Disease relevance of Mmp13

• Collagenase-3 (matrix metalloproteinase-13) is expressed by osteoblasts and seems to be involved in osteoclastic bone resorption [1].
• Histopathologic fibrosis scores, tissue hydroxyproline, TIMP-1 and MMP-13 levels were determined [2].
• Enhanced interstitial collagenase (matrix metalloproteinase-13) production of Kupffer cell by gadolinium chloride prevents pig serum-induced rat liver fibrosis [3].
• RESULTS: During gastric ulcer healing, MMP-2, MMP-3, and MMP-13 RNA expression was increased in stromal cells of the gastric mucosa bordering the ulcer, suggesting a prevalent role of non-epithelial cells in pericellular proteolysis [4].
• After 3 days of cerebral ischemia, the number of MMP-13 positive neurons in the periphery of the ischemic lesion increased compared to the respective area in the non-ischemic brain with a peak on day 7 [5].

High impact information on Mmp13

• ALN treatment reduced the local release of active TGF beta, possibly via inhibition of MMP-13 expression in articular cartilage and MMP-9 expression in subchondral bone [6].
• Injuring hepatocytes with galactosamine further increased matrix metalloproteinase-13 mRNA production [7].
• Those with myofibroblastic phenotypes produce more type I collagen whereas those resembling freshly isolated hepatic stellate cells express matrix metalloproteinase-13 [7].
• Studies performed with various hepatic stellate cell lines revealed that they are heterogeneous regarding expression of matrix metalloproteinase-13 [7].
• Serotonin-induced MMP-13 production is mediated via phospholipase C, protein kinase C, and ERK1/2 in rat uterine smooth muscle cells [8].

Chemical compound and disease context of Mmp13

• Our results suggest that MMP-13 plays an important role in estrogen deficiency-induced bone loss, while estrogen can inhibit bone resorption and reduce bone turnover rate by down-regulating the expression of MMP-13 in osteoblastic cells [9].
• CONCLUSION: MMP-13 participates in the degradation of newly-formed matrix in the early phase of rat liver fibrosis induced by ethanol, and it was induced in a distinct time frame [10].
• The aim of this study was to investigate whether matrix metalloproteinases (MMP-13, 9) of Kupffer cells induced by gadolinium chloride (GdCl(3)) treatment can reverse dimethylnitrosamine (DMN)-induced liver fibrosis (in vivo) and the effect of GdCl(3) on MAP kinase activity (in vitro) [11].

Biological context of Mmp13

• The MMP-13 mRNA up-regulation was significantly suppressed by genistein, herbimycin A and 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine [12].
• Osteoblasts obtained from calvariae of newborn JunAA mice, defective in phosphorylation of c-Jun, or newborn c-Fos knockout (Fos -/- ) mice, showed much less induction of MMP-13 with the addition of MIF than osteoblasts obtained from wild-type or littermate control mice [12].
• Serotonin (5-hydroxytryptamine; 5-HT), acting via the 5-HT(2A) receptor, up-regulates the transcription and production of interstitial collagenase (matrix metalloproteinase-13; MMP-13), a critical enzyme responsible for maintaining the integrity of the uterus, after parturition [8].
• We conclude that IL-6 increases interstitial MMP-13 gene expression at the promoter level [13].
• These effects were exerted by acting on the AP1-binding site of the MMP-13 promoter, as shown by transfecting cells with reporter plasmids containing mutations in this element [13].

Anatomical context of Mmp13

• CONCLUSIONS: MMP-14 and MMP-13 expression in rat corneas parallels that of gelatinases A and B, respectively [14].
• MMP-13 mRNA was localized exclusively to basal cells of the epithelium at the wounded area from 6 hours to 3 days after wounding [14].
• In the growth plate erosion zone, perivascular cells showed MMP-13 reactivity [15].
• These findings suggest that MMP-13 synthesized and secreted by osteoblast-lineage cells is localized under the ruffled borders of osteoclasts [15].
• Immunolocalization of matrix metalloproteinase-13 on bone surface under osteoclasts in rat tibia [15].

Associations of Mmp13 with chemical compounds

• The phospholipase C (PLC) inhibitors and D609 attenuated serotonin-mediated-IP turnover with a corresponding inhibition of MMP-13 protein production [8].
• The PKC-specific inhibitors bisindolylmaleimide I, calphostin C, CGP 41251, and the PKCdelta-selective inhibitor rottlerin were able to suppress serotonin up-regulation of MMP-13 [8].
• Pirfenidone at a dosage of 50 mg x kg(-1) x d(-1) inhibited protein expression of TGF-beta1 and TIMP-1 in lung tissue in the early phase (0.79 and 0.75 times of control group), but had no effect on expression of MMP-13 [16].
• However, the regulating action of estrogen on the expression of interstitial collagenases MMP-8 and MMP-13 in osteoblastic cells in vivo remains unclear [9].
• In this study, we investigated the effects of alendronate at concentrations of 1-100 microM on the synthesis of collagenase 3 or matrix metalloproteinase 13 (MMP-13) and tissue inhibitors of MMPs (TIMPs) 1, 2, and 3 in primary Ob-enriched cells from 22-day-old fetal rat calvariae [17].

Regulatory relationships of Mmp13

• Using primary rat calvarial osteoblastic cells obtained from 21-day old neonatal rats, we determined MMP-13 gene expression when stimulated by parathyroid hormone (PTH), interleukin (IL)-1b, or tumour necrosis factor (TNF)-alpha in the presence or absence of CMT-8 or -5 [18].

Other interactions of Mmp13

• RESULTS: MMP-13 mRNA was detected in epithelial cells of wounded corneas, but not in normal controls; MMP-14 was found in both normal and wounded corneas [14].
• MMP-13 in perivascular cells may be involved in removal of cartilage matrix proteins such as type II collagen and aggrecan [15].
• RESULTS: Zymography revealed that PSCs secrete a number of MMPs including proteinases with molecular weights consistent with MMP2, MMP9, and MMP13 [19].
• The mechanoresponsiveness was assessed by examining the expression of inducible nitric oxide synthase (iNOS), tumor necrosis factor-alpha (TNF-alpha), and matrix metalloproteinase-13 mRNA expression [20].
• Pioglitazone reduced the expression of TIMP-1 and TIMP-2 mRNA without changing MMP-13 mRNA expression compared to the liver fed a CDAA diet alone [21].

Analytical, diagnostic and therapeutic context of Mmp13

• Expression of proteins of TGF-beta 1, TIMP-1, and MMP-13 were detected by Western blotting [16].
• In situ hybridization was performed to localize the mRNA expression of MMP-14 and MMP-13 [14].
• Using immunohistochemistry and Western blotting, we investigated localization of MMP-13 in rat tibia, to clarify the role of MMP-13 in bone resorption [15].
• Immunoelectron microscopy revealed that MMP-13 was localized on the bone surfaces, under the ruffled borders and some clear zones of osteoclasts [15].
• RT-PCR for the decalcified paraffin sections indicated expression of MMP-8 and MMP-13 in the periodontal tissues [22].

References