mg/ml
-
N-formylmethionyl-leucyl-phenylalanine
-
induces release of enzyme from neutrophils
phosphocholine
-
phospholipid vesicles containing phosphatidyl-L-serine and phosphocholine are required for enzyme-mediated thrombin production in platelet-free plasma, potentially due to protection of lipid bound enzyme from inhibition
additional information
-
cathepsin G activity in samples from activated lymphocytes increases slowly with age of patients, both in intra- and extracellular compartments
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0097
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2
-
pH 7.5, 25°C
0.0099
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-amino benzoyl-NH2
-
pH 7.5, 25°C
0.0035
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2
-
pH 7.5, 25°C
0.0032
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Phe-amino benzoyl-NH2
-
pH 7.5, 25°C
0.0021
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2
-
pH 7.5, 25°C
0.203
acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2
-
pH 7.5, 25°C
0.69
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
-
wild type enzyme, in PBS buffer, pH 8.0, 37°C
1.73
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
-
wild type enzyme, in 1.8 M NaCl, pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2
-
pH 7.5, 25°C
0.421
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-amino benzoyl-NH2
-
pH 7.5, 25°C
0.604 - 6.08
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2
0.512
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Phe-amino benzoyl-NH2
-
pH 7.5, 25°C
0.524 - 6.08
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2
19
acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-amino benzoyl-NH2
-
pH 7.5, 25°C
0.604
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2
-
pH 7.5, 25°C
6.08
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Asp-amino benzoyl-NH2
-
pH 7.5, 25°C
0.524
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2
-
pH 7.5, 25°C
6.08
7-methoxycoumarin-4-yl-acetyl-Phe-Val-Thr-(4-guanidine-L-phenylalanyl)-Ser-Trp-amino benzoyl-NH2
-
pH 7.5, 25°C
14
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
-
wild type enzyme, in PBS buffer, pH 8.0, 37°C
100
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
-
wild type enzyme, in 1.8 M NaCl, pH 8.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2054
Abz-GIAPFCDLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
817
Abz-GIATFCDLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
263
Abz-GIATFCMLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
560
Abz-GIATFCPLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
68
Abz-GIATFCRLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
175
Abz-GIATFDMLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
162
Abz-GIATFRMLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
217
Abz-GIATFSMLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
69
Abz-GIATFWMLMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
1700
Abz-GIEPFSDPMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
190
Abz-GIEPKSDPMPEQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
153.8
Abz-TPFSALQ-EDDnp
at 37°C in 50mM HEPES buffer (pH 7.4), 100 mM NaCl
0.191
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2
-
at pH 7.4 and 37°C
0.179
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-Ser-Asp-Lys(Tfa)-Gly-Lys(DNP)-Gly-NH2
-
at pH 7.4 and 37°C
0.207
(7-aminocoumarin-4-yl)acetyl-Gly-His(Bzl)-Tle-Pro-Phe-Ser-Asp-Met(O)-Gly-Lys(DNP)-Gly-NH2
-
at pH 7.4 and 37°C
0.154
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe-norvaline-Asp-3-Pal-Gly-Lys(DNP)-Gly-NH2
-
at pH 7.4 and 37°C
0.17
(7-aminocoumarin-4-yl)acetyl-Gly-Phe(F)5-Tle-Pro-Phe-norvaline-Asp-Met(O)2-Gly-Lys(DNP)-Gly-NH2
-
at pH 7.4 and 37°C
20
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
-
wild type enzyme, in PBS buffer, pH 8.0, 37°C
58
N-succinyl-L-Val-L-Pro-L-Phe-4-nitroanilide
-
wild type enzyme, in 1.8 M NaCl, pH 8.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000008
dermatan sulfate
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.000003
heparan sulfate
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.0000008
heparin
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
0.00000011
RG1150
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester
-
0.0000012
RG1503
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-4-nitroanilide, in presence of 0.1 Na+
-
0.00005 - 0.00006
[2-(3-[(piperidin-4-yl)-methyl-carbamoyl]-naphthalen-2-yl)1-naphthalen-1-yl-2-oxo-ethyl]-phosphonic acid
-
-
0.00000017
RG1192
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester
-
0.00000017
RG1192
-
pH 7.4, 25°C, with substrate succinyl-Ala-Ala-Pro-Phe-thiobenzyl ester, at physiologic ionic strength
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
development of sensitive cathepsin G fluorogenic substrate using combinatorial chemistry methods, overview
additional information
-
15% cathepsin G acitivity among total proteolytic activity of fecal supernatants, in patients with ulcerative colitits
additional information
-
7% cathepsin G acitivity among total proteolytic activity of fecal supernatants, in healthy patients
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is expressed in intimal and medial cells, particularly abundant in atheroma plaque
-
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
-
-
651320, 652509, 653667, 664269, 664857, 665537, 665913, 683071, 683748, 683876, 684056, 684082, 691240, 694320, 708698, 709814, 709987, 718414, 754328, 755116, 755171
-
expression at high levels on the surface of activated human neutrophils in catalytically active but inhibitor-resistant form
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mechanism by which the enzyme binds to activated human neutrophil plasma membranes, a functional active site is not required for binding, overview, inhibition of binding by 1. trypsin, chondroitinase ABC, and heparitinases, but not other glycanases, and by 2. purified chondroitin sulfates, heparan sulfate, and other sulfated molecules, but not by non-sulfated glycans, binding kinetics, overview
-
expression at high levels on the surface of activated human neutrophils in catalytically active but inhibitor-resistant form
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
physiological function
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
malfunction
-
inhibition of CatG reduces the presentation of antigens to CD4+ T cells
malfunction
-
abrogation of CatG activity results in functional inhibition of proinsulin-reactive T cells
physiological function
-
acts as a major histocompatibility complex calls II-degrading protease, involved in major histocompatibility complex class II turnover
physiological function
-
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
-
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
-
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
-
CatG plays a critical role in proinsulin processing and is important in the activation process of diabetogenic T cells
physiological function
-
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
-
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
-
the enzyme cleaves and activates recombinant human full length interleukin-36gamma to promote CXCL-1 and CXCL-8 expression by human keratinocytes
physiological function
-
the enzyme functions in regulating excessive inflammation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CATG_HUMAN
255
0
28837
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A226E
the substitution at the bottom of the cathepsin G S1 pocket allows cathepsin G to accommodate a Lys residue at P1
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, elastin-Sepharose affinity chromatography, ion-exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
level of cathepsin G is reduced in peripheral polymorphonuclear leukocytes of hemodialysis patients, while the mRNA enzyme level is not different
patients with atherosclerosis have significantly reduced plasma enzyme levels
both CatG activity and transcript level are elevated in peripheral blood mononuclear cells from type 1 diabetes mellitus patients. Vitamin D reduces CatG activity only in myeloid dendritic cells from healthy donors
-
the enzyme expression and activity is increased in peripheral blood mononuclear cells and muscle tissues of dermatomyositis patients
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
JNJ-10311795 is an inhibitor of cathepsin G and chymase. The possibility to inhibit both cathepsin G and chymase with a single molecule suggests an exciting opportunity in the treatment of asthma and chronic obstructive pulmonary disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tschesche, H.; Wenzel, H.R.; Engelbrecht, S.; Schnabel, E.
Cathepsin G
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
164-170
1984
Homo sapiens
-
Heck, L.W.; Rostand, K.S.; Hunter, F.A.; Bhown, A.
Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors
Anal. Biochem.
158
217-227
1986
Homo sapiens
Virca, G.D.; Metz, G.; Schnebli, H.P.
Similarities between human and rat leukocyte elastase and cathepsin G
Eur. J. Biochem.
144
1-9
1984
Homo sapiens, Rattus norvegicus
Starkey, P.M.; Barret, A.J.
Neutral proteinases of human spleen. Purification and criteria for homogeneity of elastase and cathepsin G
Biochem. J.
155
255-263
1976
Homo sapiens
Braun, N.J.; Bodmer, J.L.; Virca, G.D.; Metz-Virca, G.; Maschler, R.; Bieth, J.G.; Schnebli, H.P.
Kinetic studies on the interaction of eglin c with human leukocyte elastase and cathepsin G
Biol. Chem. Hoppe-Seyler
368
299-308
1987
Homo sapiens
Stein, R.L.; Strimpler, A.M.
Slow-binding inhibition of chymotrypsin and cathepsin G by the peptide aldehyde chymostatin
Biochemistry
26
2611-2615
1987
Homo sapiens
Saklatvala, J.; Barrett, A.J.
Identification of proteinases in rheumatoid synovium. Detection of leukocyte elastase cathepsin G and another serine proteinase
Biochim. Biophys. Acta
615
167-177
1980
Homo sapiens
Lively, M.O.; Powers, J.C.
Specificity and reactivity of human granulocyte elastase and cathepsin G, porcine pancreatic elastase, bovine chymotrypsin and trypsin toward inhibition with sulfonyl fluorides
Biochim. Biophys. Acta
525
171-179
1978
Homo sapiens
Powers, J.C.; Gupton, B.F.; Harley, A.D.; Nishino, N.; Whitley, R.J.
Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G. Inhibition with peptide chloromethyl ketones
Biochim. Biophys. Acta
485
156-166
1977
Homo sapiens
Duranton, J.; Adam, C.; Bieth, J.G.
Kinetic mechanism of the inhibition of cathepsin G by alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor
Biochemistry
37
11239-11245
1998
Homo sapiens
Bania, J.; Stachowiak, D.; Polanowski, A.
Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera
Eur. J. Biochem.
262
680-687
1999
Homo sapiens
Ermolieff, J.; Boudier, C.; Laine, A.; Meyer, B.; Bieth, J.G.
Heparin protects cathepsin G against inhibition by protein proteinase inhibitor
J. Biol. Chem.
269
29502-29508
1994
Homo sapiens
Pidard, D.; Renesto, P.; Berndt, M.C.; Rabhi, S.; Clemetsons, K.J.; Chignard, M.
Neutrophil proteinase cathepsin G is proteolytically active on the human platelet glycoprotein Ib-IX receptor: characterization of the cleavage sites within the glycoprotein Ib alpha subunit
Biochem. J.
303
489-498
1994
Homo sapiens
Hogg, P.J.; Owensby, D.A.; Chesterman, C.N.
Thrombospondin 1 is a tight-binding competitive inhibitor of neutrophil cathepsin G. Determination of the kinetic mechanism of inhibition and localization of cathepsin G binding to the thrombospondin 1 type 3 repeats
J. Biol. Chem.
268
21811-21818
1993
Homo sapiens
Groutas, W.C.; Brubaker, M.J.; Verkataraman, R.; Epp, J.B.; Stang, M.A.; McClenahan, J.J.
Inhibitors of human neutrophil cathepsin G: structural and biochemical studies
Arch. Biochem. Biophys.
294
114-146
1992
Homo sapiens
-
Turkington, P.T.
Cathepsin G, a regulator of human vitamin K, dependent clotting factors and inhibitors
Thromb. Res.
67
147-155
1992
Homo sapiens
Hof, P.; Mayr, I.; Huber, R.; Korzus, E.; Potempa, J.; Travis, J.; Powers, J.C.; Bode, W.
The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities
EMBO J.
15
5481-5491
1996
Homo sapiens
Maison, C.M.; Villiers, C.L.; Colomb, M.G.
Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G
J. Immunol.
147
921-926
1991
Homo sapiens
Gutschow, M.; Kuerschner, L.; Pietsch, M.; Ambrozak, A.; Neumann, U.; Gunther, R.; Hofmann, H.J.
Inhibition of cathepsin G by 2-amino-3,1-benzoxazin-4-ones: kinetic investigations and docking studies
Arch. Biochem. Biophys.
402
180-191
2002
Homo sapiens
Tani, K.; Murphy, W.J.; Chertov, O.; Oppenheim, J.J.; Wang, J.M.
The neutrophil granule protein cathepsin G activates murine T lymphocytes and upregulates antigen-specific IG production in mice
Biochem. Biophys. Res. Commun.
282
971-976
2001
Homo sapiens
Vagnoni, L.M.; Gronostaj, M.; Kerrigan, J.E.
6-Acylamino-2-[(ethylsulfonyl)oxy]-1H-isoindole-1,3-diones mechanism-based inhibitors of human leukocyte elastase and cathepsin G: effect of chirality in the 6-acylamino substituent on inhibitory potency and selectivity
Bioorg. Med. Chem.
9
637-645
2001
Homo sapiens
Robledo, O.; Papaioannou, A.; Ochietti, B.; Beauchemin, C.; Legault, D.; Cantin, A.; King, P.D.; Daniel, C.; Alakhov, V.Y.; Potworowski, E.F.; St-Pierre, Y.
ICAM-1 isoforms: specific activity and sensitivity to cleavage by leukocyte elastase and cathepsin G
Eur. J. Immunol.
33
1351-1360
2003
Homo sapiens
Ledoux, D.; Merciris, D.; Barritault, D.; Caruelle, J.P.
Heparin-like dextran derivatives as well as glycosaminoglycans inhibit the enzymatic activity of human cathepsin G
FEBS Lett.
537
23-29
2003
Homo sapiens
Selim, T.E.; Ghoneim, H.R.; Abdel Ghaffar, H.A.; Colman, R.W.; Dela Cadena, R.A.
High molecular mass kininogen inhibits cathepsin G-induced platelet activation by forming a complex with cathepsin G
Hematol. J.
2
371-377
2001
Homo sapiens
Greco, M.N.; Hawkins, M.J.; Powell, E.T.; Almond, H.R., Jr.; Corcoran, T.W.; de Garavilla, L.; Kauffman, J.A.; Recacha, R.; Chattopadhyay, D.; Andrade-Gordon, P.; Maryanoff, B.E.
Nonpeptide inhibitors of cathepsin G: optimization of a novel beta-ketophosphonic acid lead by structure-based drug design
J. Am. Chem. Soc.
124
3810-3811
2002
Homo sapiens
Sambrano, G.R.; Huang, W.; Faruqi, T.; Mahrus, S.; Craik, C.; Coughlin, S.R.
Cathepsin G activates protease-activated receptor-4 in human platelets
J. Biol. Chem.
275
6819-6823
2000
Homo sapiens
Goel, M.S.; Diamond, S.L.
Neutrophil cathepsin G promotes prothrombinase and fibrin formation under flow conditions by activating fibrinogen-adherent platelets
J. Biol. Chem.
278
9458-9463
2003
Homo sapiens
Moriuchi, H.; Moriuchi, M.; Fauci, A.S.
Cathepsin G, a neutrophil-derived serine protease, increases susceptibility of macrophages to acute human immunodeficiency virus type 1 infection
J. Virol.
74
6849-6855
2000
Homo sapiens
Biggs, J.R.; Yang, J.; Gullberg, U.; Muchardt, C.; Yaniv, M.; Kraft, A.S.
The human brm protein is cleaved during apoptosis: the role of cathepsin G
Proc. Natl. Acad. Sci. USA
98
3814-3819
2001
Homo sapiens
Bonnefoy, A.; Legrand, C.
Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase
Thromb. Res.
98
323-332
2000
Homo sapiens
Sissi, C.; Lucatello, L.; Naggi, A.; Torri, G.; Palumbo, M.
Interactions of low-molecular-weight semi-synthetic sulfated heparins with human leukocyte elastase and human Cathepsin G
Biochem. Pharmacol.
71
287-293
2006
Homo sapiens
Mezyk-Kope?, R.; Bzowska, M.; Bzowska, M.; Mickowska, B.; Mak, P.; Potempa, J.; Bereta, J.
Effects of elastase and cathepsin G on the levels of membrane and soluble TNFalpha
Biol. Chem.
386
801-811
2005
Homo sapiens
Yui, S.; Tomita, K.; Kudo, T.; Ando, S.; Yamazaki, M.
Induction of multicellular 3-D spheroids of MCF-7 breast carcinoma cells by neutrophil-derived cathepsin G and elastase
Cancer Sci.
96
560-570
2005
Homo sapiens
Helske, S.; Syvaeranta, S.; Kupari, M.; Lappalainen, J.; Laine, M.; Lommi, J.; Turto, H.; Maeyraenpaeae, M.; Werkkala, K.; Kovanen, P.T.; Lindstedt, K.A.
Possible role for mast cell-derived cathepsin G in the adverse remodelling of stenotic aortic valves
Eur. Heart J.
27
1495-1504
2006
Homo sapiens
Tralau, T.; Meyer-Hoffert, U.; Schroeder, J.M.; Wiedow, O.
Human leukocyte elastase and cathepsin G are specific inhibitors of C5a-dependent neutrophil enzyme release and chemotaxis
Exp. Dermatol.
13
316-325
2004
Homo sapiens
Raptis, S.Z.; Shapiro, S.D.; Simmons, P.M.; Cheng, A.M.; Pham, C.T.
Serine protease cathepsin G regulates adhesion-dependent neutrophil effector functions by modulating integrin clustering
Immunity
22
679-691
2005
Homo sapiens
Rivera-Marrero, C.A.; Stewart, J.; Shafer, W.M.; Roman, J.
The down-regulation of cathepsin G in THP-1 monocytes after infection with Mycobacterium tuberculosis is associated with increased intracellular survival of bacilli
Infect. Immun.
72
5712-5721
2004
Homo sapiens
Stefansson, S.; Yepes, M.; Gorlatova, N.; Day, D.E.; Moore, E.G.; Zabaleta, A.; McMahon, G.A.; Lawrence, D.A.
Mutants of plasminogen activator inhibitor-1 designed to inhibit neutrophil elastase and cathepsin G are more effective in vivo than their endogenous inhibitors
J. Biol. Chem.
279
29981-29987
2004
Homo sapiens
de Garavilla, L.; Greco, M.N.; Sukumar, N.; Chen, Z.W.; Pineda, A.O.; Mathews, F.S.; Di Cera, E.; Giardino, E.C.; Wells, G.I.; Haertlein, B.J.; Kauffman, J.A.; Corcoran, T.W.; Derian, C.K.; Eckardt, A.J.; Damiano, B.P.; Andrade-Gordon, P.; Maryanoff, B.E.
A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo
J. Biol. Chem.
280
18001-18007
2005
Homo sapiens (P08311), Homo sapiens
Shao, B.; Belaaouaj, A.; Verlinde, C.L.; Fu, X.; Heinecke, J.W.
Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase
J. Biol. Chem.
280
29311-29321
2005
Homo sapiens
Legedz, L7.; Randon, J.; Sessa, C.; Baguet, J.P.; Feugier, P.; Cerutti, C.; McGregor, J.; Bricca, G.
Cathepsin G is associated with atheroma formation in human carotid artery
J. Hypertens.
22
157-166
2004
Homo sapiens
Burster, T.; Beck, A.; Tolosa, E.; Marin-Esteban, V.; Roetzschke, O.; Falk, K.; Lautwein, A.; Reich, M.; Brandenburg, J.; Schwarz, G.; Wiendl, H.; Melms, A.; Lehmann, R.; Stevanovic, S.; Kalbacher, H.; Driessen, C.
Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes
J. Immunol.
172
5495-5503
2004
Homo sapiens
Sun, R.; Iribarren, P.; Zhang, N.; Zhou, Y.; Gong, W.; Cho, E.H.; Lockett, S.; Chertov, O.; Bednar, F.; Rogers, T.J.; Oppenheim, J.J.; Wang, J.M.
Identification of neutrophil granule protein cathepsin G as a novel chemotactic agonist for the G protein-coupled formyl peptide receptor
J. Immunol.
173
428-436
2004
Homo sapiens
Lesner, A.; Wysocka, M.; Guzow, K.; Wiczk, W.; Legowska, A.; Rolka, K.
Development of sensitive cathepsin G fluorogenic substrate using combinatorial chemistry methods
Anal. Biochem.
375
306-312
2008
Homo sapiens
Korkmaz, B.; Moreau, T.; Gauthier, F.
Neutrophil elastase, proteinase 3 and cathepsin G: physicochemical properties, activity and physiopathological functions
Biochimie
90
227-242
2008
Homo sapiens (P08311), Homo sapiens
Burster, T.; Beck, A.; Poeschel, S.; Oren, A.; Baechle, D.; Reich, M.; Roetzschke, O.; Falk, K.; Boehm, B.O.; Youssef, S.; Kalbacher, H.; Overkleeft, H.; Tolosa, E.; Driessen, C.
Interferon-gamma regulates cathepsin G activity in microglia-derived lysosomes and controls the proteolytic processing of myelin basic protein in vitro
Immunology
121
82-93
2007
Homo sapiens, Mus musculus
Campbell, E.J.; Owen, C.A.
The sulfate groups of chondroitin sulfate- and heparan sulfate-containing proteoglycans in neutrophil plasma membranes are novel binding sites for human leukocyte elastase and cathepsin G
J. Biol. Chem.
282
14645-14654
2007
Homo sapiens
Rykl, J.; Thiemann, J.; Kurzawski, S.; Pohl, T.; Gobom, J.; Zidek, W.; Schlueter, H.
Renal cathepsin G and angiotensin II generation
J. Hypertens.
24
1797-1807
2006
Homo sapiens (P08311), Sus scrofa (Q95284), Sus scrofa
Lim, J.K.; Lu, W.; Hartley, O.; DeVico, A.L.
N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and related analogs into a truncated 4-68 variant
J. Leukoc. Biol.
80
1395-1404
2006
Homo sapiens
Wysocka, M.; Legowska, A.; Bulak, E.; Jaskiewicz, A.; Miecznikowska, H.; Lesner, A.; Rolka, K.
New chromogenic substrates of human neutrophil cathepsin G containing non-natural aromatic amino acid residues in position P1 selected by combinatorial chemistry methods
Mol. Divers.
11
93-99
2007
Homo sapiens
Miyata, J.; Tani, K.; Sato, K.; Otsuka, S.; Urata, T.; Lkhagvaa, B.; Furukawa, C.; Sano, N.; Sone, S.
Cathepsin G: the significance in rheumatoid arthritis as a monocyte chemoattractant
Rheumatol. Int.
27
375-382
2007
Homo sapiens
Gale, A.J.; Rozenshteyn, D.
Cathepsin G, a leukocyte protease, activates coagulation factor VIII
Thromb. Haemost.
99
44-51
2008
Homo sapiens
Peterszegi, G.; Texier, S.; Robert, A.M.; Moulias, R.; Robert, L.
Increased elastase and cathepsin G activity in activated lymphocytes from aged patients Role of denutrition and dementia
Arch. Gerontol. Geriatr.
25
285-298
2008
Homo sapiens
Sienczyk, M.; Lesner, A.; Wysocka, M.; Legowska, A.; Pietrusewicz, E.; Rolka, K.; Oleksyszyn, J.
New potent cathepsin G phosphonate inhibitors
Bioorg. Med. Chem.
16
8863-8867
2008
Homo sapiens
Wilson, T.J.; Nannuru, K.C.; Singh, R.K.
Cathepsin G recruits osteoclast precursors via proteolytic activation of protease-activated receptor-1
Cancer Res.
69
3188-3195
2009
Homo sapiens, Mus musculus
Stoeckle, C.; Sommandas, V.; Adamopoulou, E.; Belisle, K.; Schiekofer, S.; Melms, A.; Weber, E.; Driessen, C.; Boehm, B.O.; Tolosa, E.; Burster, T.
Cathepsin G is differentially expressed in primary human antigen-presenting cells
Cell. Immunol.
255
41-45
2009
Homo sapiens
Mambole, A.; Baruch, D.; Nusbaum, P.; Bigot, S.; Suzuki, M.; Lesavre, P.; Fukuda, M.; Halbwachs-Mecarelli, L.
The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its extracellular domain and triggers its intramembrane proteolysis by presenilin/gamma-secretase
J. Biol. Chem.
283
23627-23635
2008
Homo sapiens (P08311)
Korkmaz, B.; Attucci, S.; Juliano, M.A.; Kalupov, T.; Jourdan, M.L.; Juliano, L.; Gauthier, F.
Measuring elastase, proteinase 3 and cathepsin G activities at the surface of human neutrophils with fluorescence resonance energy transfer substrates
Nat. Protoc.
3
991-1000
2008
Homo sapiens
Dabek, M.; Ferrier, L.; Roka, R.; Gecse, K.; Annahazi, A.; Moreau, J.; Escourrou, J.; Cartier, C.; Chaumaz, G.; Leveque, M.; Ait-Belgnaoui, A.; Wittmann, T.; Theodorou, V.; Bueno, L.
Luminal cathepsin g and protease-activated receptor 4: a duet involved in alterations of the colonic epithelial barrier in ulcerative colitis
Am. J. Pathol.
175
207-214
2009
Homo sapiens
Burster, T.; Macmillan, H.; Hou, T.; Schilling, J.; Truong, P.; Boehm, B.O.; Zou, F.; Lau, K.; Strohman, M.; Schaffert, S.; Busch, R.; Mellins, E.D.
Masking of a cathepsin G cleavage site in vivo contributes to the proteolytic resistance of major histocompatibility complex class II molecules
Immunology
130
436-46
2010
Homo sapiens
Tausch, L.; Henkel, A.; Siemoneit, U.; Poeckel, D.; Kather, N.; Franke, L.; Hofmann, B.; Schneider, G.; Angioni, C.; Geisslinger, G.; Skarke, C.; Holtmeier, W.; Beckhaus, T.; Karas, M.; Jauch, J.; Werz, O.
Identification of human cathepsin G as a functional target of boswellic acids from the anti-inflammatory remedy frankincense
J. Immunol.
183
3433-3442
2009
Homo sapiens (P08311), Homo sapiens
Kudo, T.; Kigoshi, H.; Hagiwara, T.; Takino, T.; Yamazaki, M.; Yui, S.
Cathepsin G, a neutrophil protease, induces compact cell-cell adhesion in MCF-7 human breast cancer cells
Mediators Inflamm.
2009
850940
2009
Homo sapiens
Reich, M.; Lesner, A.; Legowska, A.; Sienczyk, M.; Oleksyszyn, J.; Boehm, B.O.; Burster, T.
Application of specific cell permeable cathepsin G inhibitors resulted in reduced antigen processing in primary dendritic cells
Mol. Immunol.
46
2994-2999
2009
Homo sapiens
Burster, T.; Macmillan, H.; Hou, T.; Boehm, B.O.; Mellins, E.D.
Cathepsin G: roles in antigen presentation and beyond
Mol. Immunol.
47
658-665
2010
Homo sapiens, Mus musculus
Korkmaz, B.; Jegot, G.; Lau, L.C.; Thorpe, M.; Pitois, E.; Juliano, L.; Walls, A.F.; Hellman, L.; Gauthier, F.
Discriminating between the activities of human cathepsin G and chymase using fluorogenic substrates
FEBS J.
278
2635-2646
2011
Homo sapiens (P08311), Homo sapiens
Raymond, W.W.; Trivedi, N.N.; Makarova, A.; Ray, M.; Craik, C.S.; Caughey, G.H.
How immune peptidases change specificity: cathepsin G gained tryptic function but lost efficiency during primate evolution
J. Immunol.
185
5360-5368
2010
Homo sapiens, Mus musculus
Siao, S.C.; Li, K.J.; Hsieh, S.C.; Wu, C.H.; Lu, M.C.; Tsai, C.Y.; Yu, C.L.
Tamm-Horsfall glycoprotein enhances PMN phagocytosis by binding to cell surface-expressed lactoferrin and cathepsin G that activates MAP kinase pathway
Molecules
16
2119-2134
2011
Homo sapiens
Zou, F.; Schaefer, N.; Palesch, D.; Bruecken, R.; Beck, A.; Sienczyk, M.; Kalbacher, H.; Sun, Z.; Boehm, B.O.; Burster, T.
Regulation of cathepsin G reduces the activation of proinsulin-reactive T cells from type 1 diabetes patients
PLoS ONE
6
e22815
2011
Homo sapiens
Perrin, J.; Lecompte, T.; Tournier, A.; Morlon, L.; Marchand-Arvier, M.; Vigneron, C.
In vitro effects of human neutrophil cathepsin G on thrombin generation: Both acceleration and decreased potential
Thromb. Haemost.
104
514-522
2010
Homo sapiens
Wang, J.; Sjoeberg, S.; Tang, T.T.; Ooerni, K.; Wu, W.; Liu, C.; Secco, B.; Tia, V.; Sukhova, G.K.; Fernandes, C.; Lesner, A.; Kovanen, P.T.; Libby, P.; Cheng, X.; Shi, G.P.
Cathepsin G activity lowers plasma LDL and reduces atherosclerosis
Biochim. Biophys. Acta
1842
2174-2183
2014
Homo sapiens (P08311), Homo sapiens, Mus musculus (P28293)
Cohen-Mazor, M.; Mazor, R.; Kristal, B.; Sela, S.
Elastase and cathepsin G from primed leukocytes cleave vascular endothelial cadherin in hemodialysis patients
BioMed Res. Int.
2014
459640
2014
Homo sapiens (P08311), Homo sapiens
Woloszynek, J.C.; Hu, Y.; Pham, C.T.
Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions
J. Biol. Chem.
287
34101-34109
2012
Homo sapiens (P08311)
Faraday, N.; Schunke, K.; Saleem, S.; Fu, J.; Wang, B.; Zhang, J.; Morrell, C.; Dore, S.
Cathepsin G-dependent modulation of platelet thrombus formation in vivo by blood neutrophils
PLoS ONE
8
e71447
2013
Homo sapiens (P08311), Homo sapiens, Mus musculus (P28293), Mus musculus
Gudmann, N.S.; Manon-Jensen, T.; Sand, J.M.B.; Diefenbach, C.; Sun, S.; Danielsen, A.; Karsdal, M.A.; Leeming, D.J.
Lung tissue destruction by proteinase 3 and cathepsin G mediated elastin degradation is elevated in chronic obstructive pulmonary disease
Biochem. Biophys. Res. Commun.
503
1284-1290
2018
Homo sapiens
Groborz, K.; Kolt, S.; Kasperkiewicz, P.; Drag, M.
Internally quenched fluorogenic substrates with unnatural amino acids for cathepsin G investigation
Biochimie
166
103-111
2019
Homo sapiens
Gao, S.; Zhu, H.; Yang, H.; Zhang, H.; Li, Q.; Luo, H.
The role and mechanism of cathepsin G in dermatomyositis
Biomed. Pharmacother.
94
697-704
2017
Homo sapiens
Guo, J.; Tu, J.; Hu, Y.; Song, G.; Yin, Z.
Cathepsin G cleaves and activates IL-36gamma and promotes the inflammation of psoriasis
Drug Des. Devel. Ther.
13
581-588
2019
Homo sapiens
Penczek, A.; Sienczyk, M.; Wirtz, C.R.; Burster, T.
Cell surface cathepsin G activity differs between human natural killer cell subsets
Immunol. Lett.
179
80-84
2016
Homo sapiens
Fu, Z.; Thorpe, M.; Alemayehu, R.; Roy, A.; Kervinen, J.; de Garavilla, L.; Abrink, M.; Hellman, L.
Highly selective cleavage of cytokines and chemokines by the human mast cell chymase and neutrophil cathepsin G
J. Immunol.
198
1474-1483
2017
Homo sapiens
Eipper, S.; Steiner, R.; Lesner, A.; Sienczyk, M.; Palesch, D.; Halatsch, M.E.; Zaczynska, E.; Heim, C.; Hartmann, M.D.; Zimecki, M.; Wirtz, C.R.; Burster, T.
Lactoferrin is an allosteric enhancer of the proteolytic activity of cathepsin G
PLoS ONE
11
e0151509
2016
Homo sapiens
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