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ADDITION / CORRECTIONThis article has been corrected. View the notice.

The Τumor Necrosis Factor-α Converting Enzyme (TACE):  A Unique Metalloproteinase with Highly Defined Substrate Selectivity

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Department of Biochemistry and Biophysics and Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, GlaxoSmithKline Inc., Research Triangle Park, North Carolina 27709, and Cognosci Inc., 2 Davis Drive, Research Triangle Park, North Carolina 27709
Cite this: Biochemistry 2002, 41, 30, 9462–9469
Publication Date (Web):June 27, 2002
https://doi.org/10.1021/bi0260132
Copyright © 2002 American Chemical Society

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    Abstract

    TNFα converting enzyme (TACE) processes precursor TNFα between Ala76 and Val77, yielding a correctly processed bioactive 17 kDa protein. Genetic evidence indicates that TACE may also be involved in the shedding of other ectodomains. Here we show that native and recombinant forms of TACE efficiently processed a synthetic substrate corresponding to the TNFα cleavage site only. For all other substrates, conversion occurred only at high enzyme concentrations and prolonged reaction times. Often, cleavage under those conditions was accompanied by nonspecific reactions. We also compared TNFα cleavage by TACE to cleavage by those members of the matrix metalloproteinase (MMP) family previously implied in TNFα release. The specificity constants for TNFα cleavage by the MMPs were approximately 100−1000-fold slower relative to TACE. MMP 7 also processed precursor TNFα at the correct cleavage site but did so with a 30-fold lower specificity constant relative to TACE. In contrast, MMP 1 processed precursor TNFα between Ala74 and Gln75, in addition to between Ala76 and Val77, while MMP 9 cleaved this natural substrate solely between Ala74 and Gln75. Additionally, the MMP substrate Dnp-PChaGC(Me)HK(NMA)-NH2 was not cleaved at all by TACE, while collagenase (ΜΜP 1), gelatinase (ΜΜP 9), stromelysin 1 (MMP 3), and matrilysin (MMP 7) all processed this substrate efficiently. All of these results indicate that TACE is unique in terms of its specificity requirements for substrate cleavage.

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     Supported partly by National Institutes of Health Grant AR45949 to M.E.M.

     University of Pennsylvania School of Medicine.

    §

     GlaxoSmithKline Inc.

     Current address:  Dow Corning Corp., Midland MI 48686-0994.

     Current address:  Rheumatology Research Labs, Hospital for Joint Diseases, New York University, New York, NY 10003.

    #

     Cognosci Inc.

    *

     To whom correspondence should be addressed. Tel:  215-898-7500. Fax:  215-573-4764. E-mail:  [email protected].

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