Any feedback?
Information on EC 3.4.21.39 - chymase and Organism(s) Mus musculus
for references in articles please use BRENDA:EC3.4.21.39Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.21.39 chymaseSpecify your search results
Word Map
- 3.4.21.39
- tryptase
- granule
-
degranulation
- histamine
-
allergic
- chemokines
- ige
- cathepsin
- cardiac
- artery
- fibrosis
- neutrophil
-
angiotensin-converting
-
eosinophil
- cardiovascular
- monocyte
- asthma
- heparin
- airway
-
renin-angiotensin
- rantes
-
chemoattractant
- carboxypeptidase
- c-kit
- eotaxin
- renin
- elastase
-
chemotactic
-
basophil
- angiotensinogen
- endothelins
- anaphylaxis
-
anaphylactic
- toluidine
-
granzyme
- mastocytosis
-
tryptase-positive
-
atopic
-
exocytosed
- fcepsilonri
- cromolyn
-
anti-ige
- nippostrongylus
-
mip-1alpha
-
cell-deficient
-
mip-1beta
- medicine
- 3clpro
-
enzyme-histochemical
-
non-ace
-
ige-mediated
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
chymase, mcp-4, mast cell chymase, mast cell protease, chymotrypsin-like protease, mmcp-1, mcp-5, alpha-chymase, rmcp i, mast cell protease 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAGE
-
-
-
-
chymase
mast cell chymase
mast cell protease
mast cell protease 4
mast cell protease I
-
-
-
-
MC protease 4
MCP-1
MCP-4
MCP-5
MCPT4
MMCP-1
proteinase, mast cell serine, chymase
-
-
-
-
RMCP I
-
-
-
-
skeletal muscle protease
-
-
-
-
skin chymotryptic proteinase
-
-
-
-
chymase
-
-
-
-
MMCP-1
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
97501-92-3
-
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
atrial natriuretic peptide clearance receptor + H2O
?
-
potential substrate
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
no activity with enzyme forms 1D and 1E
-
-
?
benzoyl-L-Tyr-4-nitroanilide + H2O
benzoyl-L-Tyr + 4-nitroaniline
-
activity with enzyme form 1A, no activity with enzyme form 1B, 1C, 1D, 1E
-
-
?
benzyloxycarbonyl-Ala-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Ala + 4-nitrophenyl
-
-
-
-
?
benzyloxycarbonyl-Arg-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Arg + 4-nitrophenol
-
no activity with enzyme form 1B, 1C and 1E
-
-
?
benzyloxycarbonyl-D-Ala-4-nitrophenyl ester + H2O
benzyloxycarbonyl + D-Ala-4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Phe-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Phe + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Trp-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Trp + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Tyr-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Tyr-4-nitrophenyl ester
-
no activity with enzyme form 1C and 1E
-
-
?
big-endothelin-1 (1-38) + H2O
endothelin-1 (1-31) + ?
-
chymase cleaves the tyrosine31-glycine32 peptide bond of big-endothelin-1 (1-38)
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
methoxysuccinyl-Arg-Pro-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Pro-Tyr + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Leu-L-Leu-L-Val-L-Tyr-4-nitroanilide + H2O
N-succinyl-L-Leu-L-Leu-L-Val-L-Tyr + 4-nitroaniline
-
-
-
?
pro-matrix metalloprotease 2 + H2O
matrix metalloprotease 2 + propeptide
-
-
-
-
?
pro-matrix metalloprotease 9 + H2O
matrix metalloprotease 9 + propeptide
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Ala-L-Pro-L-Phe-7-amido-4-methylcoumarin + H2O
succinyl-L-Ala-L-Ala-L-Pro-L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Phe-4-nitroanilide + H2O
succinyl-Phe + 4-nitroaniline
-
no activity with enzyme form 1C and 1D
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
methoxy-succinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxy-succinyl-Arg-Ala-Tyr + 4-nitroaniline
-
high activity
-
-
?
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
-
?
methoxysuccinyl-Arg-Ala-Tyr-4-nitroanilide + H2O
methoxysuccinyl-Arg-Ala-Tyr + 4-nitroaniline
-
-
-
?
additional information
?
-
-
in position P1 a distinct preference for Phe and Ser is observed, in position P2 a high selectivity for Phe, Trp and Leu is detected, while P3 and P4 show specificity for aliphatic amino acids
-
-
?
additional information
?
-
-
no activity with acetyl-Ile-Glu-Pro-Asp-p-nitroanilide, acetyl-Tyr-Val-Ala-Asp-p-nitroanilide, methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide, N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, H-D-Ile-Pro-Arg-p-nitroanilide, N-(p-tosyl)-Gly-Pro-Arg-p-nitroanilide, N-(p-tosyl)-Gly-Pro-Lys-p-nitroanilide, N-succinyl-Ala-Ala-Ala-p-nitroanilide, methoxy-succinyl-Ala-Ala-Pro-Met-p-nitroanilide, acetyl-Ile-Glu-Pro-Asp-p-nitroanilide, methoxy-succinyl-Arg-Pro-Tyr-p-nitroanilide, and N-(p-tosyl)-Gly-Pro-Lys-p-nitroanilide
-
-
?
additional information
?
-
-
prefers Phe in the P1 position (56%), followed by Tyr (28%) and Trp (16%), position P2 is most often occupied by Leu (22%), in positions P3 Val is the preferred amino acid, in position P4 is a preference for Val (20%) and Trp (19%) over other hydrophobic amino acids
-
-
?
additional information
?
-
interleukin-7, interleukin-22, GM-CSF, and CCL2 are resistant to chymase degradation
-
-
?
additional information
?
-
-
interleukin-7, interleukin-22, GM-CSF, and CCL2 are resistant to chymase degradation
-
-
?
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
big-endothelin-1 (1-38) + H2O
endothelin-1 (1-31) + ?
-
chymase cleaves the tyrosine31-glycine32 peptide bond of big-endothelin-1 (1-38)
-
-
?
pro-matrix metalloprotease 2 + H2O
matrix metalloprotease 2 + propeptide
-
-
-
-
?
pro-matrix metalloprotease 9 + H2O
matrix metalloprotease 9 + propeptide
-
-
-
-
?
additional information
?
-
interleukin-7, interleukin-22, GM-CSF, and CCL2 are resistant to chymase degradation
-
-
?
additional information
?
-
-
interleukin-7, interleukin-22, GM-CSF, and CCL2 are resistant to chymase degradation
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(5-formylamino-6-oxo-2-phenyl-1,6-dihydropyrimidine-1-yl)-N-[[3,4-dioxo-1-phenyl-7-(2-pyridyloxy)]-2-heptyl]acetamide
-
NK3201
2-[2-[2-[5-amino-2-(3-methoxy-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
i.e. Y40079, novel, potent and orally active chymase inhibitor which would be a useful tool in elucidating the pathophysiological roles of chymase
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
3-[(3,4-dimethoxyphenyl)sulfonyl]-1-(3,4-dimethylphenyl)imidazoline-2,4-dione
-
C41
4-[1-[[bis-(4-methyl-phenyl)-methyl]-carbamoyl]-3-(2-ethoxy-benzyl)-4-oxo-azetidine-2-yloxy]-benzoic acid
-
-
N-[2-[5-amino-2-(3-chloro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetyl]-N,N'-dibenzyl-2,2-difluoro-malonamide
-
novel, potent, and orally active inhibitor. Rapidly after oral administration and has satisfactory bioavailability
succinyl-Val-Pro-PheP-(OPh)2
-
highly-specific and metabolically stable chymase inhibitor with a biological half-life of more than 20 h
SUN-C8007
-
i.e. 3-(3-aminophenylsulfonyl)-7-chloroquinazorine-2, 4(1H,3H)-dione
SUN-C8257
-
i.e. 3-[(3-amino-4-carboxy)phenylsulfonyl]-7-chloroquinazorine 2,4(1H,3H)-dione
suramin
-
i.e. 8,8'-[carbonylbis[imino-3,1-phenylenecarbonylimino(4-methyl-3,1-phenylene)carbonylimino]]bis-1,3,5-naphthalenetrisulfonic acid
TY-51184
-
highly-specific and orally-active chymase inhibitor; i.e. 2-[4-(5-fluoro-3-methylbenzo[b]thiophen-2-yl)sulfonamide-3-methanesulfonylphenyl]oxazole-4-carboxylic acid
Y-40018
-
i.e. 4-[5-amino-2-(3-chlorophenyl)-6-oxo-1,6-dihydropyrimidin-1-ylacetamido]-N-benzyl-2,2-difluoro-3-oxo-5-phenylpentanamide
Y-40079
-
i.e. 2-[2-[2-[5-amino-2-(3-methoxyphenyl)-6-oxo-1,6-dihydropyrimidin-1-yl]acetamido]-3-phenylpropionyl]benzoxazole-5-carboxylic acid methyl ester
chymostatin
-
[(S)-1-carboxy-2-phenylethyl]-carbamoyl-alpha-[2-iminohexahydro-4(S)-pyrimidyl]-(S)-Gly-X-Phe-al, X can be the amino acid Leu, Val, or Ile, nonspecific chymase inhibitor
chymostatin
-
i.e. (S)-1-carboxy-2-(phenylethyl)-carbamoyl-alpha-[2-iminohexahydro-4(S)-pyrimidyl]-(S)-glycyl-X-phenylalaninal
TY-51469
-
i.e. 2-[4-(5-fluoro-3-methylbenzo[b]thiophen-2-yl)sulfonamido-3-methanesulfonylphenyl]thiazole-4-carboxylic acid; inhibitor with very high affinity against chymase
TY-51469
specific chymase inhibitor, i.e. 2-[4-(5-fluoro-3-methylbenzo[b]thiophen-2-yl)sulfonamido-3-methanesulfonylphenyl]thiazole-4-carboxylic acid
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000639
2-[2-[2-[5-amino-2-(3-methoxy-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
0.0000404
2-[2-[2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetylamido]-3-phenyl-propionyl]-benzooxazole-5-carboxylic acid methyl ester
-
-
0.00126
N-[2-[5-amino-2-(3-chloro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-acetyl]-N,N'-dibenzyl-2,2-difluoro-malonamide
-
pH 7.5, 37°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
656450, 656451, 669431, 679660, 680106, 680107, 680108, 681972, 681974, 682851, 695966, 697768, 697863, 699756, 701374, 709272, 717909
-
-
chymases with Val199 are found only in animals expressing multiple chymases, consistent with the premise that their substrate specificity differs from that of chymases with Gly199
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
chymase inhibition improves LV function and decreases adverse cardiac remodeling after myocardial infarction
malfunction
,ice deficient in mouse mast cell protease 4 (MCP4) have increased obstruction-induced fibrosis when compared to wild type mice. Kidneys of MCP4-deficient mice have higher levels of renal tubular damage, interstitial fibrosis, collagen deposition, increased a-smooth muscle actin, and decreased E-cadherin expression compared to the kidneys of wild type mice
malfunction
enzyme-deficient mice exhibit higher numbers of peritoneal neutrophils and increased acute kidney injury after cecal ligation and puncture, and also have significantly higher mortality after this procedure
malfunction
levels of inflammation and fibrosis are reduced in mast cell chymase MCPT4-deficient mice as compared with WT mice at day 7 after bleomycin-induced lung injury
malfunction
MCP-4-defeicient mice demonstrate elevated airway reactivity and eosinophilia in allergic airway inflammation induced by house-dust mite compared with wild type animals. The elevated airway and inflammatory responses of mMCP-4-deficient mice are associated with a profound increase in the levels of interleukin-33 in the lung tissue
physiological function
mast cell chymase degrades alarmins and may limit inflammation
physiological function
mast cell chymase plays a protective role in airway inflammation by regulation of interleukin-33
physiological function
mast cell released mast cell protease 4 has anti-fibrotic potential in acutely induced obstructive nephropathy
physiological function
MCP-4 can enhance survival after cecal ligation and puncture at least in part by limiting detrimental effects of tissue necrosis factor
physiological function
MCPT4 chymase contributes to bleomycin-induced lung inflammation and fibrosis
physiological function
-
the enzyme decreases the severity of group B Streptococcus infections
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). CMA1_MOUSE
247
0
27586
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
32000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
5 variant glycoforms, differences in the electrophoretic mobility between the variant forms of MMCP-1 are probably a result of variable glycosylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme deficient animal, lack in processing of pro-matrix metalloprotease 9 to its active form and marked defect in processing of pro-matrix metalloprotease 2. Mutant animals show an increase in collagen in the ear tissue accompanied by increased ear thickness and a higher content in hydroxyproline. Lung and ear tissue of mutant animals show increased staining for fibronectin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NAT agarose bead chromatography, heparin affinity chromatography, and gel filtration
-
Ni-NTA agarose bead chromatography and heparin-Sepharose column chromatograohy
-
Ni-NTA agarose bead chromatography and heparin-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
chronic angiotensin I-converting enzyme inhibition causes a marked bradykinin/B2 receptor-mediated increase in left ventricle interstitial fluid chymase activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
chymase is involved in angiotnesin II-induced abdominal aortic aneurysm development in apolipoprotein E-deficient mice
medicine
-
MCP-4 has a dual role in the development of autoimmune arthritis, first in the initiation phase of collagen-induced arthritis by stimulating the production of pathogenic immunglobulin G anti-collagen II antibodies, and second in the effector phase of arthritis by stimulating local joint inflammation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Newlands, G.F.Y.; Knox, D.P.; Pirie-Sheperd, S.R.; Miller, H.R.P.
Biochemical and immunological characterization of multiple glycoforms of mouse mast cell protease 1: comparison with an isolated murine serosal mast cell protease (MMCP-4)
Biochem. J.
294
127-135
1993
Mus musculus
Solivan, S.; Selwood, T.; Wang, Z.M.; Schechter, N.M.
Evidence for diversity of substrate specificity among members of the chymase family of serine proteases
FEBS Lett.
512
133-138
2002
Meriones unguiculatus, Cricetinae, Mus musculus, Rattus norvegicus
Akahoshi, F.; Ashimori, A.; Sakashita, H.; Yoshimura, T.; Imada, T.; Nakajima, M.; Mitsutomi, N.; Kuwahara, S.; Ohtsuka, T.; Fukaya, C.; Miyazaki, M.; Nakamura, N.
Synthesis, structure-activity relationships, and pharmacokinetic profiles of nonpeptidic alpha-keto heterocycles as novel inhibitors of human chymase
J. Med. Chem.
44
1286-1296
2001
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Akahoshi, F.; Ashimori, A.; Sakashita, H.; Yoshimura, T.; Eda, M.; Imada, T.; Nakajima, M.; Mitsutomi, N.; Kuwahara, S.; Ohtsuka, T.; Fukaya, C.; Miyazaki, M.; Nakamura, N.
Synthesis, structure-activity relationships, and pharmacokinetic profiles of nonpeptidic difluoromethylene ketones as novel inhibitors of human chymase
J. Med. Chem.
44
1297-1304
2001
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Tchougounova, E.; Lundequist, A.; Fajardo, I.; Winberg, J.O.; Abrink, M.; Pejler, G.
A key role for mast cell chymase in the activation of pro-matrix metalloprotease-9 and pro-matrix metalloprotease-2
J. Biol. Chem.
280
9291-9296
2005
Mus musculus
Terakawa, M.; Tomimori, Y.; Goto, M.; Fukuda, Y.
Mast cell chymase induces expression of chemokines for neutrophils in eosinophilic EoL-1 cells and mouse peritonitis eosinophils
Eur. J. Pharmacol.
538
175-181
2006
Homo sapiens, Mus musculus
Gallwitz, M.; Hellman, L.
Rapid lineage-specific diversification of the mast cell chymase locus during mammalian evolution
Immunogenetics
58
641-654
2006
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Gallwitz, M.; Enoksson, M.; Hellman, L.
Expression profile of novel members of the rat mast cell protease (rMCP)-2 and (rMCP)-8 families, and functional analyses of mouse mast cell protease (mMCP)-8
Immunogenetics
59
391-405
2007
Mus musculus, Rattus norvegicus
Caughey, G.H.
Mast cell tryptases and chymases in inflammation and host defense
Immunol. Rev.
217
141-154
2007
Homo sapiens, Mus musculus
Andersson, M.K.; Pemberton, A.D.; Miller, H.R.; Hellman, L.
Extended cleavage specificity of mMCP-1, the major mucosal mast cell protease in mouse - High specificity indicates high substrate selectivity
Mol. Immunol.
45
2548-2558
2008
Mus musculus
Andersson, M.K.; Karlson, U.; Hellman, L.
The extended cleavage specificity of the rodent beta-chymases rMCP-1 and mMCP-4 reveal major functional similarities to the human mast cell chymase
Mol. Immunol.
45
766-775
2008
Mus musculus, Rattus norvegicus
Vaali, K.; Puumalainen, T.J.; Lehto, M.; Wolff, H.; Rita, H.; Alenius, H.; Palosuo, T.
Murine model of food allergy after epicutaneous sensitization: role of mucosal mast cell protease-1
Scand. J. Gastroenterol.
41
1405-1413
2006
Mus musculus
Inoue, N.; Muramatsu, M.; Jin, D.; Takai, S.; Hayashi, T.; Katayama, H.; Kitaura, Y.; Tamai, H.; Miyazaki, M.
Effects of chymase inhibitor on angiotensin II-induced abdominal aortic aneurysm development in apolipoprotein E-deficient mice
Atherosclerosis
204
359-364
2008
Mus musculus
Terakawa, M.; Fujieda, Y.; Tomimori, Y.; Muto, T.; Tanaka, T.; Maruoka, H.; Nagahira, K.; Ogata, A.; Nakatsuka, T.; Fukuda, Y.
Oral chymase inhibitor SUN13834 ameliorates skin inflammation as well as pruritus in mouse model for atopic dermatitis
Eur. J. Pharmacol.
601
186-191
2008
Mus musculus
Magnusson, S.E.; Pejler, G.; Kleinau, S.; Abrink, M.
Mast cell chymase contributes to the antibody response and the severity of autoimmune arthritis
FASEB J.
23
875-882
2009
Mus musculus
Simard, E.; Jin, D.; Takai, S.; Miyazaki, M.; Brochu, I.; DOrleans-Juste, P.
Chymase-dependent conversion of Big endothelin-1 in the mouse in vivo
J. Pharmacol. Exp. Ther.
328
540-548
2009
Mus musculus
DOrleans-Juste, P.; Houde, M.; Rae, G.A.; Bkaily, G.; Carrier, E.; Simard, E.
Endothelin-1 (1-31): from chymase-dependent synthesis to cardiovascular pathologies
Vascul. Pharmacol.
49
51-62
2008
Homo sapiens, Mus musculus
Wei, C.C.; Hase, N.; Inoue, Y.; Bradley, E.W.; Yahiro, E.; Li, M.; Naqvi, N.; Powell, P.C.; Shi, K.; Takahashi, Y.; Saku, K.; Urata, H.; Dellitalia, L.J.; Husain, A.
Mast cell chymase limits the cardiac efficacy of Ang I-converting enzyme inhibitor therapy in rodents
J. Clin. Invest.
120
1229-1239
2010
Mus musculus
Akahoshi, M.; Song, C.H.; Piliponsky, A.M.; Metz, M.; Guzzetta, A.; Abrink, M.; Schlenner, S.M.; Feyerabend, T.B.; Rodewald, H.R.; Pejler, G.; Tsai, M.; Galli, S.J.
Mast cell chymase reduces the toxicity of Gila monster venom, scorpion venom, and vasoactive intestinal polypeptide in mice
J. Clin. Invest.
121
4180-4191
2011
Mus musculus
Piliponsky, A.M.; Chen, C.C.; Rios, E.J.; Treuting, P.M.; Lahiri, A.; Abrink, M.; Pejler, G.; Tsai, M.; Galli, S.J.
The chymase mouse mast cell protease 4 degrades TNF, limits inflammation, and promotes survival in a model of sepsis
Am. J. Pathol.
181
875-886
2012
Mus musculus (P21812), Mus musculus
Roy, A.; Ganesh, G.; Sippola, H.; Bolin, S.; Sawesi, O.; Dagaelv, A.; Schlenner, S.M.; Feyerabend, T.; Rodewald, H.R.; Kjellen, L.; Hellman, L.; Abrink, M.
Mast cell chymase degrades the alarmins heat shock protein 70, biglycan, HMGB1, and interleukin-33 (IL-33) and limits danger-induced inflammation
J. Biol. Chem.
289
237-250
2014
Mus musculus (P21812), Mus musculus, Homo sapiens (P23946), Homo sapiens
Reber, L.L.; Daubeuf, F.; Pejler, G.; Abrink, M.; Frossard, N.
Mast cells contribute to bleomycin-induced lung inflammation and injury in mice through a chymase/mast cell protease 4-dependent mechanism
J. Immunol.
192
1847-1854
2014
Mus musculus (P21812), Mus musculus
Houde, M.; Jamain, M.D.; Labonte, J.; Desbiens, L.; Pejler, G.; Gurish, M.; Takai, S.; DOrleans-Juste, P.
Pivotal role of mouse mast cell protease 4 in the conversion and pressor properties of Big-endothelin-1
J. Pharmacol. Exp. Ther.
346
31-37
2013
Mus musculus (P21812), Mus musculus
Beghdadi, W.; Madjene, L.C.; Claver, J.; Pejler, G.; Beaudoin, L.; Lehuen, A.; Daugas, E.; Blank, U.
Mast cell chymase protects against renal fibrosis in murine unilateral ureteral obstruction
Kidney Int.
84
317-326
2013
Mus musculus (P21812), Mus musculus
Waern, I.; Lundequist, A.; Pejler, G.; Wernersson, S.
Mast cell chymase modulates IL-33 levels and controls allergic sensitization in dust-mite induced airway inflammation
Mucosal Immunol.
6
911-920
2013
Mus musculus (P21812), Mus musculus
de Souza, D.A.; Toso, V.D.; Campos, M.R.; Lara, V.S.; Oliver, C.; Jamur, M.C.
Expression of mast cell proteases correlates with mast cell maturation and angiogenesis during tumor progression
PLoS ONE
7
e40790
2012
Mus musculus, Mus musculus (P21812)
de Souza Junior, D.A.; Santana, A.C.; da Silva, E.Z.; Oliver, C.; Jamur, M.C.
The role of mast cell specific chymases and tryptases in tumor angiogenesis
BioMed Res. Int.
2015
142359
2015
Homo sapiens, Mus musculus
EXTERNAL LINKS (specific for EC-Number 3.4.21.39)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
