title: Cloning of the human homolog of mouse transmembrane tryptase.
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.
  
  
  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.
  
  
  CONCLUSIONS
  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.affiliation: Department of Medicine, Harvard Medical School, and Brigham and Women's Hospital, Boston, MA, USA.
authors.forename: G W
authors.initials: GW
authors.lastname: Wong
authors.forename: Y
authors.initials: Y
authors.lastname: Tang
authors.forename: R L
authors.initials: RL
authors.lastname: Stevens
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D053818:Chymases; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000032:analysis / Q000235:genetics; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics*; D053802:Tryptases
chemical_list: D018076:DNA, Complementary; C509190:Tpsb2 protein, mouse; D012697:Serine Endopeptidases; C083294:chymase 2; D053818:Chymases; C509222:Tpsab1 protein, mouse; D053802:Tryptases