キマーゼ、チマーゼ、カイメース
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/05/26 03:05:47」(JST)
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chymase 1, mast cell |
Chymase with PMSF bound PDB: 1KLT
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Identifiers |
Symbol |
CMA1 |
Entrez |
1215 |
HUGO |
2097 |
OMIM |
118938 |
RefSeq |
NM_001836 |
UniProt |
P23946 |
Other data |
EC number |
3.4.21.39 |
Locus |
Chr. 14 q11.2 |
Chymases (EC 3.4.21.39, mast cell protease 1, skeletal muscle protease, skin chymotryptic proteinase, mast cell serine proteinase, skeletal muscle protease) are a family of serine proteases found primarily in mast cells, though also present in basophil granulocytes (e.g. alpha chymase mcpt8). They show broad peptidolytic activity and are involved in a variety of functions. For example, chymases are released by mucosal mast cells upon challenge with parasites and parasite antigens promoting an inflammatory response. Chymases are also known to convert angiotensin I to angiotensin II and thus play a role in hypertension and atherosclerosis.[1]
Because of its role in inflammation it has been investigated as a target in the treatment of asthma.[2]
References
- ^ Caughey, GH. Mast cell tryptases and chymases in inflammation and host defense. Immu Revs 2007 (217): 141-154. PMID 17498057
- ^ de Garavilla et al. Journal of Biochemistry 2005(280) pp.18001-18007.
Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
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Digestive enzymes |
- Enteropeptidase
- Trypsin
- Chymotrypsin
- Elastase
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Coagulation |
- factors: Thrombin
- Factor VIIa
- Factor IXa
- Factor Xa
- Factor XIa
- Factor XIIa
- Kallikrein
- PSA
- KLK1
- KLK2
- KLK3
- KLK4
- KLK5
- KLK6
- KLK7
- KLK8
- KLK9
- KLK10
- KLK11
- KLK12
- KLK13
- KLK14
- KLK15
- fibrinolysis: Plasmin
- Plasminogen activator
- Tissue plasminogen activator
- Urinary plasminogen activator
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Complement system |
- Factor B
- Factor D
- Factor I
- MASP
- C3-convertase
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Other immune system |
- Chymase
- Granzyme
- Tryptase
- Proteinase 3/Myeloblastin
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Venombin |
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Other |
- Acrosin
- Prolyl endopeptidase
- Pronase
- Proprotein convertases
- Prostasin
- Reelin
- Subtilisin/Furin
- Streptokinase
- S1P
- Cathepsin
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Enzymes
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Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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UpToDate Contents
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English Journal
- THE AUTOCRINE ROLE OF TRYPTASE IN PRESSURE OVERLOAD-INDUCED MAST CELL ACTIVATION, CHYMASE RELEASE AND CARDIAC FIBROSIS.
- Li J1, Jubair S1, Levick SP2, Janicki JS1.
- IJC metabolic & endocrine.IJC Metab Endocr.2016 Mar 1;10:16-23. Epub 2015 Nov 24.
- BACKGROUND: Cardiac mast cell (MC) proteases, chymase and tryptase, increase proliferation and collagen synthesis in cultured cardiac fibroblasts. However, the question as to why preventing individually the actions of either protease prevents fibrosis when both are released upon MC activation remain
- PMID 26722642
- Cathepsin K Contributes to Cavitation and Collagen Turnover in Pulmonary Tuberculosis.
- Kubler A1, Larsson C2, Luna B3, Andrade BB4, Amaral EP4, Urbanowski M3, Orandle M5, Bock K5, Ammerman NC3, Cheung LS3, Winglee K3, Halushka M6, Park JK7, Sher A4, Friedland JS8, Elkington PT9, Bishai WR3.
- The Journal of infectious diseases.J Infect Dis.2016 Feb 15;213(4):618-27. doi: 10.1093/infdis/jiv458. Epub 2015 Sep 27.
- Cavitation in tuberculosis enables highly efficient person-to-person aerosol transmission. We performed transcriptomics in the rabbit cavitary tuberculosis model. Among 17 318 transcripts, we identified 22 upregulated proteases. Five type I collagenases were overrepresented: cathepsin K (CTSK), mast
- PMID 26416658
- Improvement of cardiovascular remodeling by chymase inhibitor.
- Takai S1, Jin D2.
- Clinical and experimental pharmacology & physiology.Clin Exp Pharmacol Physiol.2016 Jan 22. doi: 10.1111/1440-1681.12549. [Epub ahead of print]
- Chymase has been identified as an angiotensin II-forming enzyme found in cardiovascular tissues. Angiotensin II is involved not only in the regulation of blood pressure, but also in the progression of cardiovascular remodeling. Interestingly, chymase inhibitors prevent cardiovascular remodeling with
- PMID 26798995
Japanese Journal
- A novel peptide of endothelin family, 31 amino-acid length endothelin in patients with acute myocardial infarction
- SIGNIFICANCE OF ANGIOTENSIN SYSTEM IN PROGRESSION OF COLORECTAL CANCER
Related Links
- Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion. ... 100% UniRef100 combines identical sequences and sub-fragments ...
- Structure-activity relationship studies of chloromethyl ketone derivatives for selective human chymase inhibitors: Y. Hayashi, et al.; Bioorg. Med. ... Chymase in exocytosed rat mast cell granules effectively proteolyzes apolipoprotein ...
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