Re-epithelialization rate and protein expression in the suction-induced wound model: comparison between intact blisters, open wounds and calcipotriol-pretreated open wounds.
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.
Leivo
T
T
Department of Anatomy, Institute of Biomedicine, PO Box 9, FIN-00014 University of Helsinki, Helsinki, Finland.
Kiistala
U
U
Vesterinen
M
M
Owaribe
K
K
Burgeson
R E
RE
Virtanen
I
I
Oikarinen
A
A
D000328:Adult; D001324:Autoantigens / Q000276:immunology; D001768:Blister / Q000188:drug therapy / Q000378:metabolism / Q000503:physiopathology*; D002117:Calcitriol / Q000031:analogs & derivatives* / Q000627:therapeutic use; D002120:Calcium Channel Agonists / Q000627:therapeutic use*; D002352:Carrier Proteins; D002455:Cell Division / Q000187:drug effects; D003094:Collagen / Q000276:immunology / Q000378:metabolism; D003598:Cytoskeletal Proteins; D003879:Dermatologic Agents / Q000627:therapeutic use*; D003896:Desmosomes / Q000187:drug effects / Q000378:metabolism; D004311:Double-Blind Method; D000071821:Dystonin; D004801:Eosine Yellowish-(YS); D004847:Epithelial Cells / Q000187:drug effects / Q000378:metabolism; D006416:Hematoxylin; D006801:Humans; D016023:Integrins / Q000187:drug effects / Q000276:immunology / Q000378:metabolism; D007381:Intermediate Filament Proteins / Q000276:immunology; D015603:Keratinocytes / Q000166:cytology; D007797:Laminin / Q000187:drug effects / Q000276:immunology / Q000378:metabolism; D008297:Male; D009419:Nerve Tissue Proteins; D024041:Non-Fibrillar Collagens; D051190:Plectin; D012867:Skin / Q000276:immunology; D013194:Staining and Labeling; D019063:Tenascin / Q000276:immunology; D014945:Wound Healing / Q000502:physiology; D000097805:Collagen Type XVII
D001324:Autoantigens; D002117:Calcitriol; D002120:Calcium Channel Agonists; D002352:Carrier Proteins; D003094:Collagen; D003598:Cytoskeletal Proteins; D003879:Dermatologic Agents; D000071821:Dystonin; D004801:Eosine Yellowish-(YS); D006416:Hematoxylin; D016023:Integrins; D007381:Intermediate Filament Proteins; D007797:Laminin; D009419:Nerve Tissue Proteins; D024041:Non-Fibrillar Collagens; D051190:Plectin; D019063:Tenascin; D000097805:Collagen Type XVII; C486268:DST protein, human; C495332:PLEC protein, human; C055085:calcipotriene