scholarly journals Potential role of matrix metalloproteinase-2,-9 and tissue inhibitors of metalloproteinase-1,-2 in exudative pleural effusions

2009 ◽  
Vol 32 (4) ◽  
pp. 293 ◽  
Author(s):  
S Vatansever ◽  
R Gelisgen ◽  
H Uzun ◽  
S Yurt ◽  
F Kosar
Keyword(s):  
Pleural Effusion ◽  
Matrix Metalloproteinase ◽  
Pleural Fluid ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitors ◽  
Tissue Inhibitors Of Metalloproteinase ◽  
Number Of Patients ◽  
Diagnostic Values ◽  
Tuberculous Pleurisy

Purpose: To investigate diagnostic values of pleural fluid matrix metalloproteinase-2 (MMP-2), MMP-9, tissue inhibitors of metalloproteinase-1 (TIMP-1) and TIMP-2 measurements in tuberculous pleurisy(TP) and malignat pleurisy (MP). Methods: The study included 24 patients with TP, 22 patients with MP and 15 patients with pleural effusion of non-tuberculous and non-malignant origin as controls. MMP-2,-9 and TIMP-1,-2 levels in pleural fluid were measured by ELISA method. Results: Pleural fluid MMP-2 and MMP-9 levels were higher (P < 0.001, P < 0.001, respectively) in TP than in MP and controls. MP patients have higher pleural fluid MMP-2 and MMP-9 levels (P < 0.01, P < 0.05, respectively) than controls. Pleural fluid TIMP-2 levels were higher (P < 0.01 and P < 0.001, respectively) in MP than in TP and controls. Pleural fluid MMP-9 levels were negatively correlated with pleural fluid TIMP-2 levels (r: 0.464, P=0.029) in patients with MP. Conclusions: Determination of TIMP-2 in pleural fluid may contribute to differentiate TP from MP. These results suggest that overproduction of MMP-9 and TIMP-2 is associated with accumulation of the pleural effusion in malignancy. Further studies with a greater number of patients are needed to confirm this hypothesis.

scholarly journals Plasma profiling determinants of matrix homeostasis in paediatric dilated cardiomyopathy

2010 ◽  
Vol 21 (1) ◽  
pp. 52-61 ◽  
Author(s):  
Tain-Yen Hsia ◽  
Jeremy M. Ringewald ◽  
Robert E. Stroud ◽  
Nadia Roessler ◽  
Nidhi Kumar ◽  
...  
Keyword(s):  
Matrix Metalloproteinases ◽  
Matrix Metalloproteinase ◽  
Dilated Cardiomyopathy ◽  
Plasma Levels ◽  
Tissue Inhibitors Of Metalloproteinases ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor ◽  
Tissue Inhibitors ◽  
Tissue Inhibitors Of Metalloproteinase

AbstractObjectiveDilated cardiomyopathy is an important cause of cardiac failure in both children and adults, but is more progressive in children. In adult dilated cardiomyopathy, left ventricular remodelling is associated with changes in the plasma levels of matrix metalloproteinases and tissue inhibitor of metalloproteinases. Plasma matrix metalloproteinases and tissue inhibitors of metalloproteinase changes in paediatric dilated cardiomyopathy have not been examined. This study developed a low blood volume, high-sensitivity assay to test the hypothesis that unique and differential plasma matrix metalloproteinases and tissue inhibitors of metalloproteinase profile exist in patients with paediatric dilated cardiomyopathy.Methods/resultsA systemic blood sample (1 millilitre) was obtained from seven children aged 8 plus or minus 7 years with dilated cardiomyopathy and 26 age-matched normal volunteers. Using a high-throughput multiplex suspension immunoassay, plasma levels were quantified for collagenases (matrix metalloproteinase-8), gelatinases (matrix metalloproteinase-2 and -9), lysins (matrix metalloproteinase-3 and -7), and tissue inhibitor of metalloproteinases-1, -2, and -4. The matrix metalloproteinase to tissue inhibitors of metalloproteinases ratios were also calculated. The plasma matrix metalloproteinase-2, -7, -8, and -9 levels were increased by greater than twofold in patients with dilated cardiomyopathy than normal patients (with p less than 0.05). Patients with dilated cardiomyopathy also had significantly higher tissue inhibitors of metalloproteinases-1 and -4 (298% and 230%; with p less than 0.05).ConclusionsThese unique findings show that a specific plasma matrix metalloproteinase/tissue inhibitor of metalloproteinase profile occurs in paediatric dilated cardiomyopathy when compared to the cases of normal children. These distinct differences in the determinants of myocardial matrix structure and function may contribute to the natural history of dilated cardiomyopathy in children and may provide a novel biomarker platform in paediatric dilated cardiomyopathy.

scholarly journals Immunohistochemical Correlation of Matrix Metalloproteinase-2 and Tissue Inhibitors of Metalloproteinase-2 in Tobacco Associated Epithelial Dysplasia

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Dipshikha Bajracharya ◽  
Bijayatha Shrestha ◽  
Asha Kamath ◽  
Aparna Menon ◽  
Raghu Radhakrishnan
Keyword(s):  
Matrix Metalloproteinase ◽  
Statistical Significance ◽  
Normal Mucosa ◽  
Epithelial Dysplasia ◽  
Matrix Metalloproteinase 2 ◽  
Immunohistochemical Expression ◽  
Tissue Inhibitors ◽  
Tissue Inhibitors Of Metalloproteinase ◽  
Potentially Malignant ◽  
Spearman’S Correlation

Aim. To study the immunohistochemical expression of matrix metalloproteinase and tissue inhibitors of matrix metalloproteinase-2 in different histological grades of tobacco associated epithelial dysplasia and correlate the association between these proteases. Potentially malignant oral disorders (PMODs) progressing to oral cancer are related to the severity of epithelial dysplasia.Methods. A retrospective immunohistochemical study was carried out on 30 clinically and histologically proven cases of leukoplakia with dysplasia and 10 cases of normal buccal mucosa using anti-MMP-2 and anti-TIMP-2 monoclonal antibodies.Results. Mann WhitneyUtest, for comparing the expression of both MMP-2 and TIMP-2 in normal mucosa with dysplasia, was highly significant (P<0.001). Kruskal-Wallis test to compare the median score of MMP-2 and TIMP-2 in different grades of dysplasia showed statistical significance (P<0.001), and a Spearman’s correlation between MMP-2 and TIMP-2 through different grades of dysplasia and cells observed showed positive correlation.Conclusion. Concomitant increase in the expression of both MMP-2 and TIMP-2 suggested that the activation of MMP-2 is dependent on TIMP-2 acting as a cofactor. Changes in TIMP-2 levels are considered important because they directly affect the level of MMP-2 activity.

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