TAILIEUCHUNG - Báo cáo khoa học: The heterogeneity of mast cell tryptase from human lung and skin Differences in size, charge and substrate affinity

Therehas longbeenconjectureover thedegree towhichthere may be structural and functional heterogeneity in the tetra-mericserineproteasetryptase(EC ), amajor mediator of allergic inflammation. We have applied 2D gel electrophoresis to analyze the extent, nature, and variability of thisheterogeneity inlysatesofmast cells isolatedfromlung and skin, and in preparations of purified tryptase. Gels were silver stained, or the proteins transferred to nitrocellulose blots and probed with either tryptase-specific monoclonal antibodies or various lectins. . | Eur. J. Biochem. 270 270-283 2003 FEBS 2003 doi The heterogeneity of mast cell tryptase from human lung and skin Differences in size charge and substrate affinity Qi Peng1 Alan R. McEuen1 R. Christopher Benyon2 and Andrew F. Walls1 1 Immunopharmacology Group and 2Tissue Remodelling and Repair University of Southampton School of Medicine Southampton General Hospital Southampton UK There has long been conjecture over the degree to which there may be structural and functional heterogeneity in the tetrameric serine protease tryptase EC a major mediator of allergic inflammation. We have applied 2D gel electrophoresis to analyze the extent nature and variability of this heterogeneity in lysates of mast cells isolated from lung and skin and in preparations of purified tryptase. Gels were silver stained or the proteins transferred to nitrocellulose blots and probed with either tryptase-specific monoclonal antibodies or various lectins. Tryptase was the major protein constituent in mast cell lysates and presented as an array of 9-12 diffuse immunoreactive spots with molecular masses ranging from 29 to 40 kDa and pl values from to . Although the patterns obtained for lung and skin tryptase were broadly similar differences were observed between tissues and between individual donors. Lectin binding studies indicated the presence of mono-antennary or bi-antennary complex-type oligosaccharide with varying degrees of sialylation. Deglycosylation with protein-N-glycosidase F PNGase F reduced the size of both lung and skin tryptase while incubation with PNGase F or neuraminidase narrowed the pI range indicating variable degrees of glycosylation as a major contributor to the size and charge heterogeneity. Comparison of different purified preparations of lung and skin tryptase revealed no significant difference in pH profiles but differences were seen in reactivity towards a range of chromogenic substrates with substantial differences

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