Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. Tryptases are enzymatically active only as heparin-stabilized tetramers, and they are resistant to all known endogenous proteinase inhibitors. Several tryptase genes are clustered on chromosome 16p13.3. There is uncertainty regarding the number of genes in this cluster. Currently four functional genes - alpha I, beta I, beta II and gamma I - have been identified. And beta I has an allelic variant named alpha II, beta II has an allelic variant beta III, also gamma I has an allelic variant gamma II. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha-tryptases predominant. This gene differs from other members of the tryptase gene family in that it has C-terminal hydrophobic domain, which may serve as a membrane anchor. Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders.
Caughey GH, Raymond WW, Blount JL, et al. (2000). "Characterization of human gamma-tryptases, novel members of the chromosome 16p mast cell tryptase and prostasin gene families.". J. Immunol.164 (12): 6566–75. doi:10.4049/jimmunol.164.12.6566. PMID10843716.
Wong GW, Foster PS, Yasuda S, et al. (2002). "Biochemical and functional characterization of human transmembrane tryptase (TMT)/tryptase gamma. TMT is an exocytosed mast cell protease that induces airway hyperresponsiveness in vivo via an interleukin-13/interleukin-4 receptor alpha/signal transducer and activator of transcription (STAT) 6-dependent pathway.". J. Biol. Chem.277 (44): 41906–15. doi:10.1074/jbc.M205868200. PMID12194977.
Daniels RJ, Peden JF, Lloyd C, et al. (2001). "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16.". Hum. Mol. Genet.10 (4): 339–52. doi:10.1093/hmg/10.4.339. PMID11157797.
Wong GW, Tang Y, Feyfant E, et al. (1999). "Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extension.". J. Biol. Chem.274 (43): 30784–93. doi:10.1074/jbc.274.43.30784. PMID10521469.
Xiang M, Gu Y, Zhao F, et al. (2010). "Mast cell tryptase promotes breast cancer migration and invasion.". Oncol. Rep.23 (3): 615–9. doi:10.3892/or_00000676. PMID20126998.