Re-epithelialization rate and protein expression in the suction-induced wound model: comparison between intact blisters, open wounds and calcipotriol-pretreated open wounds.

Abstract	We have investigated re-epithelialization following induction of suction blisters in humans in intact blisters, open wounds, i.e. blister roofs removed immediately after blister induction, and calcipotriol-pretreated open wounds. Intact blisters simulate blister healing in bullous disease, while open wounds simulate re-epithelialization during wound healing. Re-epithelialization was clearly faster in open wounds than in intact blisters, and was not affected by calcipotriol pretreatment. Bullous pemphigoid antigen 2 (BP180), bullous pemphigoid antigen 1 (BP230), plectin/hemidesmosomal 1 protein (HD1), laminin 5, laminin alpha5, laminin beta1, type VII collagen, tenascin-C, beta4, alphavbeta5, alpha5 and alpha9 integrins were studied in intact blisters and open wounds by immunohistochemistry. Hemidesmosomal plaque proteins BP230 and plectin/HD1, which connect the keratin cytoskeleton to the hemidesmosome, appeared earlier at the leading edge in intact blisters than in open wounds. Band-like immunostaining in the basement membrane for laminin 5, alpha5 and beta1 chains was continuous in blister bases, but partially discontinuous in open wound bases. The other antigens studied showed similar expression in intact blisters and open wounds. BP180, BP230, plectin/HD1, beta4 integrin, laminin 5 and tenascin-C expression were further studied in calcipotriol-pretreated open wounds. Calcipotriol did not affect the expression of these antigens. The immunohistochemical results suggest that the keratin cytoskeleton is linked to the basal plasma membrane of migrating basal cells via BP230 and plectin/HD1 earlier in the more slowly re-epithelializing blisters than in open wounds. An intact laminin sheath may inhibit keratinocyte migration in intact blisters.
Authors	T Leivo, U Kiistala, M Vesterinen, K Owaribe, R E Burgeson, I Virtanen, A Oikarinen
Journal	The British journal of dermatology (Br J Dermatol) Vol. 142 Issue 5 Pg. 991-1002 (May 2000) ISSN: 0007-0963 [Print] England
PMID	10809861 (Publication Type: Clinical Trial, Comparative Study, Controlled Clinical Trial, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	Autoantigens Calcium Channel Agonists Carrier Proteins Cytoskeletal Proteins DST protein, human Dermatologic Agents Dystonin Integrins Intermediate Filament Proteins Laminin Nerve Tissue Proteins Non-Fibrillar Collagens PLEC protein, human Plectin Tenascin collagen type XVII calcipotriene Collagen Calcitriol Eosine Yellowish-(YS) Hematoxylin
Topics	Adult Autoantigens (immunology) Blister (drug therapy, metabolism, physiopathology) Calcitriol (analogs & derivatives, therapeutic use) Calcium Channel Agonists (therapeutic use) Carrier Proteins Cell Division (drug effects) Collagen (immunology, metabolism) Cytoskeletal Proteins Dermatologic Agents (therapeutic use) Desmosomes (drug effects, metabolism) Double-Blind Method Dystonin Eosine Yellowish-(YS) Epithelial Cells (drug effects, metabolism) Hematoxylin Humans Integrins (drug effects, immunology, metabolism) Intermediate Filament Proteins (immunology) Keratinocytes (cytology) Laminin (drug effects, immunology, metabolism) Male Nerve Tissue Proteins Non-Fibrillar Collagens Plectin Skin (immunology) Staining and Labeling Tenascin (immunology) Wound Healing (physiology)

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