tps-2

Tryptases are Trypsin-like Serine Proteases. β-Tryptases are the main isoenzymes in mast cells. Βtryptases form active tetramers with heparin proteoglycan. In the tetramer, the unique arrangement of the active sites facing a narrow central pore, β-Tryptases are resistant to macromolecule protease inhibitors . When mast cells are activated, β-Tryptases are released and participate in provoking inflammatory conditions . β-Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic disorders.

Tryptases are serine proteases with trypsin-like specificity. Together with chymases and Cathepsin G, tryptases are important players in mast cell mediation of inflammatory and allergic responses. Tryptase alpha/beta-1(TPSAB1), also known as mast cell protease 7 (MCPT7), it exhibits anticoagulant activity due to its ability to degrade fibrinogen in the presence of a diverse array of protease inhibitors in plasma. The two Isoform 1 and isoform 2 are expressed in lung, stomach, spleen, heart and skin; in these tissues, isoform 1 is predominant. Isoform 2 is expressed in aorta, spleen, and breast tumor, with highest levels in the endothelial cells of some blood vessels surrounding the aorta, as well as those surrounding the tumor and low levels, if any, in mast cells. Isoform 2 cleaves large substrates, such as fibronectin, more efficiently than isoform 1, but seems less efficient toward small substrates. It may play a role in innate immunity.

TPSAB1, namely tryptase alpha/beta-1, is a serine protease with trypsin­like activity. TPSAB1 is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type. It may play a role in innate immunity. Diseases associated with TPSAB1 include mastocytosis and systemic mastocytosis.