Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.17 (MMP-3)
 3,419 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Progelatinase A was purified as a complex with TIMP-2 from the conditioned medium of a human glioblastoma cell line. The TIMP-2/progelatinase complex was resistant to the activation by p-aminophenylmercuric acetic acid (APMA), and showed less than 10% of the activity of the TIMP-2-free active enzyme. When the complex was incubated with stromelysin in the presence of APMA, the 64-kDa progelatinase was effectively converted to the 57-kDa mature enzyme, increasing its gelatinolytic activity about 8-fold. These results suggest that stromelysin is a natural activator of TIMP-2-bound progelatinase A.
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PMID:Activation of TIMP-2/progelatinase A complex by stromelysin. 132 Aug 76

To clarify the destruction of connective tissue in ulcerated regions, collagenase and gelatinolytic activities in homogenates of rat acetic acid-induced ulcers were examined. Gelatinolytic activity in the ulcerated regions was significantly higher than that in normal tissues. Collagenase, however, was not detectable. Gelatin-gel-electrophoresis showed that the gelatinolytic activity was due to several species, some of which crossreacted with a sheep anti-(rabbit prostromelysin) antibody. The H2-blocker, famotidine, significantly depressed the gelatinolytic activity in the ulcerated regions. Thus, both stromelysin and gelatinolytic enzymes may play important roles in the degradation of the basement membrane, especially type IV collagen.
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PMID:Characterization of metalloproteinases in rat gastric tissues with acetic acid-induced ulcers. 259 86

Samples containing predentin and mineralized dentin involving the mineralized front (newly formed dentin) were prepared by scraping developing porcine teeth after odontoblastic cell debris had been removed from the predentin surfaces. An extract was obtained separately from the matrices of predentin and of the newly formed dentin with a 4 M guanidine solution before and after demineralization with acetic acid solution. Enzymography detected 56 and 61 kDa gelatinases and 25 kDa proteoglycanase as neutral metalloproteinases in both extracts and proved them to be in an active form. Approximately half of the 56 and 61 kDa gelatinases binds to collagen fibers in predentin matrix. Three high molecular weight proteoglycans (70-85 kDa, 130-180 kDa, and 290 kDa) were found in the predentin matrix, but not in the newly formed dentin. The proteoglycanases in predentin degraded 290 kDa proteoglycan, if incubated together with calcium (Ca) ions. The results of this investigation indicate that active proteoglycanases which existed in the predentin perform no substantial work in proteoglycan degradation because the Ca ions are masked in the predentin matrix by coexisting proteoglycans. When mineralization occurs, however, they can degrade the proteoglycan at the mineralization front because excess Ca ions may be supplied via odontoblastic processes.
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PMID:Action of metalloproteinases on porcine dentin mineralization. 789 81

The human osteosarcoma cell culture HOS does not produce matrix metalloproteinases (MPs). However, after transformation with the Ki-ras oncogene, the resulting culture (KHOS) produced readily detectable MPs. The molecular weight of the major MP was 66 kDa, while the molecular weights of two other minor bands were 71 kDa and 60 kDa. The activity of all three enzymes was inactivated by treatment with ethylene diaminetetra acetic acid, indicating that they are probably MPs. The substrate preference of the 66-kDa MP (in decreasing order) was gelatin and collagens V, I, III, and IV. Treatment of the MPs with p-aminophenylmercuric acetate led to the appearance of 62-kDa activated enzyme. The MP produced by KHOS cells did not react with the monoclonal anti-rat stromelysin antibody MC. Treatment of KHOS cells with retinoic acid and dexamethasone, which are known to suppress c-fos/c-jun and AP-1, suppressed the production of the MPs. Therefore, the activation of MPs by Ki-ras in KHOS cells may involve c-fos/c-jun and the AP-1-responsive pathway.
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PMID:Activated production of metalloproteinases in Ki-ras-transformed human osteosarcoma cells. 815 1

Nutritional factors and resident bacteria participate in the pathogenesis of intestinal inflammation. However, the ways in which bacteria and complex diets might modulate matrix metalloproteinase (MMP) production are unknown. We hypothesized that butyrate might enhance production of MMPs, thus amplifying their response to signals in inflammatory conditions. Human mesenchymal cells were incubated with butyrate and then stimulated with cytokines. MMPs and inhibitors were studied by Western blotting and quantitative RT-PCR. Acetylation of histones was examined in Triton X acetic acid-urea gels by PAGE. We showed that butyrate selectively enhanced the protein production and mRNA expression of stromelysin-1 in tumor necrosis factor-alpha- or interleukin-1beta-stimulated mesenchymal cells. Butyrate alone did not induce any change in MMP production or mRNA expression. It increased the acetylation of histones in mesenchymal cells. Furthermore, acetylation of histones (induced by trichostatin A) reproduced the effects of butyrate. Although butyrate is a major source of nutrient for the colonic epithelial cells, it modulates intestinal inflammation through the secretion of stromelysin-1 in stimulated stromal cells via the inhibition of histone deacetylase.
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PMID:Butyrate upregulates stromelysin-1 production by intestinal mesenchymal cells. 1105 88