Matrilysin is much more efficient than other matrix metalloproteinases in the proteolytic inactivation of alpha 1-antitrypsin.

@article{Sires1994MatrilysinIM,
  title={Matrilysin is much more efficient than other matrix metalloproteinases in the proteolytic inactivation of alpha 1-antitrypsin.},
  author={Ulrike I Sires and Gillian Murphy and Vijaykumar M Baragi and C J Fliszar and Howard G. Welgus and Robert M. Senior},
  journal={Biochemical and biophysical research communications},
  year={1994},
  volume={204 2},
  pages={613-20}
}
alpha 1-antitrypsin, the primary physiologic inhibitor of human leukocyte elastase, is proteolytically inactivated by several matrix metalloproteinases including interstitial collagenase, stromelysin and 92 kDa gelatinase. In this report, we describe the catalytic effects of matrilysin, a recently identified metalloproteinase, upon alpha 1-antitrypsin. Matrilysin was found to be approximately 30-fold more effective than 92kDa gelatinase, 70-fold more effective than collagenase, and 180-fold… CONTINUE READING