[HTML][HTML] Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase
TJ Gronski, RL Martin, DK Kobayashi, BC Walsh… - Journal of Biological …, 1997 - ASBMB
Macrophage elastase (ME) was originally named when metal-dependent elastolytic activity
was detected in conditioned media of murine macrophages. Subsequent cDNA cloning of
the mouse and human enzyme demonstrated that ME is a distinct member of the matrix
metalloproteinase family. To date, the catalytic parameters that describe the hydrolysis of
elastin by ME have not been quantified and its activity against other matrix proteins have not
been described. In this report, we have examined the action of purified recombinant human …
was detected in conditioned media of murine macrophages. Subsequent cDNA cloning of
the mouse and human enzyme demonstrated that ME is a distinct member of the matrix
metalloproteinase family. To date, the catalytic parameters that describe the hydrolysis of
elastin by ME have not been quantified and its activity against other matrix proteins have not
been described. In this report, we have examined the action of purified recombinant human …