Format

Send to:

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 2010 Jan 15;285(3):2028-39. doi: 10.1074/jbc.M109.051961. Epub 2009 Nov 3.

Incorporation of tenascin-C into the extracellular matrix by periostin underlies an extracellular meshwork architecture.

Author information

  • 1Department of Biological Information, Tokyo Institute of Technology, 4259 Midori-ku, Nagatsuta, Yokohama 226-8501.

Abstract

Extracellular matrix (ECM) underlies a complicated multicellular architecture that is subjected to significant forces from mechanical environment. Although various components of the ECM have been enumerated, mechanisms that evolve the sophisticated ECM architecture remain to be addressed. Here we show that periostin, a matricellular protein, promotes incorporation of tenascin-C into the ECM and organizes a meshwork architecture of the ECM. We found that both periostin null mice and tenascin-C null mice exhibited a similar phenotype, confined tibial periostitis, which possibly corresponds to medial tibial stress syndrome in human sports injuries. Periostin possessed adjacent domains that bind to tenascin-C and the other ECM protein: fibronectin and type I collagen, respectively. These adjacent domains functioned as a bridge between tenascin-C and the ECM, which increased deposition of tenascin-C on the ECM. The deposition of hexabrachions of tenascin-C may stabilize bifurcations of the ECM fibrils, which is integrated into the extracellular meshwork architecture. This study suggests a role for periostin in adaptation of the ECM architecture in the mechanical environment.

PMID:
19887451
[PubMed - indexed for MEDLINE]
PMCID:
PMC2804360
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk