Metalloproteinase activation cascade after burn injury: A longitudinal analysis of the human wound environment

Patty K. Young, Frederick Grinnell

Research output: Contribution to journalArticlepeer-review

85 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)660-664
Number of pages5
JournalJournal of Investigative Dermatology
Issue number5
StatePublished - Nov 1994


  • gelatinase
  • inflammation
  • stromelysin
  • wound healing

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Dermatology
  • Cell Biology


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