scholarly journals Clinical significance of serum levels of matrix metalloproteinase 2 (MMP-2) and its tissue inhibitor (TIMP-2) in gastric cancer

2011 ◽  
Vol 49 (1) ◽  
pp. 125-131 ◽  
Author(s):  
Barbara Mroczko ◽  
Marta Łukaszewicz-Zając ◽  
Mariusz Gryko ◽  
Bogusław Kędra ◽  
Maciej Szmitkowski
Keyword(s):  
Gastric Cancer ◽  
Matrix Metalloproteinase ◽  
Clinical Significance ◽  
Serum Levels ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor

Matrix metalloproteinase 2 (MMP-2) and their tissue inhibitor 2 (TIMP-2) in gastric cancer patients

2013 ◽  
Vol 58 (2) ◽  
pp. 235-243 ◽  
Author(s):  
M Łukaszewicz-Zając ◽  
B Mroczko ◽  
K Guzińska-Ustymowicz ◽  
A Pryczynicz ◽  
M Gryko ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Matrix Metalloproteinase ◽  
Cancer Patients ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor ◽  
Gastric Cancer Patients

scholarly journals Pathophysiological disturbances in complicated pancreatic pseudocysts

2015 ◽  
Vol 96 (2) ◽  
pp. 191-197
Author(s):  
O Yu Gerbali ◽  
I A Krivoruchko ◽  
N N Goncharova
Keyword(s):  
Matrix Metalloproteinase ◽  
Interleukin 6 ◽  
Serum Levels ◽  
Matrix Metalloproteinase 2 ◽  
Pancreatic Pseudocysts ◽  
Type I ◽  
Tissue Inhibitor ◽  
Favorable Conditions ◽  
Endothelial Growth Factor ◽  
Metalloproteinase 9

Aim. To determine profibrogenic mediators, markers of endothelial dysfunction and hemostasis in patients with different types of complicated pancreatic pseudocysts.Methods. The study included 47 patients aged 43.58±7.38 years: 42 males and 5 females. The patients were allocated to three groups based on the classification of pancreatic pseudocysts by A. D’Egidio and М. Schein (1991). All patients underwent surgery. Serum levels of vascular endothelial growth factor, matrix metalloproteinase-9, matrix metalloproteinase-2 tissue inhibitor, the complex of metalloproteinase-9 and inhibitor, plasma levels of interleukin-6, -8, -18 and -10 were determined by ELISA method. Blood glutathione peroxidase activity and malondialdehyde serum level were determined by spectrophotometry.Results.Levels of Interleukin-6, -8 and -18 was higher in patients with type I of pseudocysts compared to control (pConclusion. Increased concentration of matrix metalloproteinase-2 tissue inhibitor and increased inhibition coefficient in patients with chronic pancreatitis may reflect favorable conditions for pancreatic remodeling and fibrosis.

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.

scholarly journals Prognostic values of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression in bladder cancer

Cancer ◽  
1998 ◽  
Vol 82 (7) ◽  
pp. 1359-1366 ◽  
Author(s):  
Hiro-omi Kanayama ◽  
Kin-ya Yokota ◽  
Yasushi Kurokawa ◽  
Yoshihide Murakami ◽  
Masaaki Nishitani ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Matrix Metalloproteinase ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor

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.

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