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Originally published In Press as doi:10.1074/jbc.M001920200 on July 10, 2000

J. Biol. Chem., Vol. 275, Issue 38, 29648-29653, September 22, 2000
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The Propeptide Domain of Membrane Type 1-Matrix Metalloproteinase Acts as an Intramolecular Chaperone when Expressed in trans with the Mature Sequence in COS-1 Cells*

Jian CaoDagger , Michelle Hymowitz§, Cathleen Conner§, Wadie F. BahouDagger , and Stanley ZuckerDagger §

From the Dagger  Department of Medicine, State University of New York at Stony Brook, Stony Brook, New York 11794 and § Department of Veterans Affairs Medical Center, Northport, New York 11768

It has been assumed that cleavage of the N-terminal propeptide domain of membrane type-1 matrix metalloproteinase (MT1-MMP) is required for enzyme function. We recently demonstrated that the propeptide domain of MT1-MMP is not cleaved and actually is required for function of the membrane-bound enzyme in transfected COS-1 cells (Cao, J., Drews, M., Lee, H. M., Conner, C., Bahou, W. F., and Zucker, S. (1998) J. Biol. Chem. 273, 34745-34752). In this report, we have inserted the cDNA encoding the signal and propeptide sequences of MT1-MMP (MT1-109) and the cDNA encoding propeptide-deleted mature MT1-MMP (MTDelta pro) in expression vectors that were then transfected into matrix metalloproteinase-deficient COS-1 cells. Co-expression of both the mature sequence and the prosequence of MT1-MMP as independent polypeptides (in trans) in COS-1 cells resulted in reconstitution of MT1-MMP function in terms of facilitating 125I-labeled tissue inhibitor of metalloproteinase 2 binding to transfected cells and subsequent activation of progelatinase A. Transfection of cells with either cDNA alone resulted in non-functional cells. These results are consistent with the propeptide sequence of MT1-MMP functioning as an intramolecular chaperone involved in protein folding and trafficking to the cell surface.

* This research was supported by a Merit Review grant and a Research Enhancement Award Program (REAP) from the Department of Veterans Affairs (to S. Z.), National Institutes of Health Grants HL-02431 and HL-49149 (to W. F. B.), a research grant (to W. F. B.) from the American Heart Association, and a post-doctoral fellowship (to J. C.) from the U. S. Army Medical Research and Materiel Command.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 and reprint requests should be addressed: Mail Code 151, VA Medical Center, Northport, NY 11768. Tel.: 631-261-4400 (ext. 2861); Fax: 631-544-5317; E-mail: s_zucker@yahoo.com.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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