Matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-2 expression in paediatric tumour cells. Effects of tumour cell proliferation modulators on gelatinolytic activity

1995 ◽  
Vol 121 (5) ◽  
pp. 275-278 ◽  
Author(s):  
Rocío Garcia de Veas ◽  
Lothar Schweigerer ◽  
Miguel Angel Medina
Keyword(s):  
Cell Proliferation ◽  
Matrix Metalloproteinase ◽  
Tumour Cell ◽  
Tumour Cells ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Gelatinolytic Activity ◽  
Matrix Metalloproteinase 2 ◽  
Tissue Inhibitor ◽  
Tumour Cell Proliferation

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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