Biology:Chymase
| chymase 1, mast cell | |
|---|---|
 Chymase with PMSF bound PDB: 1KLT | |
| Identifiers | |
| Symbol | CMA1 |
| NCBI gene | 1215 |
| HGNC | 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). Recently, Derakhshan et al. reported that a specific mast cell population expressed transcripts for Mcpt8.[1] They show broad peptidolytic activity and are involved in a variety of functions. For example, chymases are released by connective tissue-type mast cells upon challenge with parasites and parasite antigens promoting an inflammatory response, and chymase mcp1 and mcp2 are used for marker for mast cell degranulation in parasite infection such as Nematode,[2] Trichuris muris[3][4] Chymases are also known to convert angiotensin I to angiotensin II and thus play a role in hypertension and atherosclerosis.[5]
Because of its role in inflammation it has been investigated as a target in the treatment of asthma.[6]
References
- ↑ Derakhshan, Tahereh; Samuchiwal, Sachin K.; Hallen, Nils; Bankova, Lora G.; Boyce, Joshua A.; Barrett, Nora A.; Austen, K. Frank; Dwyer, Daniel F. (2021-01-04). "Lineage-specific regulation of inducible and constitutive mast cells in allergic airway inflammation" (in en). Journal of Experimental Medicine 218 (1): e20200321. doi:10.1084/jem.20200321. ISSN 0022-1007. PMID 32946563.
- ↑ "Mast cells disrupt epithelial barrier function during enteric nematode infection". Proceedings of the National Academy of Sciences of the United States of America 100 (13): 7761–6. June 2003. doi:10.1073/pnas.1231488100. PMID 12796512. Bibcode: 2003PNAS..100.7761M.
- ↑ "Mast cells, eosinophils and antibody-mediated cellular cytotoxicity are not critical in resistance to Trichuris muris". Parasite Immunology 21 (1): 45–52. January 1999. doi:10.1046/j.1365-3024.1999.00200.x. PMID 10081771.
- ↑ "B cells and antibodies are required for resistance to the parasitic gastrointestinal nematode Trichuris muris". Infection and Immunity 69 (6): 3860–8. June 2001. doi:10.1128/IAI.69.6.3860-3868.2001. PMID 11349052.
- ↑ "Mast cell tryptases and chymases in inflammation and host defense". Immunological Reviews 217: 141–54. June 2007. doi:10.1111/j.1600-065X.2007.00509.x. PMID 17498057.
- ↑ "A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo". The Journal of Biological Chemistry 280 (18): 18001–7. May 2005. doi:10.1074/jbc.M501302200. PMID 15741158.
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