Expression of SKALP/elafin during wound healing in human skin

Arch Dermatol Res. 1996 Jul;288(8):458-62. doi: 10.1007/BF02505235.

Abstract

Skin-derived antileukoproteinase (SKALP), also known as elafin, is a proteinase inhibitor with specificity for polymorphonuclear leucocyte (PMN)- derived elastase and proteinase-3. SKALP is absent in normal human epidermis, but is strongly induced in inflammatory dermatoses such as psoriasis. SKALP is putatively involved in the regulation of cutaneous inflammation by inhibiting PMN derived proteinases. The aim of this study was to investigate SKALP expression and PMN infiltration during wound healing in human skin. This was examined in healing excisional wounds in normal skin and in impaired healing in various types of chronic venous ulcers. Tissues were analysed using immunohistochemistry and Northern blot analysis. Healing of excisional wounds was studied from day 0 to day 14. An influx of PMN was seen rapidly after wounding and was maximal between day 2 and 4 and then subsided. SKALP was induced within 48 h and was expressed in the suprabasal keratinocytes of the wound edge and the migrating epidermal sheet. SKALP expression was maximal on day 4 and was downregulated at the time of complete reepithelialization (7-14 days). In venous ulcers, PMN were abundant in the wound bed and scarce under the wound edge. SKALP was strongly expressed in the keratinocytes of the wound edge in all types of ulcers studied. In the wound bed, SKALP was not detectable. Our results suggest that SKALP plays a role in the acute, inflammatory phase of wound healing. From the kinetics and topology of SKALP expression we surmise that it negatively regulates PMN infiltration.

MeSH terms

  • Adult
  • Aged
  • Chronic Disease
  • Dermatitis / metabolism*
  • Humans
  • Keratinocytes / metabolism
  • Kinetics
  • Middle Aged
  • Neutrophils / metabolism*
  • Protein Biosynthesis*
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins*
  • Serine Proteinase Inhibitors / biosynthesis*
  • Skin / metabolism*
  • Varicose Ulcer / physiopathology
  • Wound Healing / physiology*

Substances

  • Proteinase Inhibitory Proteins, Secretory
  • Proteins
  • Serine Proteinase Inhibitors