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Volume 271, Number 45, Issue of November 8, 1996 pp. 28509-28515
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Different Collagenase Gene Products Have Different Roles in Degradation of Type I Collagen

(Received for publication, May 25, 1996, and in revised form, August 19, 1996)

Stephen M. Krane , Michael H. Byrne , Vincent Lemaître ^¶ , Patrick Henriet ^¶ , John J. Jeffrey ^** , James P. Witter , Xin Liu ^§§ , Hong Wu ^§§ , Rudolf Jaenisch ^§§ and Yves Eeckhout ^¶

From the  Department of Medicine, Harvard Medical School and the Arthritis Unit, Massachusetts General Hospital, Boston, Massachusetts 02114, the ^¶ Connective Tissue Group, University of Louvain and International Institute of Cellular and Molecular Pathology, Avenue Hippocrate, 75, B-1200 Bruxelles, Belgium, the ^** Division of Hematology, Department of Medicine, Albany Medical College, Albany, New York 12208, and the ^§§ Whitehead Institute for Biomedical Research and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02142

Vertebrate collagenases, matrix metalloproteinases (MMPs), cleave type I collagen at a single helical locus. We show here that rodent interstitial collagenases (MMP-13), but not human fibroblast collagenase (MMP-1), cleave type I collagen at an additional aminotelopeptide locus. Collagenase cDNAs and chimeric constructs in pET-3d, juxtaposing MMP-13 sequences amino-terminal to the active site in the catalytic domain and MMP-1 sequences carboxyl-terminal and vice versa, were expressed in Escherichia coli. Assays utilized collagen from wild type (+/+) mice or mice that carry a targeted mutation (r/r) that encodes substitutions in 1(I) chains that prevent collagenase cleavage at the helical locus. MMP-13 and chimeric molecules that contained the MMP-13 sequences amino-terminal to the active site cleaved (+/+) collagen at the helical locus and cleaved cross-linked (r/r) collagen in the aminotelopeptide ( components converted to chains). Human MMP-1 and chimeric MMP-1/MMP-13 with MMP-1 sequences amino-terminal to the active site cleaved collagen at the helical locus but not in the aminotelopeptide. All activities were inhibited by TIMP-1, 1,10-phenanthroline, and EDTA. Sequences in the distal two-thirds of the catalytic domain determine the aminotelopeptide-degrading capacity of MMP-13.

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