Chymase (CMA1) (CMA1)

Chymase (CMA1), also known as Mast cell protease I, is a chymotrypsin-like serine protease primarily stored in the secretory granules of mast cells. Upon mast cell activation and degranulation, chymase is released into the extracellular environment where it functions as a major non-ACE (angiotensin-converting enzyme) pathway for the generation of angiotensin II from angiotensin I. This activity is particularly prominent in the heart and vascular tissues during chronic disease states, contributing to hypertension, cardiac hypertrophy, and heart failure. Beyond the renin-angiotensin system, chymase is involved in tissue remodeling and inflammation by activating pro-fibrotic factors like transforming growth factor-beta (TGF-beta) and pro-inflammatory cytokines such as interleukin-1 beta (IL-1beta). It also degrades extracellular matrix components, which can lead to tissue damage in conditions like chronic obstructive pulmonary disease (COPD) and atherosclerosis. Due to its diverse roles in pathology, chymase is a significant therapeutic target, with several small-molecule inhibitors like fulacimstat being developed to treat cardiovascular and fibrotic diseases.

Other names

Mast cell protease IAlpha-chymaseCYMCYHSkeletal muscle proteaseMast cell protease-1 (rodent homolog)

Chymase inhibition