Mast cell chymase

Mast cell chymase is a monomeric serine protease predominantly expressed and stored in the secretory granules of mast cells, with its human form encoded by the CMA1 gene[1][3]. It exhibits strong chymotrypsin-like proteolytic activity, preferentially cleaving peptide bonds after aromatic amino acids such as phenylalanine, tyrosine, and tryptophan[1][3]. Chymase is critical in regulating inflammation, degrading extracellular matrix components, and activating or inactivating peptides like angiotensin II, influencing vascular function and tissue remodeling[1][2][3][4]. It is implicated in various pathological and physiological processes, including atherosclerosis, abdominal aortic aneurysm, obesity, diabetes, and their complications, making it a potential therapeutic target[2][4]. Selective inhibitors of mast cell chymase are under investigation for their benefits in cardiovascular and metabolic diseases[2][3]. Safety concerns include possible impacts on normal physiological processes, especially immune defense and tissue repair, should chymase activity be broadly suppressed[2][3].

Other names

ChymaseChymotrypsin-like proteaseCMA1 (human)Mast cell serine protease

Inhibition of enzymatic (chymase/serine protease) activity to prevent peptide and protein cleavage relevant for inflammation, tissue remodeling, and disease progression