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Journal of Cell Communication and Signaling

, Volume 12, Issue 1, pp 301–308 | Cite as

Periostin function in communication with extracellular matrices

  • Akira Kudo
  • Isao Kii
Review

Abstract

Periostin is a secretory protein with a multi-domain structure, comprising an amino-terminal cysteine-rich EMI domain, four internal FAS 1 domains, and a carboxyl-terminal hydrophilic domain. These adjacent domains bind to extracellular matrix proteins (type I collagen, fibronectin, tenascin-C, and laminin γ2), and BMP-1 that catalyzes crosslinking of type I collagen, and proteoglycans, which play a role in cell adhesion. The binding sites on periostin have been demonstrated to contribute to the mechanical strength of connective tissues, enhancing intermolecular interactions in close proximity and their assembly into extracellular matrix architectures, where periostin plays further essential roles in physiological maintenance and pathological progression. Furthermore, periostin also binds to Notch 1 and CCN3, which have functions in maintenance of stemness, thus opening up a new field of periostin action.

Keywords

Periostin ECM EMI FAS 1 Fibronectin Tenascin Collagen BMP-1 CCN3 

Notes

Acknowledgements

We thank K. Yoshikawa in Aqua Therapeutics Co. for providing information. This work was supported by the Project for Cancer Research and Therapeutic Evolution (P-CREATE) (IK) from the Japan Agency for Medical Research and Development (AMED).

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© The International CCN Society 2017

Authors and Affiliations

  1. 1.International FrontierTokyo Institute of TechnologyTokyoJapan
  2. 2.Showa UniversityTokyoJapan
  3. 3.Common Facilities Unit, Integrated Research Group, Compass to Healthy Life Research Complex ProgramRIKEN Cluster for Science and Technology HubKobeJapan
  4. 4.Pathophysiological and Health Science Team, Imaging Platform and Innovation Group, Division of Bio-Function Dynamics ImagingRIKEN Center for Life Science TechnologiesKobeJapan

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