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Tryptase Is Expressed in Multiple Human Tissues, and a Recombinant Form Has Proteolytic Activity1
* Inflammation and
Cytokine Research Units, Department of Pathology,
School of Biochemistry and Molecular Genetics, University of New South Wales, and
Victor Chang Cardiac Research Institute, Sydney, Australia
Tryptases are neutral serine proteases selectively expressed in
mast cells and have been implicated in the development of a number of
inflammatory diseases including asthma. It has recently been
established that the number of genes encoding human mast cell tryptases
is much larger than originally believed, but it is not clear how many
of these genes are expressed. A recent report suggested that the
transcript for at least one of these genes, originally named
mMCP-7-like tryptase, is not expressed. To further address this
question, we screened tissue-specific RNA samples by RT-PCR, using
primers designed to match the putative exonic sequence of this gene. We
successfully generated and cloned the correctly sized RT-PCR product
from mRNA isolated from the human mast cell-I cell line. Two distinct
clones were identified whose nucleotide sequence matched the published
sequence of the mMCP-7-like I and mMCP-7-like II genes. Transcripts
were detected in a wide variety of human tissues including lung, heart,
stomach, spleen, skin, and colon. A polyclonal antipeptide Ab that
specifically recognizes the translated product of this transcript was
used to demonstrate its expression in mast cells that reside in the
colon, lung, and inflamed synovium. A recombinant form of this protein
expressed in bacterial cells was able to cleave a synthetic
trypsin-sensitive substrate, D-Ile-Phe-Lys pNA. These
results suggest that the range of functional tryptases is larger than
previously recognized. For simplicity, we suggest that the gene,
transcripts, and corresponding protein product be named 
tryptase.
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