Periostin, a matricellular protein, accelerates cutaneous wound repair by activating dermal fibroblasts

Kanako Ontsuka, Yorihisa Kotobuki, Hiroshi Shiraishi, Satoshi Serada, Shoichiro Ohta, Atsushi Tanemura, Lingli Yang, Minoru Fujimoto, Kazuhiko Arima, Shoichi Suzuki, Hiroyuki Murota, Shuji Toda, Akira Kudo, Simon Conway, Yutaka Narisawa, Ichiro Katayama, Kenji Izuhara, Tetsuji Naka

Research output: Contribution to journalArticle

69 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)331-336
Number of pages6
JournalExperimental Dermatology
Volume21
Issue number5
DOIs
StatePublished - May 2012

Fingerprint

Fibroblasts
Repair
Skin
Wounds and Injuries
Proteins
Integrins
Phosphatidylinositol 3-Kinase
Tissue
Molecules
Granulation
Granulation Tissue
Cell Lineage
Cell Communication
Phosphotransferases

Keywords

  • Fibroblast
  • Matrix
  • Mice
  • Periostin - integrin
  • Wound repair

ASJC Scopus subject areas

  • Dermatology
  • Molecular Biology
  • Biochemistry

Cite this

Ontsuka, K., Kotobuki, Y., Shiraishi, H., Serada, S., Ohta, S., Tanemura, A., ... Naka, T. (2012). Periostin, a matricellular protein, accelerates cutaneous wound repair by activating dermal fibroblasts. Experimental Dermatology, 21(5), 331-336. https://doi.org/10.1111/j.1600-0625.2012.01454.x

Periostin, a matricellular protein, accelerates cutaneous wound repair by activating dermal fibroblasts. / Ontsuka, Kanako; Kotobuki, Yorihisa; Shiraishi, Hiroshi; Serada, Satoshi; Ohta, Shoichiro; Tanemura, Atsushi; Yang, Lingli; Fujimoto, Minoru; Arima, Kazuhiko; Suzuki, Shoichi; Murota, Hiroyuki; Toda, Shuji; Kudo, Akira; Conway, Simon; Narisawa, Yutaka; Katayama, Ichiro; Izuhara, Kenji; Naka, Tetsuji.

In: Experimental Dermatology, Vol. 21, No. 5, 05.2012, p. 331-336.

Research output: Contribution to journalArticle

Ontsuka, K, Kotobuki, Y, Shiraishi, H, Serada, S, Ohta, S, Tanemura, A, Yang, L, Fujimoto, M, Arima, K, Suzuki, S, Murota, H, Toda, S, Kudo, A, Conway, S, Narisawa, Y, Katayama, I, Izuhara, K & Naka, T 2012, 'Periostin, a matricellular protein, accelerates cutaneous wound repair by activating dermal fibroblasts', Experimental Dermatology, vol. 21, no. 5, pp. 331-336. https://doi.org/10.1111/j.1600-0625.2012.01454.x
Ontsuka, Kanako ; Kotobuki, Yorihisa ; Shiraishi, Hiroshi ; Serada, Satoshi ; Ohta, Shoichiro ; Tanemura, Atsushi ; Yang, Lingli ; Fujimoto, Minoru ; Arima, Kazuhiko ; Suzuki, Shoichi ; Murota, Hiroyuki ; Toda, Shuji ; Kudo, Akira ; Conway, Simon ; Narisawa, Yutaka ; Katayama, Ichiro ; Izuhara, Kenji ; Naka, Tetsuji. / Periostin, a matricellular protein, accelerates cutaneous wound repair by activating dermal fibroblasts. In: Experimental Dermatology. 2012 ; Vol. 21, No. 5. pp. 331-336.
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