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Vol. 273, Issue 2, 871-880, January 9, 1998
From the We have used C-terminal domain
mutants to further define the role of interactions of progelatinase A
and membrane type 1 matrix metalloproteinase (MT1 MMP) in the binding
of TIMP2 and in the cell-associated activation of progelatinase A. Soluble constructs of MT1 MMP were used to demonstrate that binding
with TIMP2 occurs primarily through N-terminal domain interactions,
leaving the C-terminal domain free for interactions with progelatinase
A. The rate of autolytic activation of progelatinase A initiated by MT1
MMP cleavage could be potentiated by concentration of the proenzyme by
binding to heparin. Residues 568-631 of the progelatinase A C-terminal
domain are important in formation of the heparin binding site, since
replacement of this region with the corresponding stromelysin-1
sequence abolished binding to heparin and the potentiation of
activation. The same region of gelatinase A was required for binding of
latent and active enzyme to TIMP2, but residues 418-474 were not
important. A similar pattern was seen using cell membrane-associated MT1 MMP; residues 568-631 were required for binding and activation of
progelatinase A, whereas residues 418-474 were not. Neither region was
required for activation in solution. The addition of TIMP2 to HT1080
membrane preparations expressing MT1 MMP, but depleted of endogenous
TIMP2, resulted in potentiation of progelatinase A activation. This
effect was dependent upon TIMP2 binding to MT1 MMP rather than at an
independent membrane site. Together, the data suggest that TIMP2 forms
a receptor with MT1 MMP that regulates the concentration and efficient
generation of functionally active gelatinase A.
The TIMP2 Membrane Type 1 Metalloproteinase "Receptor"
Regulates the Concentration and Efficient Activation of Progelatinase
A
A KINETIC STUDY
,,,,
,, and
Strangeways Research Laboratory, Worts'
Causeway, Cambridge CB1 4RN and School of Biological Sciences,
University of East Anglia, Norwich NR4 7TJ, United Kingdom,
§ InVitek GmbH, Robert-Roessle-Strasse 10, D-13125
Berlin-Buch, Germany, ¶ Chugai Pharmaceuticals Co. Ltd., 135 Komakado, 1 Chome, Gotemba-Shi, Shizuoka 412, Japan, Celltech
Therapeutics Ltd., 216 Bath Road, Slough SL1 4EN, United Kingdom,
** British Biotech Pharmaceuticals Ltd., Watlington Road, Oxford OX4
5LY, United Kingdom, and INSERM U296,
Faculté de Médecine, Avenue du Général Sarrail,
94010 Créteil, France
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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