No abstract available.
Matrix Metalloproteinase 1* ; Spinal Diseases*

No abstract available.
Gingival Crevicular Fluid* ; Humans ; Matrix Metalloproteinase 1* ; Matrix Metalloproteinases* ; Periodontitis*

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

The high performance liquid chromatography (HPLC) and enzyme-linked immunoassay (ELISA) were used to investigate the changes of collagen and matrix metalloproteinase-1 (MMP-1) in liver, lung and kidney during growth process of mice. The mice from 0 to 18 weeks were used as the research objects. The contents and proportions of hydroxyproline (Hyp), which were used to calculate the collagen contents, in liver, lung and kidney of different weeks were analyzed with HPLC. The contents and activity of MMP-1 in liver, lung and kidney of different weeks were analyzed with ELISA. The results showed that the collagen contents in liver, lung, and kidney were different (Lung(COL)>Kidney(COL)>Liver(COL)), and they all increased first and then decreased with weeks. The collagen contents in liver, lung, and kidney reached the highest level in the ninth (5.52 ng/mg), sixth (54.10 ng/mg) and ninth (19.20 ng/mg) week, respectively. Then it declined slowly from 9 to 18 weeks. The result of ELISA showed that the MMP-1 contents in liver, lung and kidney decreased first and then increased with weeks, and the trend of MMP-1 activity was opposite. It indicated that the increase of collagen contents in the tissues will inhibit the secretion of MMP-1.
Animals ; Collagen ; Kidney ; Liver ; Lung ; Matrix Metalloproteinase 1 ; Matrix Metalloproteinase 2 ; Mice

OBJECTIVETo detect protein expression of MMPs and TIMPs in various salivary gland neoplasms and to investigate their roles in invasion and metastasis of the malignant salivary gland tumors.

METHODSImmunohistochemistry and Gelatin zymography analyses for MMP-2, MMP-9, MT1-MMP, TIMP-1 and TIMP-2 were performed in 26 malignant and 28 benign salivary gland tumors.

RESULTSThe expression of MMP-2 and MMP-9 was significantly higher in carcinomas than in adenomas (P < 0.05). The MMP-2/TIMP-1 and MMP-2/TIMP-2 was also significantly higher in carcinomas than in adenomas (P < 0.05). There was a cooperated effect among MMP-2, MT1-MMP and TIMP-2. The expression of active MMP-2, proMMP-9 and active MMP-9 was significantly higher in malignant tumors than in benign tumors (P < 0.05).

CONCLUSIONMMP-2 and MMP-9 may play important roles in invasion of malignant salivary gland tumors. A disturbed balance between MMP-2, MMP-9, TIMP-1 and TIMP-2 in malignant salivary gland tumors was detected. It was the absolute increase of MMP-2 and MMP-9 to induce the unbalance.

Enzyme Precursors ; Humans ; Immunohistochemistry ; Matrix Metalloproteinase 2 ; Matrix Metalloproteinase 9 ; Matrix Metalloproteinases ; Salivary Gland Neoplasms ; Salivary Glands ; Tissue Inhibitor of Metalloproteinase-1 ; Tissue Inhibitor of Metalloproteinase-2

OBJECTIVETo compare the distribution and concentrations of matrix metalloproteinase (MMP)-1, 2, 3, 8, 9 in human coronal dentin.

METHODSThe localization of five types of MMP was performed using immunohistochemistry. Molars were demineralized and sectioned into 5 µm thick specimens. All specimens were randomly divided into five groups according to the antibodies. Each group contained two subgroups (n = 6). Immunoreactivity of each subgroup was visualized with 3, 3-diaminobenzidine solution or fluorescein isothiocyanate and observed under microscopy respectively. Molars were sectioned into slices. The slices were divided into two groups according to superficial or deep dentin and pulverized to fine powder. After dentin protein was extracted, the concentrations of MMP-1, 2, 3, 8, 9 were detected by using fluorescent microsphere immunoassay.

RESULTSImmunohistochemical staining revealed that MMP-1, 2, 3, 8, 9 were highly concentrated in the deep dentin. However, intense immunoreactivities of MMP-2, 8, 9 were identified in a 6-10 µm wide zone adjacent to the dentino-enamel junction. The content of MMP-1 in superficial layer and deep layer of dentin were (0.037±0.025) and (0.433±0.089) ng/mg. The content of MMP-2 in superficial layer and deep layer of dentin were (0.445±0.115) and (2.730±0.712) ng/mg. The content of MMP-3 in superficial layer and deep layer of dentin were (0.071±0.069) and (0.460±0.108) ng/mg. The content of MMP-8 in superficial layer and deep layer of dentin were (0.586±0.246) and (6.159±0.948) ng/mg. The content of MMP-9 in superficial layer and deep layer of dentin were (0.384±0.185) and (1.460±0.251) ng/mg. The concentrations of all tested MMP were significantly higher in deep dentin than those in superficial dentin (P < 0.05).

CONCLUSIONSThere are five types of MMP contained in human coronal dentin, and the distribution of MMP shows a decreasing trend from the deep dentin to the superficial dentin.

Dental Enamel ; Dentin ; enzymology ; Fluorescent Antibody Technique ; Humans ; Immunohistochemistry ; Matrix Metalloproteinase 1 ; Matrix Metalloproteinase 2 ; Matrix Metalloproteinase 9 ; Matrix Metalloproteinases ; metabolism ; Molar

No abstract available.
Matrix Metalloproteinases* ; Stomach Neoplasms ; Tissue Inhibitor of Metalloproteinase-1 ; Tissue Inhibitor of Metalloproteinase-2

OBJECTIVE: Endometriosis in a surgical scar following cesarian section is rare condition. And its pathogenesis has not been well established. The purpose of this study is to observe the expressions of matrix metalloproteinase-9 (MMP-9) and tissue inhibitors of metalloproteinase-1 (TIMP-1) in scar endometriosis and full term endometrium during cesarian section. METHODS: Nineteen scar endometriotic tissue and ten full term pregnant endometrium during cesarian section were investigated by immunohistochemical stain for MMP-9 and TIMP-1. RESULTS: The MMP-9 was expressed in eleven of nineteen scar endometriotic tissue (57.9%) and eight of ten full term pregnant endometrium (80.0%). The TIMP-1 was not expressed in both scar endometriotic tissue and full term pregnant endometrium. CONCLUSION: These results suggest that the relationship between MMP-9 and TIMP-1 might play a role of pathogenesis of scar endometriosis.
Cicatrix* ; Endometriosis* ; Endometrium* ; Female ; Matrix Metalloproteinase 9* ; Tissue Inhibitor of Metalloproteinase-1

OBJECTIVE: Endometriosis in a surgical scar following cesarian section is rare condition. And its pathogenesis has not been well established. The purpose of this study is to observe the expressions of matrix metalloproteinase-9 (MMP-9) and tissue inhibitors of metalloproteinase-1 (TIMP-1) in scar endometriosis and full term endometrium during cesarian section. METHODS: Nineteen scar endometriotic tissue and ten full term pregnant endometrium during cesarian section were investigated by immunohistochemical stain for MMP-9 and TIMP-1. RESULTS: The MMP-9 was expressed in eleven of nineteen scar endometriotic tissue (57.9%) and eight of ten full term pregnant endometrium (80.0%). The TIMP-1 was not expressed in both scar endometriotic tissue and full term pregnant endometrium. CONCLUSION: These results suggest that the relationship between MMP-9 and TIMP-1 might play a role of pathogenesis of scar endometriosis.
Cicatrix* ; Endometriosis* ; Endometrium* ; Female ; Matrix Metalloproteinase 9* ; Tissue Inhibitor of Metalloproteinase-1

OBJECTIVETo study the changes of metalloproteinases 1, 2, 13 in granulation wound after the treatment of vacuum-assisted closure (VAC).

METHODSThe chronic wounds in 5 patients were treated with VAC. The expressions of MMP-1, 2, 13 in the granulation tissues of the chronic wounds were determined and quantified using RT-PCR technique before and at 1, 4, 7 days after the treatment.

RESULTSThe MMP-1, 13 mRNA showed obvious decrease, with the steepest variation of MMP-13. The MMP-2 mRNA also showed a decreased tendency, though in an undulatory fashion.

CONCLUSIONVAC can promote healing of chronic wounds through depressing the expressions of MMP-1, 2, 13 mRNA and protein synthesis, depressing the degradations of collagen and gelatin.

Collagen ; metabolism ; Humans ; Matrix Metalloproteinase 1 ; metabolism ; Matrix Metalloproteinase 13 ; metabolism ; Matrix Metalloproteinase 2 ; metabolism ; Negative-Pressure Wound Therapy ; Polymerase Chain Reaction ; Time Factors ; Wound Healing