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Periostin modulates myofibroblast differentiation during full-thickness cutaneous wound repair

Elliott, Christopher G. and Wang, Jian and Guo, Xiaolei and Xu, Shi-wen and Eastwood, Mark and Guan, Jianjun and Leask, Andrew and Conway, Simon J. and Hamilton, Douglas W. (2012) Periostin modulates myofibroblast differentiation during full-thickness cutaneous wound repair. Journal of Cell Science, 125 (1). pp. 121-132. ISSN 0021-9533

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Official URL: http://dx.doi.org/10.1242/jcs.087841

Abstract

The matricellular protein periostin is expressed in the skin. Although periostin has been hypothesized to contribute to dermal homeostasis and repair, this has not been directly tested. To assess the contribution of periostin to dermal healing, 6 mm full-thickness excisional wounds were created in the skin of periostin-knockout and wild-type, sex-matched control mice. In wild-type mice, periostin was potently induced 5–7 days after wounding. In the absence of periostin, day 7 wounds showed a significant reduction in myofibroblasts, as visualized by expression of α-smooth muscle actin (α-SMA) within the granulation tissue. Delivery of recombinant human periostin by electrospun collagen scaffolds restored α-SMA expression. Isolated wild-type and knockout dermal fibroblasts did not differ in in vitro assays of adhesion or migration; however, in 3D culture, periostin-knockout fibroblasts showed a significantly reduced ability to contract a collagen matrix, and adopted a dendritic phenotype. Recombinant periostin restored the defects in cell morphology and matrix contraction displayed by periostin-deficient fibroblasts in a manner that was sensitive to a neutralizing anti-β1-integrin and to the FAK and Src inhibitor PP2. We propose that periostin promotes wound contraction by facilitating myofibroblast differentiation and contraction.

Item Type:Article
Research Community:University of Westminster > Life Sciences, School of
ID Code:11266
Deposited On:23 Oct 2012 13:46
Last Modified:23 Oct 2012 13:47

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