Intracellular processing and activation of membrane type 1 matrix metalloprotease depends on its partitioning into lipid domains.

@article{Mazzone2004IntracellularPA,
  title={Intracellular processing and activation of membrane type 1 matrix metalloprotease depends on its partitioning into lipid domains.},
  author={Marco Mazzone and Massimiliano Baldassarre and Galina V. Beznoussenko and Giada Giacchetti and Jian Zhong Cao and Stanley Zucker and Alberto Luini and Roberto Buccione},
  journal={Journal of cell science},
  year={2004},
  volume={117 Pt 26},
  pages={6275-87}
}
The integral membrane type 1 matrix metalloprotease (MT1-MMP) is a pivotal protease in a number of physiological and pathological processes and confers both non-tumorigenic and tumorigenic cell lines with a specific growth advantage in a three-dimensional matrix. Here we show that, in a melanoma cell line, the majority (80%) of MT1-MMP is sorted to detergent-resistant membrane fractions; however, it is only the detergent-soluble fraction (20%) of MT1-MMP that undergoes intracellular processing… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 21 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 61 references

Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin . A possible cell surface activator

  • P. Osenkowski, M. Toth, R. Fridman
  • FEBS Lett .
  • 2004

Similar Papers

Loading similar papers…