fibermatrixadhesion

Fibermatrix adhesion describes the adhesive interactions between cells and fibrous extracellular matrix (ECM) networks, as well as the bonding between fibers within a matrix and between a matrix and implanted biomaterials. In most tissues, the fibrous ECM is dominated by collagen fibers linked with other proteins such as fibronectin and elastin, forming a three-dimensional scaffold that carries mechanical loads and presents signaling cues to resident cells.

Molecular basis: Cell attachment to fibrous ECM is primarily mediated by integrin receptors that bind specific ECM ligands (for example, integrin α5β1–fibronectin, α1β1–collagen). Intracellular adaptor proteins (talin, kindlin, vinculin) couple activated integrins to the actin cytoskeleton, assembling focal adhesions. Adhesion strength and signaling are modulated by ECM composition, fiber alignment, crosslinking, and matrix stiffness. ECM remodeling enzymes (matrix metalloproteinases) and crosslinking enzymes (lysyl oxidase) alter adhesion landscapes by changing fiber architecture and stiffness, influencing cell fate and migration.

Biological significance: Fibermatrix adhesion is essential for tissue development, maintenance, and repair. Proper adhesion enables cell migration during morphogenesis, stable tissue architecture, and directed wound healing. Aberrant adhesion is linked to pathology, including fibrosis, cancer cell invasion, and impaired healing.

Measurement and applications: Researchers assess fibermatrix adhesion with cell adhesion assays, immunostaining of focal adhesion markers, traction force microscopy, and assays of integrin activation. In tissue engineering, designing fibrous scaffolds aims to mimic native adhesion cues to guide cell behavior.