Nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways.

@article{Ridnour2007NitricOR,
  title={Nitric oxide regulates matrix metalloproteinase-9 activity by guanylyl-cyclase-dependent and -independent pathways.},
  author={Lisa A. Ridnour and Alisha N. Windhausen and Jeffrey S. Isenberg and Nolan Yeung and Douglas D. Thomas and Michael P Vitek and David D. Roberts and David A Wink},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 43},
  pages={16898-903}
}
Matrix metalloproteinases (MMPs) are of central importance in the proteolytic remodeling of matrix and the generation of biologically active molecules. MMPs are distinguished by a conserved catalytic domain containing a zinc ion, as well as a prodomain that regulates enzyme activation by modulation of a cysteine residue within that domain. Because nitric oxide (NO) and derived reactive nitrogen species target zinc ions and cysteine thiols, we assessed the ability of NO to regulate MMPs. A dose… CONTINUE READING
57 Citations
8 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 57 extracted citations

References

Publications referenced by this paper.
Showing 1-8 of 8 references

Front Biosc

  • RB Pilz, KE Broderick
  • 2005

Trends Cell Biol

  • C Chang, Z Werb
  • 2001

Trends Cell Biol 11:S37–S43

  • C Chang, Z Werb
  • 2001

Matrix Metalloproteinases and TIMPs (Oxford

  • JF Woessner, H Nagase
  • 2000

Wound Repair Regen

  • WC Parks
  • 1999

Wound Repair Regen 7:423–432

  • WC Parks
  • 1999

Free Radic Biol Med

  • DA Wink, JB Mitchell
  • 1998

Protein Sci 4:1966–1976

  • JW Becker, AI Marcy, +7 authors JD Hermes
  • 1995

Similar Papers

Loading similar papers…