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The integrin–extracellular matrix (ECM) interface between periodontal ligament stem cells (PDLSCs) and the host or preserved ECM is a fundamental biological system governing periodontal tissue repair and regeneration. Integrins, a family of heterodimeric transmembrane receptors, serve as the primary link between the PDLSC cytoskeleton and the surrounding ECM proteins such as collagen, laminin, and fibronectin (Hynes, 2002, Cell). This physical connection facilitates mechanotransduction and activates vital signaling pathways, including the Focal Adhesion Kinase (FAK) and Mitogen-Activated Protein Kinase (MAPK) cascades, which dictate cell fate and osteogenic potential (Chen et al., 2016, J Periodontal Res). In the context of periodontitis or alveolar bone loss, therapeutic strategies often focus on optimizing this interface by using decellularized ECM scaffolds or functionalizing synthetic materials with adhesion motifs like RGD peptides to promote PDLSC recruitment and integration (Seo et al., 2004, Lancet; Zhang et al., 2018, Stem Cells Int). While not a single molecular target, this interface is a focal point for bioengineering efforts aimed at restoring the functional attachment of the tooth to the alveolar bone. Understanding the specific integrin subunits involved, such as alpha-2 and beta-1, is critical for developing targeted regenerative therapies in dentistry.
Modulation of integrin-mediated signaling pathways (e.g., FAK, ERK, and PI3K/Akt) to enhance cell attachment, survival, and osteogenic differentiation on biological or synthetic scaffolds.
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