Identification of functional markers in a self-assembled skin substitute in vitro |
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Authors: | Bisera Cvetkovska Nazrul Islam Francine Goulet Lucie Germain |
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Institution: | 1.Laboratoire de Recherche des Grands Br?lés/LOEX, H?pital du Saint-Sacrement du CHA,Université Laval,Quebec City,Canada;2.Laboratoire de Génie Tissulaire/LOEX, H?pital de l’Enfant-Jésus du CHA,Université Laval,Quebec City,Canada;3.Département de Chirurgie,Université Laval,Quebec City,Canada;4.Département de Réadaptation,Université Laval,Quebec City,Canada;5.Laboratoire de Recherche des Grands Br?lés/LOEX, H?pital du Saint-Sacrement du CHA,Sainte-Foy,Canada |
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Abstract: | Some functional parameters were identified and assessed in a tissue-engineered self-assembled skin substitute. This skin substitute
was produced using fibroblasts and keratinocytes isolated from adult human skin. Keratinocytes were seeded on a dermal layer,
composed of two fibroblast sheets cultured for 35 d. The epidermal cells formed a stratified and cornified epidermis and expressed
differentiation markers, notably involucrin and transglutaminase. Interestingly and for the first time, the receptor for vitamin
D3 was detected in all of the epidermal cell layers of the skin substitute, as it is reported for normal human skin. This
observation suggests that keratinocytes retain key receptors during their differentiation in the skin model. A network of
collagen fibers was observed by electron microscopy in the dermal layer of the model. In the dermis, collagen fibers remodeling
and assembly is dependent on enzymes, notably prolyl-4-hydroxylase. For the first time in a skin construct, the expression
of prolyl-4-hydroxylase was detected in dermal fibroblasts by in situ hybridization. The secretion of collagenases by the
cells seeded in our skin substitute was confirmed by zymography. We conclude that the self-assembly approach allows the maintenance
of several functional activities of human skin cells in a skin model in vitro. |
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Keywords: | Skin substitute Vitamin D3 receptor Prolyl-4-hydroxylase |
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