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J Biol Chem, Vol. 275, Issue 15, 11368-11378, April 14, 2000
From the Tissue inhibitor of metalloproteinase 2 (TIMP-2)
is required for the membrane type 1 matrix metalloproteinase
(MT1-MMP)-dependent activation of pro-MMP-2 on the cell
surface. MT1-MMP-bound TIMP-2 has been shown to function as a receptor
for secreted pro-MMP-2, resulting in the formation of a trimolecular
complex. In the presence of uncomplexed active MT1-MMP, the prodomain
of cell surface-associated MMP-2 is cleaved, and activated MMP-2 is
released. However, the behavior of MT1-MMP-bound TIMP-2 during MMP-2
activation is currently unknown. In this study,
125I-labeled recombinant TIMP-2
(125I-rTIMP-2) was used to investigate the fate of TIMP-2
during pro-MMP-2 activation by HT1080 and transfected A2058 cells.
HT1080 and A2058 cells transfected with MT1-MMP cDNA (but not
vector-transfected A2058 cells) were able to bind
125I-rTIMP-2, to activate pro-MMP-2, and to process MT1-MMP
into an inactive 43-kDa form. Under these conditions,
125I-rTIMP-2 bound to the cell surface was rapidly
internalized and degraded in intracellular organelles through a
bafilomycin A1-sensitive mechanism, and
125I-bearing low molecular mass fragment(s) were released
in the culture medium. These different processes were inhibited
by hydroxamic acid-based synthetic MMP inhibitors and rTIMP-2, but not
by rTIMP-1 or cysteine, serine, or aspartic proteinase inhibitors.
These results support the concept that the
MT1-MMP-dependent internalization and degradation of TIMP-2
by some tumor cells might be involved in the regulation of pericellular proteolysis.
Membrane Type 1 Matrix Metalloproteinase-associated
Degradation of Tissue Inhibitor of Metalloproteinase 2 in Human
Tumor Cell Lines*
,,,,,,§,
Laboratory of Tumor and Development Biology,
University of Liège, Tour de Pathologie (B23), Sart Tilman,
B-4000 Liège, Belgium and the ¶ School of Biological
Sciences, University of East Anglia,
Norwich NR4 7TJ, United Kingdom
*
This work was supported by grants from the Communauté
Française de Belgique (Actions de Recherche Concertées),
the Caisse Générale d'Epargne et de Retraite-Assurances
(1996-1999), the Association contre le Cancer, the Association
Sportive contre le Cancer, the Loterie Nationale, the Fonds de la
Recherche Scientifique Médicale, the Fonds d'Investissement de
Recherche Scientifique 1997-Centre Hospitalier Universitaire
Liège, the Center Anticancéreux près de
l'Université de Liège, and the Fondation Léon
Frédéricq, University of Liège, Liège (all in
Belgium); the General Reinsurance Luxembourg; the Commission of
European Communities (Concerted European Action Biotech
BIO4-CT96-0464); the Arthritis Research Campaign, United Kingdom (to
G. M.); and Roche Molecular Biochemicals, Mannheim, Germany.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
32-4-366-25-69; Fax: 32-4-366-29-36; E-mail:
jm.foidart@ulg.ac.be.
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