Fibronectin is a high molecular weight (about 440 kDa) glycoprotein of the extracellular matrix that binds to membrane-receptor proteins called integrins. Like integrins, fibronectin binds to extracellular matrix components such as collagen, fibrin, and heparan sulfate proteoglycans. Fibronectin exists as a protein dimer and consists of two nearly identical monomers linked by a pair of disulfide bonds. Fibronectin plays a major role in cell adhesion, growth, migration and differentiation, and is important for the process of wound healing and embryonic development. Altered fibronectin expression, degradation and tissue are associated with many pathologies, including cancer and fibrosis. Cell fibronectin assembles into an extracellular matrix, an insoluble network that separates and supports biological organs and tissues. Fibronectin plays a key role in wound healing. Together with fibrin, plasma fibronectin deposits on the site of injury, forming a blood clot, stopping bleeding and protecting the underlying tissue. In addition, fibronectin is important for guiding cell attachment and migration during embryonic development. In mammalian development, the lack of fibronectin causes defects in mesodermal, neural tube and vascular development. Fibronectin is also present in normal human saliva, which helps prevent the colonization of the mouth and pharynx by potentially pathogenic bacteria. Fibronectin has been involved in the development of cancer. In lung cancer, fibronectin expression increases, especially in non-small cell lung cancer. Adhesion of lung cancer cells to fibronectin enhances tumorigenicity and confers resistance to apoptosis-inducing chemotherapeutic agents. Radretumab is an anti-tumor drug. Its role is fibronectin.
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