Fibronectin: Difference between revisions
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== Fibronectin == | |||
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File:The_Modular_Structure_of_Fibronectin_and_its_Binding_Domains.png|The Modular Structure of Fibronectin and its Binding Domains | |||
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Latest revision as of 01:53, 17 February 2025
Fibronectin is a high-molecular weight (~440kDa) glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins. In addition to integrins, fibronectin also binds extracellular matrix components such as collagen, fibrin, and heparan sulfate proteoglycans (e.g. syndecans).
Structure[edit]
Fibronectin exists as a protein dimer, consisting of two nearly identical monomers linked by a pair of disulfide bonds. The fibronectin protein is produced from a single gene, but alternative splicing of its pre-mRNA leads to the creation of several isoforms.
Function[edit]
Fibronectin plays a crucial role in wound healing. Along with fibrin, fibronectin is essential to blood clotting. Following tissue injury, fibronectin is released into the wound site where it assists in platelet aggregation.
Clinical significance[edit]
Abnormal fibronectin levels have been associated with a number of health conditions, including cancer and fibrosis. In addition, fibronectin has been implicated in the pathogenesis of cardiovascular diseases due to its role in atherosclerotic lesion formation.
