Differential expression of tissue inhibitor of metalloproteinases-3 in cultured astrocytes and neurons regulates the activation of matrix metalloproteinase-2

2007 ◽  
Vol 85 (4) ◽  
pp. 829-836 ◽  
Author(s):  
Wenlan Liu ◽  
Takamitsu Furuichi ◽  
Minoru Miyake ◽  
Gary A. Rosenberg ◽  
Ke Jian Liu
Keyword(s):  
Matrix Metalloproteinase ◽  
Differential Expression ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor ◽  
Cultured Astrocytes

scholarly journals Steps involved in activation of the complex of pro-matrix metalloproteinase 2 (progelatinase A) and tissue inhibitor of metalloproteinases (TIMP)-2 by 4-aminophenylmercuric acetate

1995 ◽  
Vol 308 (2) ◽  
pp. 645-651 ◽  
Author(s):  
Y Itoh ◽  
S Binner ◽  
H Nagase
Keyword(s):  
Matrix Metalloproteinase ◽  
Noncovalent Complex ◽  
The Other ◽  
Gelatinolytic Activity ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor ◽  
Sh Group ◽  
Inhibitory Domain ◽  
Interstitial Collagenase

Tissue inhibitor of metalloproteinases (TIMP)-2 forms a noncovalent complex with the precursor of matrix metalloproteinase 2 (proMMP-2, progelatinase A) through interaction of the C-terminal domain of each molecule. We have isolated the proMMP-2-TIMP-2 complex from the medium of human uterine cervical fibroblasts and investigated the processes involved in its activation by 4-aminophenylmercuric acetate (APMA). The treatment of the complex with APMA-activated proMMP-2 by disrupting the Cys73-Zn2+ interaction of the zymogen. This is triggered by perturbation of the proMMP-2 molecule, but not by the reaction of the SH group of Cys73 with APMA. The ‘activated’ proMMP-2 (proMMP-2*) formed a new complex with TIMP-2 by binding to the N-terminal inhibitory domain of the inhibitor without processing the propeptide. Thus the APMA-treated proMMP-2*-TIMP-2 complex exhibited no gelatinolytic activity. In the presence of a small amount of free MMP-2, however, proMMP-2* in the complex was converted into the 65 kDa MMP-2 by proteolytic attack of MMP-2, but the complex did not exhibit gelatinolytic activity. The gelatinolytic activity detected after APMA treatment was solely derived from the activation of free proMMP-2. The removal of the propeptide of the proMMP-2* bound to TIMP-2 was also observed by MMP-3 (stromelysin 1), but not by MMP-1 (interstitial collagenase). MMP-3 cleaved the Asn80-Tyr81 bond of proMMP-2*. On the other hand, when MMP-3 was incubated with the proMMP-2-TIMP-2 complex, it bound to TIMP-2 and rendered proMMP-2 readily activatable by APMA. These results indicate that the blockage of TIMP-2 of the complex with an active MMP is essential for the activation of proMMP-2 when it is complexed with TIMP-2.

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 Some indicators of left ventricular dysfunction in hypertensive patients, depending on the level of matrix metalloproteinases and tissue inhibitors of metalloproteinase-1

2021 ◽  
Vol 102 (6) ◽  
pp. 815-820
Author(s):  
T V Kalinkina ◽  
N V Lareva ◽  
M V Chistyakova
Keyword(s):  
Matrix Metalloproteinases ◽  
Matrix Metalloproteinase ◽  
Diastolic Dysfunction ◽  
Longitudinal Strain ◽  
Global Longitudinal Strain ◽  
Serum Levels ◽  
Left Ventricular ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor

Aim. To study the level of matrix metalloproteinases-1 and -2, and tissue inhibitor of metalloproteinases-1, the indicator of left ventricular myocardial deformation in patients with stage 12 hypertension. Methods. 114 patients (40 women and 74 men) with hypertension of 12 stages observed in the cardiology Department of the Road clinical hospital Chita II were examined. The median age was 428.3 years. Left ventriclular diastolic function was studied by using tissue Doppler imaging in apical four-chamber views. Serum matrix metalloproteinase-1, matrix metalloproteinase-2, and tissue inhibitor of metalloproteinases-1 levels were measured in all patients on automated immunoassay analyzers using ready-to-use ELISA kits. Results. An increase in serum levels of matrix metalloproteinases-1 and -2 in the group of patients with hypertension and diastolic dysfunction by 46 and 47%, respectively, was found against increased levels of serum tissue inhibitor of metalloproteinase-1 (р=0.049). In patients with diastole dysfunction, myocardial global longitudinal strain was decreased in was observed by 22.8% compared with patients without diastole dysfunction (p 0.05). The analysis revealed a moderate negative relationship between left ventricular global longitudinal strain and the serum levels of metalloproteinases-2 (r=0.64, p 0.05). Conclusion. In patients with hypertension and left ventricular diastolic dysfunction, a decrease in left ventricular global longitudinal strain is associated with the serum level of matrix metalloproteinase-2; a tissue inhibitor of metalloproteinases-1 is unrelated to left ventricular global myocardial strain.

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