Disease relevance of MMP3

• This MMP-3 increase appears to play a key role in the efficacy of this treatment for open-angle glaucoma [1].

High impact information on MMP3

• CONCLUSIONS: JNK activity is necessary for the induction of MMP-3 and MMP-9 by TNFalpha, IL-1alpha, or IL-1beta in TM cells [1].
• PURPOSE: The cytokines TNF and IL-1 mediate the MMP-3 increase that occurs in response to trabecular meshwork (TM) treatment by laser trabeculoplasty [1].
• Phosphorylation of components of the JNK signaling pathway and of the transcription factors c-Jun and ATF-2 support a role for this pathway in the induction of MMP-3 and MMP-9 in the TM in response to these cytokines [1].
• The Fn-f 45-induced increase in MMP-3 and MMP-13 synthesis occurred via an interleukin 1-independent mechanism, since the receptor antagonist of interleukin-1 was unable to block the increased synthesis [2].
• Fn-f 45 also stimulated the synthesis of MMP-3 (stromelysin-1) from cultured chondrocytes and cartilage cultures [2].

Biological context of MMP3

• In contrast, the outer meniscus was found to contain higher gene expression for proteins associated with fibrous tissues including type I collagen, and the proteases MMP2 and MMP3 [3].
• The resultant 8-hour-conditioned culture medium was then tested for factor activity by evaluating its ability to produce two typical trabecular responses to laser treatment, that is, to induce stromelysin expression or to trigger cell division, when applied to fresh organ cultures or to cell cultures [4].
• The relative resistance of nonhuman link protein to stromelysin may in part be due to a unique amino acid substitution present near the enzymic cleave site [5].
• CONCLUSION: Because MMP-3 (stromelysin) mRNA showed the highest upregulation, our findings suggest that trabecular cells preferentially degrade and turn over the proteoglycan components of the extracellular matrix in response to short-term exposure to increased hydrostatic pressure with and without Dex as a homeostatic mechanism [6].

Anatomical context of MMP3

• In contrast EGF (epidermal growth factor), which stimulates collagenase and/or stromelysin synthesis in fibroblast systems, stimulated minimal amounts of these enzymes at both the message and protein levels [7].
• Stretching stationary organ cultures or stretching TM cells grown on membranes resulted in similar increases in gelatinase A without changes in gelatinase B or stromelysin levels [8].
• Upon resumption of feed intake by the fourth d postweaning, villus height and crypt depth, CD8(+) T cell numbers, MHC class I RNA expression and local expression of stromelysin returned to Day 0 values [9].
• Trabecular cell expression of fibronectin and MMP-3 is modulated by aqueous humor growth factors [10].
• On digestion of human proteoglycan aggregate with stromelysin, rapid modification of the link protein components occurred, whereas the aggregates from nonhuman cartilages showed incomplete cleavage of their link protein components [5].

Associations of MMP3 with chemical compounds

• The digestion of proteoglycan aggregate (6 mg/ml) by stromelysin was unaffected by the addition of a high concentration of extra chondroitin sulphate chains (14 mg/ml), and the digestion of proteoglycan monomer showed that the G1 domain was resistant to stromelysin digestion even when not bound to hyaluronan and link protein [11].
• Tumor necrosis factor alpha and epidermal growth factor regulation of collagenase and stromelysin in adult porcine articular chondrocytes [7].
• Bradykinin treatment induced MMP-3 and MMP-20 gene expression to an extreme degree [12].
• Bafilomycin A1 inhibits IL-1-stimulated proteoglycan degradation by chondrocytes without affecting stromelysin synthesis [13].
• The immunoreactivity for matrix metalloproteinase-3 (MMP-3) increased in cholesterol-fed coronary arteries, predominantly in the neointima [14].

Regulatory relationships of MMP3

• Nuclear run-on transcription analysis demonstrated that the TNF alpha-stimulated increase in stromelysin and collagenase message levels was, at least partially, due to increased transcription [7].

Other interactions of MMP3

• After 1 month, the specimens were rapidly thawed (37 degrees C) and processed for biomechanical, ultrastructural, morphological and immunohistochemical (MMP-1, MMP-2, MMP-3 and MMP-9) analysis [15].
• We investigated the mRNA and protein expression of fibronectin and stromelysin-1 (matrix metalloproteinase-3, MMP-3) by trabecular cells treated with growth factors present in primary and secondary aqueous humors [10].
• Acidic and basic FGF, IL-1 beta, TGF beta and PDGF AB produce similar but smaller effects, while HGF, VEGF, EGF, KGF, and LIF produce small to moderate elevations in stromelysin with minimal other responses [16].
• The immunoreactivity for matrix metalloproteinase-3 (MMP-3) increased in cholesterol-fed coronary arteries, predominantly in the neointima and adventitia [17].
• RESULTS: The most significant changes were detected in the levels of MMP-3 mRNA in control cells (2.4-fold increase), of TIMP-1 and -2 mRNA in cells treated with Il-1beta (2.6-fold increase) and of MMP-3 mRNA in cells treated with Dex (3.5-fold increase) exposed to 50 mmHg pressure [6].

Analytical, diagnostic and therapeutic context of MMP3

• Changes in MMP-3 and MMP-9 protein levels in the media were then determined by Western immunoblot [1].
• Medium conditioned for 8 hours, but not for 30 minutes, induced typical increases in stromelysin expression in these organ cultures and in cell cultures [4].
• Western immunoblots, zymography, and confocal immunohistochemistry were used to evaluate changes in MMPs and their tissue inhibitors, the TIMPS: RESULTS: Doubling the flow rate in perfused human organ cultures increased gelatinase A levels in the perfusate by 30% to 50% without affecting gelatinase B or stromelysin levels [8].
• Accordingly, the relative abundance of specific MMPs (MMP-1, MMP-2, and MMP-3) was examined by immunoblotting [18].

References