Chymase: Difference between revisions
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'''Chymases''' ({{EC number|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 protease]]s found primarily in [[mast cell]]s, though also present in [[basophil granulocyte]]s (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 [[parasitism|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]].<ref>Caughey | '''Chymases''' ({{EC number|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 protease]]s found primarily in [[mast cell]]s, though also present in [[basophil granulocyte]]s (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 [[parasitism|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]]<ref>{{cite journal | vauthors = McDermott JR, Bartram RE, Knight PA, Miller HR, Garrod DR, Grencis RK | title = Mast cells disrupt epithelial barrier function during enteric nematode infection | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 13 | pages = 7761–6 | date = June 2003 | pmid = 12796512 | doi = 10.1073/pnas.1231488100 | pmc = 164661 }}</ref>, [[Trichuris muris]]<ref>{{cite journal | vauthors = Betts CJ, Else KJ | title = Mast cells, eosinophils and antibody-mediated cellular cytotoxicity are not critical in resistance to Trichuris muris | journal = Parasite Immunology | volume = 21 | issue = 1 | pages = 45–52 | date = January 1999 | pmid = 10081771 }}</ref><ref>{{cite journal | vauthors = Blackwell NM, Else KJ | title = B cells and antibodies are required for resistance to the parasitic gastrointestinal nematode Trichuris muris | journal = Infection and Immunity | volume = 69 | issue = 6 | pages = 3860–8 | date = June 2001 | pmid = 11349052 | doi = 10.1128/IAI.69.6.3860-3868.2001 }}</ref> Chymases are also known to convert [[angiotensin]] I to angiotensin II and thus play a role in [[hypertension]] and [[atherosclerosis]].<ref name="pmid17498057">{{cite journal | vauthors = Caughey GH | title = Mast cell tryptases and chymases in inflammation and host defense | journal = Immunological Reviews | volume = 217 | issue = | pages = 141–54 | date = June 2007 | pmid = 17498057 | pmc = 2275918 | doi = 10.1111/j.1600-065X.2007.00509.x }}</ref> | ||
Because of its role in inflammation it has been investigated as a target in the treatment of asthma.<ref>de Garavilla | Because of its role in inflammation it has been investigated as a target in the treatment of asthma.<ref name="pmid15741158">{{cite journal | vauthors = de Garavilla L, Greco MN, Sukumar N, Chen ZW, Pineda AO, Mathews FS, Di Cera E, Giardino EC, Wells GI, Haertlein BJ, Kauffman JA, Corcoran TW, Derian CK, Eckardt AJ, Damiano BP, Andrade-Gordon P, Maryanoff BE | display-authors = 6 | title = A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and chymase: molecular mechanisms and anti-inflammatory activity in vivo | journal = The Journal of Biological Chemistry | volume = 280 | issue = 18 | pages = 18001–7 | date = May 2005 | pmid = 15741158 | doi = 10.1074/jbc.M501302200 }}</ref> | ||
== References == | == References == | ||
Revision as of 13:13, 5 June 2018
| chymase 1, mast cell | |
|---|---|
| File:1KLT.png Chymase with PMSF bound PDB: 1KLT | |
| 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, and chymase mcp1 and mcp2 are used for marker for mast cell degranulation in parasite infection such as Nematode[1], Trichuris muris[2][3] Chymases are also known to convert angiotensin I to angiotensin II and thus play a role in hypertension and atherosclerosis.[4]
Because of its role in inflammation it has been investigated as a target in the treatment of asthma.[5]
References
- ↑ McDermott JR, Bartram RE, Knight PA, Miller HR, Garrod DR, Grencis RK (June 2003). "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. doi:10.1073/pnas.1231488100. PMC 164661. PMID 12796512.
- ↑ Betts CJ, Else KJ (January 1999). "Mast cells, eosinophils and antibody-mediated cellular cytotoxicity are not critical in resistance to Trichuris muris". Parasite Immunology. 21 (1): 45–52. PMID 10081771.
- ↑ Blackwell NM, Else KJ (June 2001). "B cells and antibodies are required for resistance to the parasitic gastrointestinal nematode Trichuris muris". Infection and Immunity. 69 (6): 3860–8. doi:10.1128/IAI.69.6.3860-3868.2001. PMID 11349052.
- ↑ Caughey GH (June 2007). "Mast cell tryptases and chymases in inflammation and host defense". Immunological Reviews. 217: 141–54. doi:10.1111/j.1600-065X.2007.00509.x. PMC 2275918. PMID 17498057.
- ↑ de Garavilla L, Greco MN, Sukumar N, Chen ZW, Pineda AO, Mathews FS, et al. (May 2005). "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. doi:10.1074/jbc.M501302200. PMID 15741158.
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