Cloning of the human homolog of mouse transmembrane tryptase.
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.
Wong
G W
GW
Department of Medicine, Harvard Medical School, and Brigham and Women's Hospital, Boston, MA, USA.
Tang
Y
Y
Stevens
R L
RL
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
D018076:DNA, Complementary; C509190:Tpsb2 protein, mouse; D012697:Serine Endopeptidases; C083294:chymase 2; D053818:Chymases; C509222:Tpsab1 protein, mouse; D053802:Tryptases