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

• The elevation of MMP-3 following cell death was consistently found in the superficial zone of loaded cartilage [2].
• Production of MMP-3 was only decreased by tetracycline (IC50 = 45.4 microM) [7].

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

• The protein synthesis of TIMP-1 and MMP-3 was determined by immunoprecipitation, PAI-1 protein was quantitated by ELISA [12].
• RESULTS: Upregulated MMP-3, MMP-13, and Agg-1 transcripts at 24 hours were repressed by the GLN and CS combination by at least approximately 6-fold [13].

Analytical, diagnostic and therapeutic context of MMP3

• The protein synthesis of TIMP-1 and MMP-3 was determined by immunoprecipitation [14].

References