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Gene Review

MMP3  -  matrix metallopeptidase 3 (stromelysin 1,...

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Disease relevance of MMP3

  • Matrix metalloprotease 1 (MMP-1) and MMP-3 mRNA were increased by IL-1beta in normoxia and hypoxia, whereas only MMP-3 mRNA was enhanced in reoxygenated cultures [1].
  • Since MMP-3 can degrade PG and super-activate procollagenase, the increase of MMP-3 can therefore induce matrix degradation and PG depletion in mechanically injured articular cartilage, both of which are important to the development of osteoarthritis [2].

High impact information on MMP3

  • RT-PCR analysis showed that the expression levels of MMP-3, type II collagen, and COMP messenger RNA, which are tightly associated with the activation of RAR, RXR, or Sp-1, were up-regulated by treatment with HA(6) [3].
  • Matrix molecules showed little change in expression after injurious compression, whereas MMP-3 increased approximately 250-fold, ADAMTS-5 increased approximately 40-fold, and tissue inhibitor of metalloproteinases 1 increased approximately 12-fold above the levels in free swelling cultures [4].
  • Furthermore, the matrix metalloproteases MMP-1, MMP-3, and MMP-13, could be easily detected in pressure-treated disks by immunohistochemistry whereas staining in controls was low or undetectable [5].
  • RESULTS: MSU induced MMP-3 and iNOS expression and NO release in chondrocytes in a p38-dependent manner that did not require interleukin-1 (IL-1), as demonstrated by using IL-1 receptor antagonist [6].
  • But, despite the observed FAK phosphorylation, a selective pharmacologic FAK inhibitor and a FAK dominant-negative mutant both failed to block MSU-induced NO release or MMP-3 expression in parallel experiments [6].

Biological context of MMP3


Anatomical context of MMP3

  • HA(oligos) treatment of TMJ chondrocytes resulted in enhanced MMP-3 expression, whereas wash-out of the HA(oligos) in the middle of the experimental period reduced this induction [8].
  • OBJECTIVE: To determine whether load-induced injury causes alterations in proteoglycan (PG), stromelysin-1 (MMP-3) and collagen in articular cartilage [2].
  • Stromelysin (MMP-3) is a connective tissue matrix-degrading enzyme [9].

Associations of MMP3 with chemical compounds

  • X-ray crystallography data obtained for MMP-3 cocrystallized with 20 gave detailed information on key binding interactions defining an overall scaffold geometry for piperazine-based MMP inhibitors [10].
  • Sequencing of activation intermediates demonstrated cleavage on the NH2-terminal side of certain basic residues in the MMP-3 propeptide [11].

Other interactions of MMP3


Analytical, diagnostic and therapeutic context of MMP3


  1. Effect of hypoxia and reoxygenation on gene expression and response to interleukin-1 in cultured articular chondrocytes. Martin, G., Andriamanalijaona, R., Grässel, S., Dreier, R., Mathy-Hartert, M., Bogdanowicz, P., Boumédiene, K., Henrotin, Y., Bruckner, P., Pujol, J.P. Arthritis Rheum. (2004) [Pubmed]
  2. Increased stromelysin-1 (MMP-3), proteoglycan degradation (3B3- and 7D4) and collagen damage in cyclically load-injured articular cartilage. Lin, P.M., Chen, C.T., Torzilli, P.A. Osteoarthr. Cartil. (2004) [Pubmed]
  3. Hyaluronan oligosaccharide-induced activation of transcription factors in bovine articular chondrocytes. Ohno, S., Im, H.J., Knudson, C.B., Knudson, W. Arthritis Rheum. (2005) [Pubmed]
  4. Mechanical injury of cartilage explants causes specific time-dependent changes in chondrocyte gene expression. Lee, J.H., Fitzgerald, J.B., Dimicco, M.A., Grodzinsky, A.J. Arthritis Rheum. (2005) [Pubmed]
  5. Mechanical overload induces VEGF in cartilage discs via hypoxia-inducible factor. Pufe, T., Lemke, A., Kurz, B., Petersen, W., Tillmann, B., Grodzinsky, A.J., Mentlein, R. Am. J. Pathol. (2004) [Pubmed]
  6. Proline-rich tyrosine kinase 2 and Src kinase signaling transduce monosodium urate crystal-induced nitric oxide production and matrix metalloproteinase 3 expression in chondrocytes. Liu, R., Lioté, F., Rose, D.M., Merz, D., Terkeltaub, R. Arthritis Rheum. (2004) [Pubmed]
  7. Effects of tetracyclines on the production of matrix metalloproteinases and plasminogen activators as well as of their natural inhibitors, tissue inhibitor of metalloproteinases-1 and plasminogen activator inhibitor-1. Sadowski, T., Steinmeyer, J. Inflamm. Res. (2001) [Pubmed]
  8. Induction of MMP-3 by hyaluronan oligosaccharides in temporomandibular joint chondrocytes. Ohno, S., Ohno-Nakahara, M., Knudson, C.B., Knudson, W. J. Dent. Res. (2005) [Pubmed]
  9. Identification of the metalloproteinase stromelysin in the physis. Armstrong, A.L., Barrach, H.J., Ehrlich, M.G. J. Orthop. Res. (2002) [Pubmed]
  10. Design and synthesis of piperazine-based matrix metalloproteinase inhibitors. Cheng, M., De, B., Pikul, S., Almstead, N.G., Natchus, M.G., Anastasio, M.V., McPhail, S.J., Snider, C.E., Taiwo, Y.O., Chen, L., Dunaway, C.M., Gu, F., Dowty, M.E., Mieling, G.E., Janusz, M.J., Wang-Weigand, S. J. Med. Chem. (2000) [Pubmed]
  11. A matrix metalloproteinase proenzyme activator produced by articular cartilage. Towle, C.A., Wright, M., Hecht, A.C., Kuong, S.J., Papanicolas, L.E., Totkovic, R., Mankin, H.J., Treadwell, B.V. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  12. Effects of polysulfated glycosaminoglycan and triamcinolone acetonid on the production of proteinases and their inhibitors by IL-1alpha treated articular chondrocytes. Sadowski, T., Steinmeyer, J. Biochem. Pharmacol. (2002) [Pubmed]
  13. Effect of glucosamine and chondroitin sulfate on regulation of gene expression of proteolytic enzymes and their inhibitors in interleukin-1-challenged bovine articular cartilage explants. Chan, P.S., Caron, J.P., Orth, M.W. Am. J. Vet. Res. (2005) [Pubmed]
  14. Effects of non-steroidal antiinflammatory drugs and dexamethasone on the activity and expression of matrix metalloproteinase-1, matrix metalloproteinase-3 and tissue inhibitor of metalloproteinases-1 by bovine articular chondrocytes. Sadowski, T., Steinmeyer, J. Osteoarthr. Cartil. (2001) [Pubmed]
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