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. These genes are characterized by several distinct features. They have a highly conserved 3' UTR and contain tandem repeat sequences at the 5' flank and 3' UTR which are thought to play a role in regulation of the mRNA stability. These genes have an intron immediately upstream of the initiator Met codon, which separates the site of transcription initiation from protein coding sequence. This feature is characteristic of tryptases but is unusual in other genes. The alleles of this gene exhibit an unusual amount of sequence variation, such that the alleles were once thought to represent two separate genes, beta II and beta III. Beta tryptases appear to be the main isoenzymes expressed in mast cells, whereas in basophils, alpha-tryptases predominate. Tryptases have been implicated as mediators in the pathogenesis of asthma and other allergic and inflammatory disorders.
Hallgren J, Lindahl S, Pejler G (2005). "Structural requirements and mechanism for heparin-dependent activation and tetramerization of human betaI- and betaII-tryptase.". J. Mol. Biol.345 (1): 129–39. doi:10.1016/j.jmb.2004.10.029. PMID15567416.
Sommerhoff CP, Bode W, Matschiner G, et al. (2000). "The human mast cell tryptase tetramer: a fascinating riddle solved by structure.". Biochim. Biophys. Acta1477 (1-2): 75–89. doi:10.1016/s0167-4838(99)00265-4. PMID10708850.
Huang C, Li L, Krilis SA, et al. (1999). "Human tryptases alpha and beta/II are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft.". J. Biol. Chem.274 (28): 19670–6. doi:10.1074/jbc.274.28.19670. PMID10391906.
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.
Guida M, Riedy M, Lee D, Hall J (2000). "Characterization of two highly polymorphic human tryptase loci and comparison with a newly discovered monkey tryptase ortholog.". Pharmacogenetics10 (5): 389–96. doi:10.1097/00008571-200007000-00002. PMID10898108.
Pallaoro M, Fejzo MS, Shayesteh L, et al. (1999). "Characterization of genes encoding known and novel human mast cell tryptases on chromosome 16p13.3.". J. Biol. Chem.274 (6): 3355–62. doi:10.1074/jbc.274.6.3355. PMID9920877.
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.
Pereira PJ, Bergner A, Macedo-Ribeiro S, et al. (1998). "Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.". Nature392 (6673): 306–11. doi:10.1038/32703. PMID9521329.
Wu C, Ma MH, Brown KR, et al. (2007). "Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening.". Proteomics7 (11): 1775–85. doi:10.1002/pmic.200601006. PMID17474147.