title: Periostin, a matricellular protein, accelerates cutaneous wound repair by activating dermal fibroblasts.
abstract: Cutaneous wound repair is a highly ordered and well-coordinated process involving various cell lineages and many molecular effectors. Cell-matrix interactions through integrin molecules provide key signals important for wound repair. Periostin is a matricellular protein that may provide signals important during tissue development and remodelling by interacting with several integrin molecules, via the phosphatidylinositol 3-kinase/Akt and MAP kinase pathways. In this study, we examined the role of periostin in the process of cutaneous wound repair using periostin-deficient mice and by analysing the effects of periostin on dermal fibroblasts. We first determined the expression profile and localization of periostin in a well-characterized wound repair model mice. Periostin was robustly deposited in the granulation tissues beneath the extended epidermal wound edges and at the dermal-epidermal junctions in wounded mice. Moreover, periostin-deficient mice exhibited delayed in vivo wound repair, which could be improved by direct administration of exogenous periostin. In vitro analyses revealed that loss of periostin impaired proliferation and migration of dermal fibroblasts, but exogenous supplementation or enforced periostin expression enhanced their proliferation. Combined, these results demonstrate that periostin accelerates the process of cutaneous wound repair by activating fibroblasts.
authors.affiliation: Division of Medical Biochemistry, Department of Biomolecular Sciences, Saga Medical School, Saga, Japan.
authors.forename: Kanako
authors.initials: K
authors.lastname: Ontsuka
authors.forename: Yorihisa
authors.initials: Y
authors.lastname: Kotobuki
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Shiraishi
authors.forename: Satoshi
authors.initials: S
authors.lastname: Serada
authors.forename: Shoichiro
authors.initials: S
authors.lastname: Ohta
authors.forename: Atsushi
authors.initials: A
authors.lastname: Tanemura
authors.forename: Lingli
authors.initials: L
authors.lastname: Yang
authors.forename: Minoru
authors.initials: M
authors.lastname: Fujimoto
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Arima
authors.forename: Shoichi
authors.initials: S
authors.lastname: Suzuki
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Murota
authors.forename: Shuji
authors.initials: S
authors.lastname: Toda
authors.forename: Akira
authors.initials: A
authors.lastname: Kudo
authors.forename: Simon J
authors.initials: SJ
authors.lastname: Conway
authors.forename: Yutaka
authors.initials: Y
authors.lastname: Narisawa
authors.forename: Ichiro
authors.initials: I
authors.lastname: Katayama
authors.forename: Kenji
authors.initials: K
authors.lastname: Izuhara
authors.forename: Tetsuji
authors.initials: T
authors.lastname: Naka
mesh_terms: D000818:Animals; D015815:Cell Adhesion Molecules / Q000172:deficiency / Q000494:pharmacology / Q000502:physiology*; D002465:Cell Movement / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D002478:Cells, Cultured; D020405:Dermis / Q000293:injuries* / Q000473:pathology; D005347:Fibroblasts / Q000473:pathology*; D066298:In Vitro Techniques; D016023:Integrins / Q000502:physiology; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D020929:Mitogen-Activated Protein Kinase Kinases / Q000502:physiology; D023421:Models, Animal; D015398:Signal Transduction / Q000502:physiology; D015854:Up-Regulation / Q000502:physiology; D014945:Wound Healing / Q000502:physiology*
chemical_list: D015815:Cell Adhesion Molecules; D016023:Integrins; C082838:Postn protein, mouse; D020929:Mitogen-Activated Protein Kinase Kinases