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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

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. 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.[1]

References

  1. Cloning of the human homolog of mouse transmembrane tryptase. Wong, G.W., Tang, Y., Stevens, R.L. Int. Arch. Allergy Immunol. (1999) [Pubmed]
 
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