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CUTTING EDGE |
Converting Enzyme Inhibits ProTNF and TNFRII Secretion
Department of Inflammatory Diseases Research, DuPont Pharmaceuticals Company, Wilmington, DE 19880
TNF-
converting enzyme (TACE) is the protease responsible for
processing proTNF from the 26-kDa membrane-anchored precursor to the
secreted 17-kDa TNF-. We show here that a deletion mutant of TACE
(dTACE), lacking the pro and catalytic domains of the protease, acts as
a dominant negative for proTNF processing in transfected HEK293 cells.
We used the same system to test the effect of dTACE on TNFRII
processing. Overexpression of dTACE with TNFRII resulted in >80%
inhibition of TNFRII shedding. Although significant inhibition of
TNF- and TNFRII shedding was achieved with dTACE, we could not
detect a cell surface accumulation of the noncleaved substrates above
that observed in the absence of dTACE. Our results suggest that TNFRII
is a substrate for TACE, and that dTACE is capable of interfering with
the function of endogenous TACE, either by binding and sequestering
TACE substrates via the disintegrin domain, transmembrane domain, or
cytoplasmic tail, or by some other mechanism that has yet to be
determined.
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