Inhibition of dipeptidyl peptidase I in the human mast cell line HMC-1: blocked activation of tryptase, but not of the predominant chymotryptic activity.

Abstract

The mast cell proteases tryptase and chymase are synthesised as inactive precursors, but are stored and secreted as active enzymes. The cysteinyl protease dipeptidyl peptidase I (DPPI, cathepsin C) can activate the corresponding proenzymes in cell-free systems, but it is unknown whether it fulfils this role within the intact cell. We, therefore, tested the… (More)

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@article{Sheth2003InhibitionOD, title={Inhibition of dipeptidyl peptidase I in the human mast cell line HMC-1: blocked activation of tryptase, but not of the predominant chymotryptic activity.}, author={Parimal D Sheth and John Pedersen and Andrew F. Walls and Alan R. Mceuen}, journal={Biochemical pharmacology}, year={2003}, volume={66 11}, pages={2251-62} }