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Human mast cell β-tryptase is a trypsin-like serine protease and the major secretory granule protease of human mast cells. Encoded by the TPSAB1 and TPSB2 genes on chromosome 16p13.3, β-tryptase forms a homotetrameric structure stabilized by heparin proteoglycans, with active sites oriented toward the inner cavity of the tetramer. It is released upon mast cell activation and is resistant to most endogenous protease inhibitors. β-Tryptase plays key roles in mediating allergic inflammation, airway hyperresponsiveness, tissue remodeling, and the pathogenesis of asthma and anaphylaxis. Levels are elevated in conditions such as anaphylactic shock and systemic mastocytosis, making it a useful biomarker. Therapeutically, inhibition of β-tryptase is being pursued to treat inflammatory and allergic diseases
Competitive inhibition of β-tryptase’s serine protease active site; Allosteric inhibition disrupting tetramer stabilization; Inhibition of PAR-2 activation; Blockade of mast cell degranulation and mediator release
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