Activation of MMP-9 by neutrophil elastase in an in vivo model of acute lung injury.
The effect of neutrophil elastase on the functional status of gelatinases was studied in an hamster model developed by intratracheal administration of lipopolysaccharide followed by in situ cell activation with phorbol myristate acetate. This resulted in the production in bronchoalveolar lavage fluids, in addition to the matrix metalloproteinase MMP-9, of a 75 kDa gelatinase associated with collagenolytic activity. Treatment in vivo with an elastase inhibitor abolished the latter activity. Since, in addition, elastase activates in vitro purified MMP-9 gelatinase into a similar 75 kDa entity, these data suggest that elastase may be a physiological activator of MMP-9 in vivo.
Ferry
G
G
Department of Oncology, Institut de Recherches Servier, Suresnes, France.
Lonchampt
M
M
Pennel
L
L
de Nanteuil
G
G
Canet
E
E
Tucker
G C
GC
D000818:Animals; D001992:Bronchoalveolar Lavage Fluid; D017364:Collagenases / Q000378:metabolism*; D006224:Cricetinae; D004789:Enzyme Activation; D018093:Gelatinases / Q000378:metabolism; D019272:Leukocyte Elastase / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000633:toxicity*; D008168:Lung / Q000187:drug effects / Q000473:pathology* / Q000503:physiopathology; D008297:Male; D020780:Matrix Metalloproteinase 9; D008647:Mesocricetus; D013379:Substrate Specificity; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D008070:Lipopolysaccharides; D019272:Leukocyte Elastase; D017364:Collagenases; D018093:Gelatinases; D020780:Matrix Metalloproteinase 9; D013755:Tetradecanoylphorbol Acetate