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The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin.

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Saus, J, Quinones, S, Otani, Y, Nagase, H, Harris, E D, Kurkinen, M·1988·Journal of Biological Chemistry

Abstract

We have determined the complete primary structure for human matrix metalloproteinase-3 (MMP-3), which has 477 residues including a 17-residue signal peptide. The result indicates that MMP-3 is identical with stromelysin (Whitham, S. E., Murphy, G., Angel, P., Rahmsdorf, H.-J., Smith, B. J., Lyons, A., Harris, T. J. R., Reynolds, J. J., Herrlich, P., and Docherty, A. J. P. (1986) Biochem. J. 240, 913-916). A striking result is that MMP-3 and collagenase are 54% identical in sequence, suggesting a common origin for the evolution of the two proteinases. We also show that in human synovial fibroblast cultures human recombinant interleukin-1 beta rapidly induces high levels of MMP-3 mRNA and, conversely, that retinoic acid or dexamethasone can suppress the MMP-3 mRNA levels. Similar results were obtained for human synovial collagenase mRNA. The data suggest that MMP-3 and collagenase expression are coordinately modulated in synovial fibroblast cultures.

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Metadata

Authors
Saus, J., Quinones, S., Otani, Y., Nagase, H., Harris, E. D., & Kurkinen, M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1988-05
Volume
263
Issue
14
Pages
6742-6745
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1491598928
Cited by
223
References
0
FWCI
14.86
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin. https://app.cochat.ai/papers/10.1016/s0021-9258(18)68705-8
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Saus, J., Quinones, S., Otani, Y., Nagase, H., Harris, E. D., & Kurkinen, M. (1988). The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysin. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)68705-8

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