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J Biol Chem, Vol. 273, Issue 25, 15514-15520, June 19, 1998
From the Department of Medicine and the Cardiovascular Research
Institute, University of California, San Francisco,
California 94143-0911
Dipeptidyl peptidase I (DPPI) is a cysteine
protease found predominantly in myelomonocytic cells, cytotoxic
T-cells, and mast cells. Recent studies identify an intracellular role
for mast cell-DPPI (MC-DPPI) by activating prochymase and protryptase
to their mature forms. To better define MC-DPPI and to explore the possibility of extracellular roles, we purified MC-DPPI from
mastocytoma cells. We found the dog C2 mastocytoma cell line to be the
richest source yet described for DPPI, purifying up to 200 µg of
enzyme per g of cells. Dog MC-DPPI has an Mr of
~175,000 and consists of four subunits, each composed of a
propeptide, light chain, and heavy chain. The heavy chain is
N-glycosylated and is heterogeneously processed to three
different forms. NH2-terminal sequences of the heavy chain
and propeptide are identical to those predicted from a cDNA clone
we sequenced from a mastocytoma cDNA library. The dog
cDNA-derived sequence is 86% identical to that of human DPPI. Dog
mastocytoma cells incubated with
12-O-tetradecanoylphorbol-13-acetate increase expression of
MC-DPPI mRNA. MC-DPPI maintains its activity for dipeptide
substrates at a neutral to alkaline pH. Cells stimulated with ionophore
or substance P secrete MC-DPPI in parallel with the granule-associated
mediators tryptase and histamine. Thus, dog mastocytoma cells
secrete DPPI that is active at the pH of extracellular fluids,
suggesting that MC-DPPI may act outside the cell.
Regulated Expression, Processing, and Secretion of Dog Mast Cell
Dipeptidyl Peptidase I
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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