Epithelialization of normal
wounds occurs by an orderly series of events whereby keratinocytes migrate, proliferate, and differentiate to restore the barrier function. Keratinocyte migration is one of the most earliest and crucial event determining the efficiency of the overall
wound repair process.
Laminin 332, composed by the association of α3, β3 and γ2 chains, is a major adhesion substrate for keratinocytes and is known for its role in supporting cell adhesion and migration during
wound repair. The α3 chain comprises a large globular region in its carboxyl-terminal end, which consists of five homologous globular domains (LG1-LG5), known to be involved in cellular interactions. Recent findings have suggested that the α3 chain C-terminal domains LG45 may have a role to play during the epithelialization phase in
wound repair. In the present study, we have analyzed whether a
peptide mimicking the major
heparin binding sequence KKLRIKSKEK in α3LG45 may interact with keratinocytes to promote cell adhesion and migration. In vitro experiments supported this hypothesis and revealed that the KKLRIKSKEK
peptide induces human primary keratinocyte adhesion and has the ability to promote keratinocyte migration when added in the culture medium. To examine the
peptide efficacy in vivo, the KKLRIKSKEK
peptide was applied over partial-thickness cutaneous
wounds in pigs. Compared with vehicle-treated cutaneous
wounds, the
peptide application significantly promoted early-stage wound healing by accelerating re-epithelialization. Additional beneficial effects such as reduced inflammatory response and decreased granulation tissue formation were also noticed in the
peptide-treated
wounds.