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J Biol Chem, Vol. 273, Issue 52, 34745-34752, December 25, 1998
,, and§
From the Departments of Activation of secreted latent matrix
metalloproteinases (MMPs) is accompanied by cleavage of the N-terminal
propeptide, thereby liberating the active zinc from binding to the
conserved cysteine in the pro-domain. It has been assumed that an
analogous mechanism is responsible for the activation of membrane type
1 MMP (MT1-MMP). Using recombinant wild-type MT1-MMP cDNA and
mutant cDNAs transfected into COS-1 cells lacking endogenous
MT1-MMP, we have examined the function of the propeptide domain of
MT1-MMP. MT1-MMP was characterized by immunoblotting, surface
biotinylation, gelatin substrate zymography, and
125I-tissue inhibitor of metalloproteinases 2 (TIMP-2) binding. In contrast to wild-type MT1-MMP-transfected COS-1
cells, transfected COS-1 cells containing a deletion of the N-terminal
propeptide domain of MT1-MMP or a chimeric construction (substitution
of the pro-domain of MT1-MMP with that of collagenase 3) were
functionally inactive in terms of binding of 125I-labeled
TIMP-2 to the cell surface and initiating the activation of
pro-gelatinase A. These results support the concept that in its native plasma membrane-inserted form, the pro-domain of MT1-MMP plays an essential role in TIMP-2 binding and subsequent activation of
pro-gelatinase A.
Medicine and ¶ Oral
Biology, Schools of Medicine and Dentistry, State University of New
York, Stony Brook, New York 11794 and § Department of
Veterans Affairs Medical Center, Northport, New York 11768
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