Collagen-binding heat shock protein HSP47 expression during healing of fetal skin wounds.

Wounds in fetal animals are known to heal without scar formation, but the mechanism involved remains unclear. Scar tissue is characterized by disorganized collagen bundles. The 47-kDa heat shock protein (HSP47) is a molecular chaperone that specifically targets collagen processing. However, the role of HSP47 in scar formation is poorly understood. We studied the relation of HSP47 expression in skin to scar formation during fetal wound healing. Immunohistochemical analysis demonstrated HSP47-positive cells in the epidermal cell layer of fetal and neonatal rat skin and the absence of such cells in subcutaneous tissue. After induction of a wound on the back of fetal and neonatal rats, the message of collagen type I was increased only in neonatal skin but not in fetal skin. HSP47-positive cells consistently increased for 7 days after wound induction in neonatal rats. In contrast, HSP47-positive cells and HSP47 protein were unchanged in fetal rats. We conclude that the scarless healing of fetal skin wounds is related to lack of change in HSP47 expression. HSP47 may thus be an important determinant of scar formation during wound healing.