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Matrix metalloproteinase activity in transformed cells exposed to an antioxidant

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Abstract

We showed that antioxidant N-acetylcysteine (NAC, 2–10 mM) rapidly (in 2 h) and completely deactivated the activity of matrix metalloproteinases (MMPs) (MMP-2 and MMP-9 gelatinases and MMP-1 and MMP-8 collagenases) secreted by transformed 3T3-SV40 mouse fibroblasts into the medium. The same MMP inhibition took place in the cell-free medium conditioned by HT-1080 fibroblasts. This suggests that the direct chemical interaction between NAC and MMP resulted in the loss of MMP activity. In addition to this 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 inhibitors (TIMP-1) remained normal, indicating a shift in the balance between the enzyme and inhibitor. The correlation between MMP-2 and the tissue enzyme inhibitor TIMP-2 level was similar in control and NAC-treated cells. Moreover, reorganization of collagen type I at the cell surface was observed. Taken together, our results suggest that NAC exposure results in extracellular matrix remodeling and a change in cellular functions.

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Authors and Affiliations

  1. Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia

    I. V. Voronkina, E. A. Vakhromova, K. M. Kirpichnikova, L. V. Smagina & I. A. Gamaley

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  1. I. V. Voronkina
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  2. E. A. Vakhromova
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  3. K. M. Kirpichnikova
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  4. L. V. Smagina
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  5. I. A. Gamaley
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Correspondence to I. A. Gamaley.

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Original Russian Text © I.V. Voronkina, E.A. Vakhromova, K.M. Kirpichnikova, L.V. Smagina, I.A. Gamaley, 2014, published in Tsitologiya, 2014, Vol. 56, No. 10, pp. 717–724.

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Voronkina, I.V., Vakhromova, E.A., Kirpichnikova, K.M. et al. Matrix metalloproteinase activity in transformed cells exposed to an antioxidant. Cell Tiss. Biol. 9, 16–23 (2015). https://doi.org/10.1134/S1990519X15010113

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