Periostin protein (POSTN)

Periostin is a secreted extracellular matrix protein encoded by the POSTN gene, classified as a matricellular protein and a member of the fasciclin 1 family[1][2][4][5]. It is characterized by a multi-domain structure including an EMI domain, four FAS1 domains, and a C-terminal region which is subject to alternative splicing, leading to various isoforms with tissue/disease-dependent functions[2][5]. Periostin binds to integrins such as αvβ3 and αvβ5, supporting cell adhesion, migration, and survival[1][3][6]. It plays essential roles in collagen assembly, ECM organization, and tissue remodeling and is transiently upregulated during injury, development, and pathological changes such as cancer, fibrosis, and inflammatory diseases[1][4][7]. Periostin's involvement in epithelial-mesenchymal transition, tumor invasion, metastasis, and tissue fibrosis makes it a promising diagnostic marker and potential therapeutic target, particularly in oncology, pulmonary, and fibrotic disorders[3][6][7].

Other names

Osteoblast-specific factor 2OSF-2PN

Drugs targeting periostin aim to inhibit its interaction with integrins (such as αvβ3, αvβ5), thereby reducing tumor growth, metastasis, fibrosis, or inflammation[1][6][3]. Antibodies or inhibitors may prevent periostin-mediated activation of the PI3K/Akt and FAK signaling pathways, block ECM remodeling, or limit EMT (epithelial-mesenchymal transition).