Chymase is an
enzyme that in humans is encoded by the CMA1gene.[5]
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.[6]
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.
PMID9400368.
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.
PMID9675146.
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.
PMID9931257.
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.
PMID10224464.
S2CID29124141.
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.
PMID10899625.
Chymase is an
enzyme that in humans is encoded by the CMA1gene.[5]
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.[6]
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.
PMID9400368.
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.
PMID9675146.
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.
PMID9931257.
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.
PMID10224464.
S2CID29124141.
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.
PMID10899625.