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J Biol Chem, Vol. 274, Issue 43, 30563-30570, October 22, 1999
From the The tumor necrosis factor-
Specific Sequence Elements Are Required for the Expression of
Functional Tumor Necrosis Factor-
-converting Enzyme (TACE)
,
,,,,,, Department of Biochemistry and Biophysics
and Johnson Research Foundation, University of Pennsylvania School of
Medicine, Philadelphia, Pennsylvania 19104 and the Divisions of
¶ Biochemistry and Chemistry, Glaxo Wellcome Research
and Development, Research Triangle Park, North Carolina 27709
-converting enzyme
(TACE) is a membrane-anchored zinc metalloprotease involved in
precursor tumor necrosis factor- secretion. We designed a series of
constructs containing full-length human TACE and several truncate forms
for overexpression in insect cells. Here, we demonstrate that
full-length TACE is expressed in insect cells inefficiently: only minor
amounts of this enzyme are converted from an inactive precursor to the mature, functional form. Removal of the cytoplasmic and transmembrane domains resulted in the efficient secretion of mature, active TACE.
Further removal of the cysteine-rich domain located between the
catalytic and transmembrane domains resulted in the secretion of mature
catalytic domain in association with the precursor (pro) domain. This
complex was inactive and function was only restored after dissociation
of the complex by dilution or treatment with 4-aminophenylmercuric
acetate. Therefore, the pro domain of TACE is an inhibitor of the
catalytic domain, and the cysteine-rich domain appears to play a role
in the release of the pro domain. Insect cells failed to secrete a
deletion mutant encoding the catalytic domain but lacking the
inhibitory pro domain. This truncate was inactive and extensively
degraded intracellularly, suggesting that the pro domain is required
for the secretion of functional TACE.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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