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Periostin, originally named as osteoblast-specific factor-2 (Osf2) (genebank D13664), was first identified in bone and is implicated in regulating adhesion and differentiation of osteoblasts. Periostin is a secreted protein that shares a structural homology to the axon guidance protein fasciclin I (FAS1) in insects. Proteins that share homology with FAS1 include βig-h3, stablin I and II, MBP-70, Algal-CAM, Periostin, and Periostin-like factor (PLF). An approximately 90 kDa periostin has an NH2-terminal secretory signal peptide, followed by a cysteine-rich domain, four internal homologous repeats, and a COOH-terminal hydrophilic domain. In N-terminus, periostin has an EMI domain, which is a small cysteine-rich module of approximately 75 amino acids. Periostin binds to αvβ3, αvβ5, and α6β4 Integrins, fibronection, tenacin-C, collagen V, and periostin itself. Mouse and human periostingene (POSTN) share 89.2% amino acid identity...
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Takeshita S, Kikuno R, Tezuka K et al (1993) Osteoblast-specific factor 2: cloning of a putative bone adhesion protein with homology with the insect protein fasciclin I. Biochem J 294:271–278
Gillan L, Matei D, Fishman DA et al (2002) Periostin secreted by epithelial ovarian carcinoma is a ligand for alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell motility. Cancer Res 62:5358–5364
Bao S, Ouyang G, Bai X et al (2004) Periostin potently promotes metastatic growth of colon cancer by augmenting cell survival via the Akt/PKB pathway. Cancer Cell 5:329–339
Shao R, Bao S, Bai X et al (2004) Acquired expression of periostin by human breast cancers promotes tumor angiogenesis through up-regulation of vascular endothelial growth factor receptor 2 expression. Mol Cell Biol 24:3992–4003
Kudo Y, Ogawa I, Kitajima S et al (2006) Periostin promotes invasion and anchorage-independent growth in the metastatic process of head and neck cancer. Cancer Res 66:6928–6935
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© 2011 Springer-Verlag Berlin Heidelberg
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Kudo, Y., Takata, T. (2011). Periostin. In: Schwab, M. (eds) Encyclopedia of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16483-5_4450
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DOI: https://doi.org/10.1007/978-3-642-16483-5_4450
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Publisher Name: Springer, Berlin, Heidelberg
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Online ISBN: 978-3-642-16483-5
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