Periostin is an extracellular matrix protein required for eruption of incisors in mice.

A characteristic tooth of rodents, the incisor continuously grows throughout life by the constant formation of dentin and enamel. Continuous eruption of the incisor is accompanied with formation of shear zone, in which the periodontal ligament is remodeled. Although the shear zone plays a role in the remodeling, its molecular biological aspect is barely understood. Here, we show that periostin is essential for formation of the shear zone. Periostin-/- mice showed an eruption disturbance of incisors. Histological observation revealed that deletion of periostin led to disappearance of the shear zone. Electron microscopy revealed that the disappearance of the shear zone resulted from a failure in digestion of collagen fibers in the periostin-/- mice. Furthermore, immunohistochemical analysis using anti-periostin antibodies demonstrated the restricted localization of periostin protein in the shear zone. Periostin is an extracellular matrix protein, and immunoelectron microscopy showed a close association of periostin with collagen fibrils in vivo. These results suggest that periostin functions in the remodeling of collagen matrix in the shear zone.

[1]  B. Berkovitz.  Periodontal ligament: structural and clinical correlates. , 2004, Dental update.

[2]  Lynda F. Bonewald,et al.  Identification and Characterization of a Novel Protein, Periostin, with Restricted Expression to Periosteum and Periodontal Ligament and Increased Expression by Transforming Growth Factor β , 1999 .

[3]  V. Everts,et al.  Phagocytosis of fibronectin and collagens type I, III, and V by human gingival and periodontal ligament fibroblasts in vitro. , 2001, Journal of periodontology.

[4]  L. Creemers,et al.  Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling , 1996, The Histochemical Journal.

[5]  N. Amizuka,et al.  Immunohistochemical localization of periostin in tooth and its surrounding tissues in mouse mandibles during development. , 2004, The anatomical record. Part A, Discoveries in molecular, cellular, and evolutionary biology.

[6]  E. Hanssen,et al.  Covalent and non-covalent interactions of betaig-h3 with collagen VI. Beta ig-h3 is covalently attached to the amino-terminal region of collagen VI in tissue microfibrils. , 2003, The Journal of biological chemistry.

[7]  V. Everts,et al.  Fine structure and possible function of cells containing leptomergic organelles in the periodontal ligament of the rat incisor. , 1974, Archives of oral biology.

[8]  D. Fishman,et al.  Periostin secreted by epithelial ovarian carcinoma is a ligand for alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell motility. , 2002, Cancer research.

[9]  K. Moriyama,et al.  The divergent expression of periostin mRNA in the periodontal ligament during experimental tooth movement , 2003, Cell and Tissue Research.

[10]  Howard C. Tenenbaum,et al.  Phenotypic comparison of periodontal ligament cells in vivo and in vitro. , 2001, Journal of periodontal research.

[11]  Takeshi Kawamoto,et al.  Characterization of a cartilage-derived 66-kDa protein (RGD-CAP/beta ig-h3) that binds to collagen. , 1997, Biochimica et biophysica acta.

[12]  Ryan M. Anderson,et al.  Periostin potently promotes metastatic growth of colon cancer by augmenting cell survival via the Akt/PKB pathway. , 2004, Cancer cell.

[13]  V. Everts,et al.  The site of remodelling of collagen in the periodontal ligament of the mouse incisor , 1977, The Anatomical record.

[14]  K. Moriyama,et al.  Messenger RNA expression of periostin and Twist transiently decrease by occlusal hypofunction in mouse periodontal ligament. , 2005, Archives of oral biology.

[15]  R. Kikuno,et al.  Osteoblast-specific factor 2: cloning of a putative bone adhesion protein with homology with the insect protein fasciclin I. , 1993, The Biochemical journal.

[16]  G. Hendy,et al.  Cell-Specific Expression of the Parathyroid Hormone (PTH)/PTH-Related Peptide Receptor Gene in Kidney from Kidney-Specific and Ubiquitous Promoters1. , 1997, Endocrinology.

[17]  H. Mitani,et al.  Expression of MMP-8 and MMP-13 Genes in the Periodontal Ligament during Tooth Movement in Rats , 2003, Journal of dental research.

[18]  N. Amizuka,et al.  Zebrafish periostin is required for the adhesion of muscle fiber bundles to the myoseptum and for the differentiation of muscle fibers. , 2004, Developmental biology.

[19]  In‐San Kim,et al.  Identification of Motifs for Cell Adhesion within the Repeated Domains of Transforming Growth Factor-β-induced Gene,βig-h3 * , 2000, The Journal of Biological Chemistry.

[20]  Ryan M. Anderson,et al.  Acquired Expression of Periostin by Human Breast Cancers Promotes Tumor Angiogenesis through Up-Regulation of Vascular Endothelial Growth Factor Receptor 2 Expression , 2004, Molecular and Cellular Biology.

[21]  A. Bolcato-Bellemin,et al.  Expression of mRNAs Encoding for α and β Integrin Subunits, MMPs, and TIMPs in Stretched Human Periodontal Ligament and Gingival Fibroblasts , 2000 .

[22]  A. Kudo,et al.  Expression and characterization of murine osteoblast-specific factor 2 (OSF-2) in a baculovirus expression system. , 1995, Protein expression and purification.

[23]  Ghislaine Morvan Dubois,et al.  Structure and spatio temporal expression of the full length DNA complementary to RNA coding for alpha2 type I collagen of zebrafish. , 2002, Gene.

[24]  H. Shimauchi,et al.  Expression of MMP-8 and MMP-13 mRNAs in Rat Periodontium during Tooth Eruption , 2002, Journal of dental research.

[25]  Adam P. Summers,et al.  The evolution of tendon--morphology and material properties. , 2002, Comparative biochemistry and physiology. Part A, Molecular & integrative physiology.

[26]  T. Koob,et al.  Tendon--bridging the gap. , 2002, Comparative biochemistry and physiology. Part A, Molecular & integrative physiology.

[27]  J. Park,et al.  Identification of Motifs in the Fasciclin Domains of the Transforming Growth Factor-β-induced Matrix Protein βig-h3 That Interact with the αvβ5 Integrin* , 2002, The Journal of Biological Chemistry.