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Periostin contributes to the maturation and shape retention of tissue-engineered cartilage.


ABSTRACT: Traditional tissue-engineered cartilage applied in clinical practice consists of cell suspensions or gel-form materials for which it is difficult to maintain their shapes. Although biodegradable polymer scaffolds are used for shape retention, deformation after transplantation can occur. Here, we showed that periostin (PN), which is abundantly expressed in fibrous tissues, contributes to the maturation and shape retention of tissue-engineered cartilage through conformational changes in collagen molecules. The tissue-engineered cartilage transplanted in an environment lacking PN exhibited irregular shapes, while transplants originating from chondrocytes lacking PN showed limited regeneration. In the in vitro assay, PN added to the culture medium of chondrocytes failed to show any effects, while the 3D culture embedded within the collagen gel premixed with PN (10??g/mL) enhanced chondrogenesis. The PN-mediated collagen structure enhanced the mechanical strength of the surrounding fibrous tissues and activated chondrocyte extracellular signaling by interstitial fibrous tissues.

SUBMITTER: Inaki R 

PROVIDER: S-EPMC6060118 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

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Periostin contributes to the maturation and shape retention of tissue-engineered cartilage.

Inaki Ryoko R   Fujihara Yuko Y   Kudo Akira A   Misawa Masaki M   Hikita Atsuhiko A   Takato Tsuyoshi T   Hoshi Kazuto K  

Scientific reports 20180725 1


Traditional tissue-engineered cartilage applied in clinical practice consists of cell suspensions or gel-form materials for which it is difficult to maintain their shapes. Although biodegradable polymer scaffolds are used for shape retention, deformation after transplantation can occur. Here, we showed that periostin (PN), which is abundantly expressed in fibrous tissues, contributes to the maturation and shape retention of tissue-engineered cartilage through conformational changes in collagen m  ...[more]

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