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J Biol Chem, Vol. 274, Issue 6, 3531-3540, February 5, 1999
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From the Metalloprotease disintegrins are a
family of membrane-anchored glycoproteins that are known to function in
fertilization, myoblast fusion, neurogenesis, and ectodomain shedding
of tumor necrosis factor (TNF)- Cellular Biochemistry and Biophysics
Program, ** Molecular Biology Program, Laboratori
de Recerca Oncologica, Hospital General, Psg. Vall d'Hebron, 08035 Barcelona, Spain
. Here we report the analysis of the
intracellular maturation and catalytic activity of the widely expressed
metalloprotease disintegrin MDC9. Our results suggest that the
pro-domain of MDC9 is removed by a furin-type pro-protein convertase in
the secretory pathway before the protein emerges on the cell surface.
The soluble metalloprotease domain of MDC9 cleaves the insulin B-chain,
a generic protease substrate, providing the first evidence that MDC9 is
catalytically active. Soluble MDC9 appears to have distinct specificities for cleaving candidate substrate peptides compared with
the TNF- convertase (TACE/ADAM17). The catalytic activity of MDC9
can be inhibited by hydroxamic acid-type metalloprotease inhibitors in
the low nanomolar range, in one case with up to 50-fold selectivity for
MDC9 versus TACE. Peptides mimicking the predicted
cysteine-switch region of MDC9 or TACE inhibit both enzymes in the low
micromolar range, providing experimental evidence for regulation of
metalloprotease disintegrins via a cysteine-switch mechanism. Finally,
MDC9 is shown to become phosphorylated when cells are treated with the
phorbol ester phorbol 12-myristate 13-acetate, a known inducer of
protein ectodomain shedding. This work implies that removal of the
inhibitory pro-domain of MDC9 by a furin-type pro-protein convertase in
the secretory pathway is a prerequisite for protease activity. After
pro-domain removal, additional steps, such as protein kinase
C-dependent phosphorylation, may be involved in regulating
the catalytic activity of MDC9, which is likely to target different
substrates than the related TNF--convertase.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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