G W Wong1, Y Tang, R L Stevens. 1. Department of Medicine, Harvard Medical School, and Brigham and Women's Hospital, Boston, MA, USA.
Abstract
BACKGROUND: Three functionally distinct tryptases have been identified in the mouse, one of which encodes an unusual protease that possesses a membrane-spanning domain located in its C terminus. METHODS AND RESULTS: Using the deduced nucleotide sequence of this mouse transmembrane tryptase (mTMT) gene in a polymerase chain reaction approach, cDNAs were isolated from a number of tissues which encode its human homolog. The amino acid sequences of hTMT and mTMT are 74% identical, and the human tryptase also has the novel membrane-spanning domain. CONCLUSION: The discovery that the human genome contains a large number of homologous, but distinct, tryptase genes suggests that the individual members of this family of proteases evolved to carry out discrete functions in mast cell-mediated allergic reactions.
BACKGROUND: Three functionally distinct tryptases have been identified in the mouse, one of which encodes an unusual protease that possesses a membrane-spanning domain located in its C terminus. METHODS AND RESULTS: Using the deduced nucleotide sequence of this mousetransmembrane tryptase (mTMT) gene in a polymerase chain reaction approach, cDNAs were isolated from a number of tissues which encode its human homolog. The amino acid sequences of hTMT and mTMT are 74% identical, and the human tryptase also has the novel membrane-spanning domain. CONCLUSION: The discovery that the human genome contains a large number of homologous, but distinct, tryptase genes suggests that the individual members of this family of proteases evolved to carry out discrete functions in mast cell-mediated allergic reactions.
Authors: Bettina Sprinzl; Georg Greiner; Goekhan Uyanik; Michel Arock; Torsten Haferlach; Wolfgang R Sperr; Peter Valent; Gregor Hoermann Journal: Int J Mol Sci Date: 2021-02-28 Impact factor: 5.923