Metalloproteinase activation cascade after burn injury: a longitudinal analysis of the human wound environment.
In this paper, we present a longitudinal study on metalloproteinases in wound-fluid samples collected from three patients with partial- to full-thickness burn wounds. Gelatin zymography showed that 92-kDa gelatinase (MMP-9) and its 225-kDa complex could be detected in burn fluid beginning as early as 4-8 h after injury. Marked increases in MMP-9 levels as well as activation of the proenzyme occurred between day 0 and day 2. The 72-kDa gelatinase (MMP-2) proenzyme was not detected until day 2 and activated enzyme did not appear until day 4. Stromelysin (MMP-3), both proenzyme and activated-enzyme forms, was first observed on day 4. Fluid-phase proteinase activity detected by azocoll degradation roughly corresponded with the level of stromelysin rather than the gelatinases. Our results provide evidence for a regulated metalloproteinase activation cascade following acute traumatic injury and demonstrate in vivo expression of metalloproteinase activity.
Department of Cell Biology and Neuroscience, UT Southwestern Medical School, Dallas 75235.
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Young
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Grinnell
D000328:Adult; D001391:Azo Compounds / Q000378:metabolism; D001826:Body Fluids / Q000378:metabolism; D002056:Burns / Q000378:metabolism*; D003094:Collagen / Q000378:metabolism; D004396:Coloring Agents; D004789:Enzyme Activation; D005260:Female; D006801:Humans; D008137:Longitudinal Studies; D008297:Male; D019278:Matrix Metalloproteinase 3; D008666:Metalloendopeptidases / Q000378:metabolism*; D008875:Middle Aged
D001391:Azo Compounds; D004396:Coloring Agents; C028470:Azocoll; D003094:Collagen; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3