Abstract
Mast cell (MC) phenotypes may vary with respect to tissue site, sensitivity to degranulating agents, dependency on T lymphocytes and, above all, the composition of their granules. Proteinases (either trypsin-like or chymotrypsin-like) are granule constituents which provide an important means of distinguishing subtypes of MCs in man and rodents. The purpose of this study was to compare the distribution of MC trypsin-like protease (tryptase) in a variety of bovine tissues with the aim of examining MC heterogeneity. Tryptase was found in MCs regardless of their location within tissues. With respect to tryptase content, bovine MC distribution resembled more that of human and canine tissues than that of mice and rats. Comparison of the results yielded by enzyme- and immuno-histochemical staining suggested that a tryptase-negative, dual-specific chymase-positive MC subset occurred, at least in duodenal lamina propria, around bronchioles and within alveolar septa. The study also suggested that monoclonal antibodies raised against human tryptase can be used for quantitation of bovine tryptase in biological fluids; this offers a promising tool for evaluating the role of MC activation in disease.
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