Bovine tryptase (TPSB2)

Bovine tryptase is a major neutral serine protease found in the secretory granules of mast cells in cattle (Bos taurus) (UniProt: P56690). It is characterized by its unique tetrameric structure, which is stabilized by heparin or other glycosaminoglycans, protecting it from endogenous inhibitors (PDB: 1LTO). Upon mast cell activation and degranulation, bovine tryptase is released into the extracellular space where it exerts its proteolytic activity on various substrates. Its biological functions include the activation of protease-activated receptor 2 (PAR-2), the degradation of extracellular matrix proteins, and the processing of neuropeptides and cytokines (PubMed: 10430871). In the context of disease, tryptase is a key mediator of allergic inflammation and asthma, contributing to bronchoconstriction and tissue edema. While human tryptase is the primary clinical focus, bovine tryptase has been extensively used as a biochemical model to study enzyme kinetics and the binding of inhibitors like nafamostat and gabexate (PubChem: CID 4413). Research into this enzyme has provided foundational insights into the development of selective tryptase inhibitors for treating chronic inflammatory and allergic conditions.

Other names

Mast cell tryptaseTryptase-2Tryptase-1Serine protease 31TPS1TPS2

Competitive inhibition of the serine protease active site, preventing the cleavage of peptide substrates and subsequent activation of pro-inflammatory signaling pathways such as protease-activated receptor 2 (PAR-2).