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Hamster chymase is a chymotrypsin-like serine protease primarily localized within the secretory granules of mast cells. In the Syrian hamster (Mesocricetus auratus), this enzyme functions similarly to human chymase (CMA1) by serving as a major non-ACE pathway for the generation of Angiotensin II from Angiotensin I (Jin et al., 1998, PubMed: 9634404). Beyond its role in the renin-angiotensin system, it is involved in the activation of pro-fibrotic factors such as TGF-beta and the degradation of the extracellular matrix (Takai et al., 2004, PubMed: 15131263). These activities link hamster chymase to the progression of cardiac remodeling, heart failure, and various inflammatory conditions like atopic dermatitis. Because of its high functional homology to the human enzyme, hamster chymase is frequently used as a target in preclinical studies to evaluate the therapeutic potential of chymase inhibitors (He et al., 1998, PubMed: 9738411). Inhibitors such as TY-51184 and SUN-C8257 have demonstrated efficacy in reducing fibrosis and improving cardiac function in hamster models.
Inhibition of the serine protease catalytic site to prevent the conversion of Angiotensin I to Angiotensin II and the proteolytic activation of pro-fibrotic mediators.
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