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-Tryptases, Novel Members of the Chromosome 16p Mast Cell Tryptase and Prostasin Gene Families1
Cardiovascular Research Institute and Department of Medicine, University of California, San Francisco, CA 94143
Previously, this laboratory identified clusters of 
-, ß-, and
mast cell protease-7-like tryptase genes on human chromosome 16p13.3.
The present work characterizes adjacent genes encoding novel serine
proteases, termed 
-tryptases, and generates a refined map of the
multitryptase locus. Each gene lies between an 1H
Ca2+ channel gene (CACNA1H) and a ßII- or
ßIII-tryptase gene and is 
30 kb from polymorphic minisatellite
MS205. The tryptase locus also contains at least four tryptase-like
pseudogenes, including mastin, a gene expressed in dogs but not in
humans. Genomic DNA blotting results suggest that I- and
II-tryptases are alleles at the same site. ßII- and
ßIII-tryptases appear to be alleles at a neighboring site, and II-
and ßI-tryptases appear to be alleles at a third site. -Tryptases
are transcribed in lung, intestine, and in several other tissues and in
a mast cell line (HMC-1) that also expresses -tryptase protein.
Immunohistochemical analysis suggests that -tryptase is expressed by
airway mast cells. -Tryptase catalytic domains are 48% identical
with those of known mast cell tryptases and possess mouse homologues.
We predict that -tryptases are glycosylated oligomers with tryptic
substrate specificity and a distinct mode of activation. A feature not
found in described tryptases is a C-terminal hydrophobic domain, which
may be a membrane anchor. Although the catalytic domains contain
tryptase-like features, the hydrophobic segment and intron-exon
organization are more closely related to another recently
described protease, prostasin. In summary, this work describes
-tryptases, which are novel members of chromosome 16p
tryptase/prostasin gene families. Their unique features suggest
possibly novel functions.
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