No abstract available.
Matrix Metalloproteinase 9

OBJECTIVEThis study aimed to investigate the difference in salivary protease expression in patients with chronic periodontitis and normal individuals.

METHODSThe stimulating saliva in patients with chronic periodontitis and normal individuals were collected. Protein chip technology was adapted to analyze salivary protease spectrum.

RESULTSAmong the 34 proteases in the chip, disintegrin and metalloproteinase (ADAM)8, matrix metalloproteinase (MMP)-8, MMP-12, neprilysin/CD10, and uridylyl phosphate adenosine/urokinase showed a significantly increased concentration in the saliva of chronic periodontitis patients compared with those in the saliva of normal individuals (P<0.01). By contrast, the concentrations of ADAM9, a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)1, ADAMTS13, cathepsin B, E, L, V, X/Z/P, kallikrein 6, 7, 11, 13, MMP-9, proteinase 3, presenilin-1, and proprotein convertase 9 sharply decreased (P<0.05).

CONCLUSIONSThe results demonstrated that protease spectrum in the saliva of chronic periodontitis patients and normal individuals significantly differed. Analysis of salivary protease spectrum is a potential clinical method to examine, diagnose, and monitor chronic periodontitis.

BACKGROUND/AIMS: Matrix metalloproteinases (MMP)-2 and -9 can degrade essential components of vascular integrity. The aim of this study was to investigate the association between those MMPs and variceal bleeding (VB). METHODS: Fifteen controls, 12 patients with acute ulcer bleeding (UB) group, 37 patients with varix (V group), and 35 patients with acute VB group were enrolled. Serum was obtained to measure MMP-2 and -9 activity by zymogram protease assays. RESULTS: The activity levels of these compounds were compared with the controls' median value. The median MMP-9 activity was 1.0 in controls, 1.05 in the UB group, 0.43 in the V group, and 0.96 in the VB group. The level of MMP-9 activity was higher in the VB group than in the V group (p<0.001). In the VB group, there was a signifi cant decrease in MMP-9 activity over time after bleeding (p<0.001). The median MMP-2 activity level was 1.0 in controls, 1.01 in the UB group, 1.50 in the V group, and 1.55 in the VB group. The level of MMP-2 activity was similar in the VB and V groups. CONCLUSIONS: The level of MMP-9 activity increased in association with VB. The role of MMP-9 in the pathogenesis of VB should be verified.
Esophageal and Gastric Varices ; Hemorrhage ; Humans ; Matrix Metalloproteinase 2 ; Matrix Metalloproteinase 9 ; Matrix Metalloproteinases ; Ulcer ; Varicose Veins

OBJECTIVETo investigate the mRNA and protein expression of axin inhibitor (AXIN), β-chain protein (β-catenin), matrix metalloproteinase-7 (MMP-7) and matrix metalloproteinase-9 (MMP-9), and their relationship in lymphoma cells.

METHODSThe expressions of MMP-7, MMP-9, β-catenin and AXIN in lymphoma cell lines were detected by Western blot and RT-PCR. Moreover, the lymphoma cells with relatively low expression of AXIN were grouped and were transiently transfected by using pcDNA5-His-β-catenin and pCMV5-HA-AXIN; the protein and mRNA expression of MMP-7, MMP-9 and β-catenin in lymphoma cells was detected by Western blot and RT-PCR, respectively; the cell infiltration and migration ability in group with stable ligh expression of AXIN, group of interfering stable high expression of AXIN and blank control group were analyzed by transwell experiment.

RESULTSThe AXIN negatively correlated with MMP-7, MMP-9 and β-catenin expression in lymphoma cell lines. After the up-regulation of AXIN, the mRNA expression of MMP7, MMP-9 and β-catenin in Raji cells all not significantly changed, while the pratein expression of MMP-7, MMP-9 and β-catenin all significantly decreased (P<0.05); after the up-regulation of β-catenin, the mRNA and protein expression of MMP-7, MMP-9 was also up-regulated significantly (P<0.05). After interfering the AXIN, the mRNA expression of MMP-7, MMP-9 and β-catenin in group with stable high expression of AXIN all not changed significantly, while protein expression of MMP-7, MMP-9 and β-catenin was down-regulated significantly (P<0.05); after interfering the β-catenin, the protein and mRNA expression of MMP-7 and MMP-9 in group with stable high expression of AXIN all were down-regulated significantly(P<0.05).

CONCLUSIONThe up-regulation of AXIN expression in lymphoma cells can lead to decrease of β-catenin expression and the resuts in significant decrease of MMP-7 and MMP-9 expression, there by plays a role to block the infiltration and migration of lymphoma cells.

BACKGROUND: Matrix metalloproteinase-9 (MMP-9) is a matrix-degrading enzyme that's believed to play a crucial role not only for tumor invasion and metastasis, but also for a variety of stromal reactions, including neovascularization. The aim of this study was to investigate the expression of MMP-9 and to compare its expression with the angiogenesis activity in human osteosarcoma. METHODS: Archival tumor tissue samples from 20 patients with osteosarcoma were analyzed by performing immunohistochemistry for the expression of MMP-9 and CD34. The vascularity was measured as the average microvascular density (MVD) of the CD34-positive vessels. The clinical information was obtained through searching the computerized retrospective database from the tumor registry. RESULTS: MMP-9 was expressed in 90% (18/20) of the tumors we examined. The MVD ranged from 10.5 to 179.7 with a mean of 64.9. There was no significant correlation between the MMP-9 expression and the MVD (p=.613). The MMP-9 expression was not associated with any of the clinicopathologic variables, whereas the MVD showed an increasing tendency according to the metastasis status (p=.073). CONCLUSIONS: We demonstrated that MMP-9 activation is likely to occur in human osteosarcoma. However, there was no direct involvement of MMP-9 with tumor angiogenesis. It is noteworthy that MVD may aid physicians to predict the presence of distant metastasis in osteosarcoma patients.
Humans* ; Immunohistochemistry ; Matrix Metalloproteinase 9* ; Neoplasm Metastasis ; Osteosarcoma* ; Retrospective Studies

OBJECTIVE: To understand the pathogenesis of adenomyosis through the immunohistochemical staining with bcl-2 and matrix metalloproteinase-9 (MMP-9) antibody. METHODS: We selected 45 cases of adenomyosis among the uterine specimens that were extirpated surgically due to benign gynecologic problem. Immunohistochemical staining to the myometrial tissue was performed using anti-bcl-2 and anti-MMP-9 antibodies. Staining was qualitatively assessed in terms of extent and intensity. RESULTS: There were 32 cases of proliferative phase and 13 cases of secretory phase depending on the date of endometrium. Anti-bcl-2 stained 81.3% (26/32) compared with anti-MMP-9 stained 6.3% (2/32) in the glandular tissue of the proliferative phase (p<.001). In the secretory phase, anti-bcl-2 92.3% (12/13) and anti- MMP-9 7.7% (1/13) respectively (p<.001). In the stromal tissue of the proliferative phase, anti-bcl-2 stained 62.5% (20/32) compared with anti- MMP-9 stained 6.3% (2/32) (p<.001). In the secetory phase, anti-bcl-2 84.6% (11/13) and anti-MMP-9 15.4% (2/13) (p<.001). CONCLUSION: The adenomyosis may be developed from simple invagination and cellular proliferation of endometrial tissue, not caused by myometrial infiltration of endometrial tissue.
Adenomyosis* ; Antibodies ; Cell Proliferation ; Endometrium ; Female ; Matrix Metalloproteinase 9

OBJECTIVES: The proliferation, migration capacity, and expression of activation-related proteins of NHGFs+Cal27-exo were determined by coculturing Cal27 exosome (Cal27-exo) with normal human gingival fibroblasts (NHGFs) to explore the effects of Cal27-exo on the activation and biological behavior of NHGFs. METHODS: Cal27-exo was extracted using supercentrifugation, and exosomes were identified using Western blot, transmission electron microscopy (TEM), and particle size detection. Cal27-exo was cocultured with NHGFs to detect the uptake of Cal27-exo by NHGFs, and the proliferation and migration capacity of NHGFs+Cal27-exo were detected using CCK8 and wound healing tests, respectively. The expression levels of NHGF activation-related proteins, i.e., matrix metalloproteinase-9 (MMP-9), fibroblast-activating protein (FAP), alpha smooth muscle actin (αSMA), and transforming growth factor-β (TGF-β), were detected using real-time quantitative polymerase chain reaction (qRT-PCR). RESULTS: Cal27-exo was extracted u-sing supercentrifugation, and Western blot showed the positive expression levels of Alix and CD63. TEM showed that Cal27-exo had a circular double-layer vesicle. The particle size was between 30 and 150 nm. Cal27-exo labeled with PKH67 entered NHGFs after the coculture method. The wound healing test showed that the migration capacity of NHGFs+Cal27-exo was stronger after the scratch compared with that of NHGFs. CCK8 results showed that the proliferation activity of NHGFs+Cal27-exo was enhanced. qRT-PCR results showed that the MMP-9 levels of NHGFs+Cal27-exo were upregulated, whereas the TGF-β and αSMA mRNA levels of NHGFs+Cal27-exo were downregulated ( CONCLUSIONS The proliferation and migration ability of NHGFs+Cal27-exo are enhanced, and the mRNA expression of related proteins is changed. Cal27-exo can activate NHGFs, which suggests that Cal27-exo has potential significance in tumor invasion and metastasis.
Cell Proliferation ; Exosomes ; Fibroblasts ; Gingiva ; Humans ; Matrix Metalloproteinase 9

PURPOSE: Bronchial asthma is an inflammatory respiratory disease characterized by the activation of inflammatory cells and its infiltration. It has been recently reported that MMP- 9 dose an importance role in the movement of inflammatory cells through basal membrane, that the function may be suppressed by TIMP-1. We studied to know the change of MMP-9 and TIMP-1 in sputum before and after corticosteroid (CS) therapy, and the relation with MMP-9/TIMP-1 ratio and improvement of FEV1. METHODS: Seventeen acute moderate to severe asthmatics were selected as was a control group of 17 healthy children. MMP-9 and TIMP-1 in sputum were measured on the 0 day, 7 days and 3 months later and observed as to the flow of time. FEV1 was measured before the CS therapy and 3 months later, and the change of FEV1 & FEV1 at 3 months were compared with the relation of MMP-9/TIMP-1 ratio. RESULTS: Sputum MMP-9 was lowered more at 7 days and 3 months compared with 0 day (P< 0.05). Sputum TIMP-1 was significantly high on 7 days (P< 0.05) and then had a tendency to decrease until 3 months (P< 0.05). MMP-9/TIMP-1 ratio decreased according to the flow of time (P< 0.05). MMP-9/TIMP-1 ratio at 3 months closely correlated with the change of FEV1 (r=0.65, P< 0.05). CONCLUSION: These data suggest that the overproduction of MMP-9 after asthma exacerbation correlates with airway inflammation and TIMP-1 production might contribute to airway fibrosis. MMP-9/TIMP-1 ratio at 3 months correlates with improvement of pulmonary function after CS therapy.
Asthma* ; Child ; Fibrosis ; Gelatinases ; Humans ; Inflammation ; Matrix Metalloproteinase 1* ; Matrix Metalloproteinase 9* ; Membranes ; Prednisolone ; Sputum* ; Tissue Inhibitor of Metalloproteinase-1

OBJECTIVE: This study was performed to investigate the influence of hepatocyte growth factor (HGF) on matrix metalloproteinase (MMP), which are related in the lysis process of tissue during the invasion of trophoblasts. METHOD: HT cell line was treated with recombinant HGF (rHGF) of different concentration (0, 10, 50 and 100 ng/mL) and was cultured for 24 hours to check the changes in the expression of MMP-2 and MMP-9. Also, HT cell line was treated with recombinant HGF 50 ng/mL and was cultured for 24, 36, 48, and 72 hours to check the changes in the expression of MMPs according to the different time span. Total RNA were extracted from each cultured sample and RT-PCR and Western blotting were used to analyze the expression of MMP-2 and MMP-9. RESULTS: MMP-2 mRNA expression with treated rHGF showed increase of 2, 2.5 and 2.2 times with the increase of concentration level of 10, 50 and 100 ng/mL accordingly, while MMP-2 protein expression were increased 1.4 and 1.5 times in 50 ng/mL and 100 ng/mL of rHGF respectively compared with that of normal control. MMP-9 mRNA showed no significant changes in its expression with all different levels of concentration, while MMP-9 protein showed 1.5 times increase with 10 ng/mL rHGF but 0.4 times decrease with 100 ng/mL. MMP-2 mRNA expression treated with recombinat HGF were increased 1.6 times with 24 hour culture and 2.3 times with 36 hour culture. MMP-2 protein showed 1.9 times increase only for the case of 24 hour culture. MMP-9 mRNA expression of recombinant HGF-treated groups was decreased 0.7 times compared with that of control group in 36 hours. MMP-9 protein expression were increased by 1.2, 1.6 and 1.9 times as culture time increase to 36, 48, and 72 hours accordingly, compared with that of normal control. CONCLUSION: This result suggests that the HGF might partially regulate the invasion of trophoblasts through MMP-2 and MMP-9.
Blotting, Western ; Cell Line* ; Hepatocyte Growth Factor* ; Hepatocytes* ; Matrix Metalloproteinase 2 ; Matrix Metalloproteinase 9 ; Matrix Metalloproteinases ; RNA ; RNA, Messenger ; Trophoblasts

OBJECTIVE: This study was performed to investigate the influence of hepatocyte growth factor (HGF) on matrix metalloproteinase (MMP), which are related in the lysis process of tissue during the invasion of trophoblasts. METHOD: HT cell line was treated with recombinant HGF (rHGF) of different concentration (0, 10, 50 and 100 ng/mL) and was cultured for 24 hours to check the changes in the expression of MMP-2 and MMP-9. Also, HT cell line was treated with recombinant HGF 50 ng/mL and was cultured for 24, 36, 48, and 72 hours to check the changes in the expression of MMPs according to the different time span. Total RNA were extracted from each cultured sample and RT-PCR and Western blotting were used to analyze the expression of MMP-2 and MMP-9. RESULTS: MMP-2 mRNA expression with treated rHGF showed increase of 2, 2.5 and 2.2 times with the increase of concentration level of 10, 50 and 100 ng/mL accordingly, while MMP-2 protein expression were increased 1.4 and 1.5 times in 50 ng/mL and 100 ng/mL of rHGF respectively compared with that of normal control. MMP-9 mRNA showed no significant changes in its expression with all different levels of concentration, while MMP-9 protein showed 1.5 times increase with 10 ng/mL rHGF but 0.4 times decrease with 100 ng/mL. MMP-2 mRNA expression treated with recombinat HGF were increased 1.6 times with 24 hour culture and 2.3 times with 36 hour culture. MMP-2 protein showed 1.9 times increase only for the case of 24 hour culture. MMP-9 mRNA expression of recombinant HGF-treated groups was decreased 0.7 times compared with that of control group in 36 hours. MMP-9 protein expression were increased by 1.2, 1.6 and 1.9 times as culture time increase to 36, 48, and 72 hours accordingly, compared with that of normal control. CONCLUSION: This result suggests that the HGF might partially regulate the invasion of trophoblasts through MMP-2 and MMP-9.
Blotting, Western ; Cell Line* ; Hepatocyte Growth Factor* ; Hepatocytes* ; Matrix Metalloproteinase 2 ; Matrix Metalloproteinase 9 ; Matrix Metalloproteinases ; RNA ; RNA, Messenger ; Trophoblasts