Collagenase-1 complexes with α2-macroglobulin in the acute and chronic wound environments

F. Grinnell, M. Zhu, W. C. Parks

Research output: Contribution to journalArticlepeer-review

36 Scopus citations


The purpose of this study was to examine the appearance and activation of collagenase-1 (MMP-1) in the wound environment. We found that MMP-1 accumulates in the fluid phase of the burn wound environment within 2 d of injury and reaches maximal levels by day 4. Two forms of the enzyme were evident; one that corresponded to proMMP-1 and another that corresponded to a group of high molecular mass (≃200 kDa and >200 kDa doublet) MMP-1 containing complexes. ProMMP-1 and MMP-1 containing complexes also occurred in wound fluid from venous stasis ulcers, but neither was detected in mastectomy fluid or in plasma. Levels of the proteinase inhibitor α2- macroglobulin in burn fluid and chronic ulcer wound fluid were almost as high as in plasma, and the high molecular mass MMP-1 containing complexes in burn fluid appeared to result from binding between α2-macroglobulin and activated MMP-1. These observations provide direct evidence that active MMP-1 in the fluid phase of the wound environment becomes complexed to α2-macroglobulin.

Original languageEnglish (US)
Pages (from-to)771-776
Number of pages6
JournalJournal of Investigative Dermatology
Issue number5
StatePublished - 1998


  • Metalloproteinase
  • TIMP
  • Wound repair

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Dermatology
  • Cell Biology


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