ACTIVITY OF MATRIX METALLOPROTEINASES OF TRANSFORMED FIBROBLASTS
UNDER THE ANTIOXIDANT ACTION
I.V. Voronkina, E.A. Vakhromova, K.M. Kirpichnikova, L.V. Smagina, I.A. Gamaley *
Institute of Cytology RAS, St. Petersburg;
* e-mail: igamaley@mail.cytspb.rssi.ru
We have shown that antioxidant N-acetylcysteine (NAC, 2—10 mM) quickly (for 2 hours) and completely
inactivates the activity of matrix metalloproteinases (gelatinases MMP-2 and MMP-9, and collagenases
MMP-1 and MMP-8) secreted by transformed mouse fibroblasts 3T3-SV40 into the medium. The same MMP
inhibition took place in the cell-free conditioned medium of حز-1080 fibroblasts, which suggests a direct chemical
interaction between NAC and MMP resulting in the loss of MMP activity. Besides inhibitory effect, NAC
decreased MMP-1 and MMP-9 (but not MMP-2) production in the cell medium. However, the level of MMP-1
and MMP-9 inhibitor (TIMP-1) remained normal, indicating a shift in the balance between the enzyme and inhibitor.
The correlation between MMP-2 level and tissue enzyme inhibitor TIMP-2 was similar in control and
NAC treated cells. At the same time, reorganization of type I collagen at the cell surface occurred. All together
permits the conclusion that NAC action results in the extracellular matrix remodeling and changing in cellular
functions.
Key words: N-acetylcysteine, matrix metalloproteinases, tissue inhibitor of MMP, extracellular matrix,
collagen I
| Back
| Contents
| Main |
