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- Title
Collagenase-2 (MMP-8) and matrilysin-2 (MMP-26) expression in human wounds of different etiologies.
- Authors
Pirilä, Emma; Korpi, Jarkko T; Korkiamäki, Timo; Jahkola, Tiina; Gutierrez‐Fernandez, Ana; Lopez‐Otin, Carlos; Saarialho‐Kere, Ulpu; Salo, Tuula; Sorsa, Timo
- Abstract
Wound healing involves highly controlled events including reepithelialization, neoangiogenesis, and reformation of the stromal compartment. Matrix metalloproteinases (MMPs) are a family of neutral zinc-dependent endopeptidases known to be essential for the wound-healing process. MMP-8 (collagenase-2) is a neutrophil-derived highly effective type I collagenase, recently indicated to be important for acute wound healing. MMP-26 is a more recent and less well-studied member of the MMP family. Our aim was to study the expression of MMP-8 and MMP-26 in human cutaneous wound repair and chronic wounds using histological methods and cell culture. MMP-8 expression was associated with epithelial cells, neutrophils, and other inflammatory cells in chronic human wounds. MMP-26 was prominently expressed in the extracellular compartment of most chronic wounds in close vicinity to the basement membrane area. MMP-26 was also expressed in acute day 1 wounds with declining expression thereafter. In vitro wound experiments showed that both MMP-8 and MMP-26 were expressed by migrating human mucosal keratinocytes. Inhibiting MMP-26 resulted in aberrant keratinocyte migration and proliferation. We conclude that MMP-8 and MMP-26 are differentially expressed in acute and chronic wounds.
- Subjects
WOUND healing; COLLAGENASES; METALLOPROTEINASES; ENDOPEPTIDASES; CELL culture; REGENERATION (Biology)
- Publication
Wound Repair & Regeneration, 2007, Vol 15, Issue 1, p47
- ISSN
1067-1927
- Publication type
Article
- DOI
10.1111/j.1524-475X.2006.00184.x