重组APC Anti-Periostin抗体[EPR19934]

补充信息

This supplementary information is collated from multiple sources and compiled automatically.

Periostin also known as POSTN or OSF-2 is an extracellular matrix protein with a molecular weight of approximately 90 kDa. It plays a mechanical role in tissue remodeling by binding to integrins which supports tissue repair and regeneration. Periostin is mainly expressed in collagen-rich tissues such as bone periodontal ligament and cardiac tissues. It is synthesized by osteoblasts fibroblasts and other stromal cells functioning as a structural protein that supports cell adhesion and migration.

Biological function summary

The periostin protein contributes to the maintenance of tissue integrity and mechanical properties. It does not solely act; it forms part of a multiprotein complex with collagen and other extracellular matrix components. This involvement is necessary for maintaining cellular interactions and promoting tissue healing processes. Additionally periostin influences cell proliferation and migration impacting developmental and wound healing biology.

Pathways

Periostin is involved in the integrin signaling pathway and the Wnt/β-catenin pathway both important for cell communication and movement. Through these pathways periostin interacts with integrins αvβ3 and αvβ5 facilitating cell adhesion and migration. The Wnt/β-catenin pathway interaction involves several proteins including Frizzled receptors ensuring regulation of cellular proliferation and differentiation. These pathways make periostin a coordinator of complex cellular processes.

The periostin protein is associated with conditions such as fibrotic diseases and cardiovascular disorders. In fibrosis periostin promotes collagen cross-linking exacerbating tissue stiffness. This involves increased interaction with proteins like collagen types I and V contributing to pathological fibrotic progression. In cardiovascular disorders elevated periostin levels after myocardial injury are linked with fibrotic scarring where it collaborates with matrix metalloproteinases to remodel the cardiac tissue architecture. Understanding these connections can lead to novel therapeutic strategies.