CMA1

Chymase 1, mast cell, also known as CMA1, is a human gene.

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: CMA1 chymase 1, mast cell| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1215| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Urata H, Nishimura H, Ganten D |title=Chymase-dependent angiotensin II forming systems in humans. |journal=Am. J. Hypertens. |volume=9 |issue= 3 |pages= 277–84 |year= 1996 |pmid= 8695029 |doi=
*cite journal | author=Takai S, Miyazaki M |title=Effect of chymase inhibitor on vascular proliferation. |journal=Jpn. J. Pharmacol. |volume=90 |issue= 3 |pages= 223–7 |year= 2003 |pmid= 12499576 |doi=
*cite journal | author=Urata H, Kinoshita A, Perez DM, "et al." |title=Cloning of the gene and cDNA for human heart chymase. |journal=J. Biol. Chem. |volume=266 |issue= 26 |pages= 17173–9 |year= 1991 |pmid= 1894611 |doi=
*cite journal | author=Jenne DE, Tschopp J |title=Angiotensin II-forming heart chymase is a mast-cell-specific enzyme. |journal=Biochem. J. |volume=276 ( Pt 2) |issue= |pages= 567–8 |year= 1991 |pmid= 2049082 |doi=
*cite journal | author=Caughey GH, Zerweck EH, Vanderslice P |title=Structure, chromosomal assignment, and deduced amino acid sequence of a human gene for mast cell chymase. |journal=J. Biol. Chem. |volume=266 |issue= 20 |pages= 12956–63 |year= 1991 |pmid= 2071582 |doi=
*cite journal | author=Urata H, Boehm KD, Philip A, "et al." |title=Cellular localization and regional distribution of an angiotensin II-forming chymase in the heart. |journal=J. Clin. Invest. |volume=91 |issue= 4 |pages= 1269–81 |year= 1993 |pmid= 7682566 |doi=
*cite journal | author=Saarinen J, Kalkkinen N, Welgus HG, Kovanen PT |title=Activation of human interstitial procollagenase through direct cleavage of the Leu83-Thr84 bond by mast cell chymase. |journal=J. Biol. Chem. |volume=269 |issue= 27 |pages= 18134–40 |year= 1994 |pmid= 8027075 |doi=
*cite journal | author=Schechter NM, Wang ZM, Blacher RW, "et al." |title=Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions. |journal=J. Immunol. |volume=152 |issue= 8 |pages= 4062–9 |year= 1994 |pmid= 8144971 |doi=
*cite journal | author=Schechter NM, Jordan LM, James AM, "et al." |title=Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties. |journal=J. Biol. Chem. |volume=268 |issue= 31 |pages= 23626–33 |year= 1993 |pmid= 8226889 |doi=
*cite journal | author=Caughey GH, Schaumberg TH, Zerweck EH, "et al." |title=The human mast cell chymase gene (CMA1): mapping to the cathepsin G/granzyme gene cluster and lineage-restricted expression. |journal=Genomics |volume=15 |issue= 3 |pages= 614–20 |year= 1993 |pmid= 8468056 |doi= 10.1006/geno.1993.1115
*cite journal | author=Sukenaga Y, Kido H, Neki A, "et al." |title=Purification and molecular cloning of chymase from human tonsils. |journal=FEBS Lett. |volume=323 |issue= 1-2 |pages= 119–22 |year= 1993 |pmid= 8495723 |doi=
*cite journal | author=Nakano A, Kishi F, Minami K, "et al." |title=Selective conversion of big endothelins to tracheal smooth muscle-constricting 31-amino acid-length endothelins by chymase from human mast cells. |journal=J. Immunol. |volume=159 |issue= 4 |pages= 1987–92 |year= 1997 |pmid= 9257865 |doi=
*cite journal | author=McGrath ME, Mirzadegan T, Schmidt BF |title=Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A. |journal=Biochemistry |volume=36 |issue= 47 |pages= 14318–24 |year= 1998 |pmid= 9400368 |doi= 10.1021/bi971403n
*cite journal | author=Kishi F, Minami K, Okishima N, "et al." |title=Novel 31-amino-acid-length endothelins cause constriction of vascular smooth muscle. |journal=Biochem. Biophys. Res. Commun. |volume=248 |issue= 2 |pages= 387–90 |year= 1998 |pmid= 9675146 |doi= 10.1006/bbrc.1998.8980
*cite journal | author=Pereira PJ, Wang ZM, Rubin H, "et al." |title=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=J. Mol. Biol. |volume=286 |issue= 1 |pages= 163–73 |year= 1999 |pmid= 9931257 |doi= 10.1006/jmbi.1998.2462
*cite journal | author=Pereira PJ, Wang ZM, Rubin H, "et al." |title=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= |volume=286 |issue= 4 |pages= 817 |year= |pmid= 10208809 |doi= 10.1006/jmbi.1999.2691
*cite journal | author=de Paulis A, Minopoli G, Dal Piaz F, "et al." |title=Novel autocrine and paracrine loops of the stem cell factor/chymase network. |journal=Int. Arch. Allergy Immunol. |volume=118 |issue= 2-4 |pages= 422–5 |year= 1999 |pmid= 10224464 |doi=
*cite journal | author=Caughey GH, Raymond WW, Wolters PJ |title=Angiotensin II generation by mast cell alpha- and beta-chymases. |journal=Biochim. Biophys. Acta |volume=1480 |issue= 1-2 |pages= 245–57 |year= 2000 |pmid= 10899625 |doi=
*cite journal | author=Mellon MB, Frank BT, Fang KC |title=Mast cell alpha-chymase reduces IgE recognition of birch pollen profilin by cleaving antibody-binding epitopes. |journal=J. Immunol. |volume=168 |issue= 1 |pages= 290–7 |year= 2002 |pmid= 11751973 |doi=

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