Different collagenase gene products have different roles in degradation of type I collagen
(1996) Journal of Biological Chemistry — Vol. 271, n° 45, p. 28509-28515 (1996)
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- Abstract
- 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 aminoitelopeptide 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 alpha 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 (beta components converted to ct chains), Human MMP-1 and chimeric MMP-1/MMP-13 with MMP-1 sequences aminoterminal 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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Krane, SM., Byrne, MH., Henriet, P., Jeffrey, JJ., Witter, JP., Liu, X., Wu, H., Jaenisch, R., Eeckhout, Y., & Lemaitre, V. (1996). Different collagenase gene products have different roles in degradation of type I collagen. Journal of Biological Chemistry, 271(45), 28509-28515. https://doi.org/10.1074/jbc.271.45.28509 (Original work published 1996)