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Vol. 273, Issue 2, 1216-1222, January 9, 1998
From the It has been proposed that tissue inhibitor of
metalloproteinase-2 (TIMP-2), in stoichiometric concentrations, serves
as an intermediate in progelatinase A activation by binding to
activated membrane type 1-matrix metalloproteinase 1 (MT1-MMP) on the
plasma membrane. An MT1-MMP-independent cell surface receptor for
TIMP-2 has also been postulated. To clarify TIMP-2 binding, we have
performed 125I-TIMP-2 binding studies on transfected
COS-1 cells and endothelial cells. Specific receptors for TIMP-2 were
identified on COS-1 cells transfected with MT1-MMP cDNA, but not on
vector-transfected cells. Treatment of MT1-MMP transfected COS-1 cells
with a hydroxamic acid inhibitor of MMPs, CT-1746, but not an inactive
stereoisomer, CT-1915, produced dose-dependent inhibition
of specific TIMP-2 binding comparable with that noted with excess
unlabeled TIMP-2. This result suggests that TIMP-2 binds to the zinc
catalytic site of MT1-MMP. As demonstrated by the limited competition
for binding of C-terminal deleted TIMP-2, the C-terminal domain of
TIMP-2 participates in binding to MT1-MMP. Cross-linking studies
followed by immunoprecipitation using antibodies to MT1-MMP were
employed to identify 125I-TIMP-2·MT1-MMP complexes in
MT1-MMP-transfected COS-1 cell membrane extracts. TIMP-2 receptors were
also identified on concanavalin A-treated human umbilical vein
endothelial cells; inhibition of TIMP-2 binding with CT-1746 was
demonstrated.
Tissue Inhibitor of Metalloproteinase-2 (TIMP-2) Binds to the
Catalytic Domain of the Cell Surface Receptor, Membrane Type
1-Matrix Metalloproteinase 1 (MT1-MMP)
§,,,§,
,, and Departments of Medicine and Research,
Department of Veterans Affairs Medical Center, Northport, New York
11768, the § State University of New York, Stony Brook, New
York 11794, the Division of Hematology-Oncology, Department of
Pediatrics, Childrens Hospital, Los Angeles, and the Department of
Biochemistry and Molecular Biology, University of Southern California,
Los Angeles, California 90027, ** Amgen, Inc., Thousand Oaks, California
91320, and CellTech Ltd., SL1-4EN
Slough, Great Britain
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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