title: Laminin-5 expression is independent of the injury and the microenvironment during reepithelialization of wounds.
abstract: We examined the expression of laminin-5 and its integrin receptors during reepithelialization of human wounds. We used suction blisters of skin as a model of keratinocyte migration on a basement membrane matrix and mucosal full-thickness wounds as a model in which keratinocytes migrate in a provisional matrix. An animal model, in which human epidermal keratinocytes were injected into the back of athymic mice, was used to follow the deposition of the basement membrane components. In 4-day-old blisters, about 20-50 cells at the leading edge of the migrating tongue showed cytoplasmic laminin-5 immunostaining. Laminin-5 mRNA was detected in 15-30 cells at the leading edge of the migrating epidermis. alpha3beta1 and alpha6beta4 integrins were found in membrane projections of the migrating basal cells and also in suprabasal cell layers, suggesting their combined role in binding laminin-5. In mucosal wounds, laminin-5 was the only basement membrane zone component that was deposited between the clot and the migrating keratinocytes. In the animal model, linear deposition of laminin-5 and alpha6beta4 integrin was already seen on Day 2, whereas the other basement membrane zone components were not yet organized. The results suggest that, regardless of the injury and the microenvironment, laminin-5 plays an essential role in the interaction between wound keratinocytes and the surrounding matrix.
authors.affiliation: Department of Oral and Maxillofacial Surgery, University of Oulu, Oulu, Finland.
authors.forename: T
authors.initials: T
authors.lastname: Kainulainen
authors.forename: L
authors.initials: L
authors.lastname: Hakkinen
authors.forename: S
authors.initials: S
authors.lastname: Hamidi
authors.forename: K
authors.initials: K
authors.lastname: Larjava
authors.forename: M
authors.initials: M
authors.lastname: Kallioinen
authors.forename: J
authors.initials: J
authors.lastname: Peltonen
authors.forename: T
authors.initials: T
authors.lastname: Salo
authors.forename: H
authors.initials: H
authors.lastname: Larjava
authors.forename: A
authors.initials: A
authors.lastname: Oikarinen
mesh_terms: D000328:Adult; D000368:Aged; D000818:Animals; D000951:Antigens, Neoplasm / Q000378:metabolism / Q000502:physiology; D000954:Antigens, Surface / Q000378:metabolism; D001485:Basement Membrane / Q000502:physiology; D015815:Cell Adhesion Molecules / Q000378:metabolism* / Q000502:physiology; D002478:Cells, Cultured; D016207:Cytokines / Q000494:pharmacology; D004195:Disease Models, Animal; D005353:Fibronectins / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D039201:Integrin alpha3beta1; D039161:Integrin alpha6beta4; D016023:Integrins / Q000378:metabolism*; D015603:Keratinocytes / Q000187:drug effects / Q000378:metabolism / Q000502:physiology / Q000637:transplantation; D051379:Mice; D008819:Mice, Nude; D008875:Middle Aged; D017474:Receptors, Laminin / Q000378:metabolism / Q000502:physiology; D015854:Up-Regulation; D014945:Wound Healing / Q000502:physiology*; D000097794:Kalinin
chemical_list: D000951:Antigens, Neoplasm; D000954:Antigens, Surface; D015815:Cell Adhesion Molecules; D016207:Cytokines; D005353:Fibronectins; D039201:Integrin alpha3beta1; D039161:Integrin alpha6beta4; D016023:Integrins; D017474:Receptors, Laminin; D000097794:Kalinin