CMA1
Protein-coding gene in the species Homo sapiens
CMA1 Identifiers Aliases CMA1 External IDs OMIM : 118938 ; MGI : 96941 ; GeneCards : CMA1 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3S0N , 1NN6 , 4AFS , 1PJP , 1T31 , 2HVX , 3N7O , 4AG1 , 4K69 , 4KP0 , 1KLT , 4AFZ , 4AG2 , 4K2Y , 4K60 , 4AFU , 4K5Z , 4AFQ
Gene location (Mouse ) Chr. Chromosome 14 (mouse) Band 14 C3| 14 28.19 cM Start 56,178,908 bp End 56,182,132 bp
Wikidata
Chymase is an enzyme that in humans is encoded by the CMA1 gene .
This gene product is a chymotryptic serine proteinase that belongs to the peptidase family S1. It is expressed in mast cells and thought to function in the degradation of the extracellular matrix , the regulation of submucosal gland secretion, and the generation of vasoactive peptides . In the heart and blood vessels, this protein, rather than angiotensin converting enzyme, is largely responsible for converting angiotensin I to the vasoactive peptide angiotensin II. Angiotensin II has been implicated in blood pressure control and in the pathogenesis of hypertension , cardiac hypertrophy , and heart failure . Thus, this gene product is a target for cardiovascular disease therapies. This gene maps to 14q11.2 in a cluster of genes encoding other proteases.
References
1 2 3 GRCh38: Ensembl release 89: ENSG00000092009 – Ensembl , May 20171 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022225 – Ensembl , May 2017↑ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .↑ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .↑ Caughey GH, Schaumberg TH, Zerweck EH, Butterfield JH, Hanson RD, Silverman GA, Ley TJ (May 1993). "The human mast cell chymase gene (CMA1): mapping to the cathepsin G/granzyme gene cluster and lineage-restricted expression". Genomics . 15 (3): 614– 20. doi :10.1006/geno.1993.1115 . PMID 8468056 . ↑ "Entrez Gene: CMA1 chymase 1, mast cell" .
Further reading
Urata H, Nishimura H, Ganten D (1996). "Chymase-dependent angiotensin II forming systems in humans" . Am. J. Hypertens . 9 (3): 277– 84. doi :10.1016/0895-7061(95)00349-5 PMID 8695029 . Takai S, Miyazaki M (2003). "Effect of chymase inhibitor on vascular proliferation" . Jpn. J. Pharmacol . 90 (3): 223– 7. doi :10.1254/jjp.90.223 PMID 12499576 . Urata H, Kinoshita A, Perez DM, et al. (1991). "Cloning of the gene and cDNA for human heart chymase" . J. Biol. Chem . 266 (26): 17173– 9. doi :10.1016/S0021-9258(19)47355-9 PMID 1894611 . Jenne DE, Tschopp J (1991). "Angiotensin II-forming heart chymase is a mast-cell-specific enzyme" . Biochem. J . 276 (2): 567– 8. doi :10.1042/bj2760567 . PMC 1151130 PMID 2049082 . Caughey GH, Zerweck EH, Vanderslice P (1991). "Structure, chromosomal assignment, and deduced amino acid sequence of a human gene for mast cell chymase" . J. Biol. Chem . 266 (20): 12956– 63. doi :10.1016/S0021-9258(18)98788-0 PMID 2071582 . Urata H, Boehm KD, Philip A, et al. (1993). "Cellular localization and regional distribution of an angiotensin II-forming chymase in the heart" (PDF) . J. Clin. Invest . 91 (4): 1269– 81. doi :10.1172/JCI116325 . PMC 288095 PMID 7682566 . Saarinen J, Kalkkinen N, Welgus HG, Kovanen PT (1994). "Activation of human interstitial procollagenase through direct cleavage of the Leu83-Thr84 bond by mast cell chymase" . J. Biol. Chem . 269 (27): 18134– 40. doi :10.1016/S0021-9258(17)32427-4 PMID 8027075 . Schechter NM, Wang ZM, Blacher RW, et al. (1994). "Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions" . J. Immunol . 152 (8): 4062– 9. doi :10.4049/jimmunol.152.8.4062 PMID 8144971 . Schechter NM, Jordan LM, James AM, et al. (1993). "Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties" . J. Biol. Chem . 268 (31): 23626– 33. doi :10.1016/S0021-9258(19)49508-2 PMID 8226889 . Sukenaga Y, Kido H, Neki A, et al. (1993). "Purification and molecular cloning of chymase from human tonsils" . FEBS Lett . 323 (1– 2): 119– 22. doi :10.1016/0014-5793(93)81461-8 PMID 8495723 . S2CID 3925572 . Nakano A, Kishi F, Minami K, et al. (1997). "Selective conversion of big endothelins to tracheal smooth muscle-constricting 31-amino acid-length endothelins by chymase from human mast cells" . J. Immunol . 159 (4): 1987– 92. doi :10.4049/jimmunol.159.4.1987 PMID 9257865 . McGrath ME, Mirzadegan T, Schmidt BF (1998). "Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A". Biochemistry . 36 (47): 14318– 24. doi :10.1021/bi971403n . PMID 9400368 . Kishi F, Minami K, Okishima N, et al. (1998). "Novel 31-amino-acid-length endothelins cause constriction of vascular smooth muscle". Biochem. Biophys. Res. Commun . 248 (2): 387– 90. doi :10.1006/bbrc.1998.8980 . PMID 9675146 . Pereira PJ, Wang ZM, Rubin H, et al. (1999). "The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity". J. Mol. Biol . 286 (1): 163– 73. doi :10.1006/jmbi.1998.2462 . PMID 9931257 . Pereira PJ, Wang ZM, Rubin H, et al. (1999). "The 2.2 A Crystal Structure of Human Chymase in Complex with Succinyl-Ala-Ala-Pro-Phe-chloromethylketone: Structural Explanation for its Dipeptidyl Carboxypeptidase Specificity" . Journal of Molecular Biology . 286 (4): 817. doi :10.1006/jmbi.1999.2691 PMID 10208809 . de Paulis A, Minopoli G, Dal Piaz F, et al. (1999). "Novel autocrine and paracrine loops of the stem cell factor/chymase network". Int. Arch. Allergy Immunol . 118 (2– 4): 422– 5. doi :10.1159/000024153 . PMID 10224464 . S2CID 29124141 . Caughey GH, Raymond WW, Wolters PJ (2000). "Angiotensin II generation by mast cell alpha- and beta-chymases". Biochim. Biophys. Acta . 1480 (1– 2): 245– 57. doi :10.1016/S0167-4838(00)00076-5 . PMID 10899625 . Mellon MB, Frank BT, Fang KC (2002). "Mast cell alpha-chymase reduces IgE recognition of birch pollen profilin by cleaving antibody-binding epitopes" . J. Immunol . 168 (1): 290– 7. doi :10.4049/jimmunol.168.1.290 PMID 11751973 .
External links
PDB gallery
1klt : CRYSTAL STRUCTURE OF PMSF-TREATED HUMAN CHYMASE AT 1.9 ANGSTROMS RESOLUTION
1nn6 : Human Pro-Chymase
1pjp : THE 2.2 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE
1t31 : A Dual Inhibitor of the Leukocyte Proteases Cathepsin G and Chymase with Therapeutic Efficacy in Animals Models of Inflammation
