Structure[ edit ] Fibronectin exists as a protein dimer, consisting of two nearly identical polypeptide chains linked by a pair of C-terminal disulfide bonds. The absence of disulfide bonds in type III modules allows them to partially unfold under applied force.
It is present in most cellular fibronectin, but only one of the two subunits in a plasma fibronectin dimer contains a V-region sequence. The modules are arranged into several functional and protein -binding domains along the length of a fibronectin monomer.
There are four fibronectin-binding domains, allowing fibronectin to associate with other fibronectin molecules. Modules III9—10 correspond to the "cell-binding domain" of fibronectin. Cellular fibronectin is assembled into the extracellular matrixan insoluble network that separates and supports the organs and tissues of an organism.
Fibronectin plays a crucial role in wound healing. As repair of the injured tissue continues, fibroblasts and macrophages begin to remodel the area, degrading the proteins that form the provisional blood clot matrix and replacing them with a matrix that more resembles the normal, surrounding tissue.
Fibroblasts secrete proteasesincluding matrix metalloproteinasesthat digest the plasma fibronectin, and then the fibroblasts secrete cellular fibronectin and assemble it into an insoluble matrix.
Fragmentation of fibronectin by proteases has been suggested to promote wound contraction, a critical step in wound healing. Fibronectin is necessary for embryogenesisand inactivating the gene for fibronectin results in early embryonic lethality. In mammalian development, the absence of fibronectin leads to defects in mesodermalneural tubeand vascular development.
Similarly, the absence of a normal fibronectin matrix in developing amphibians causes defects in mesodermal patterning and inhibits gastrulation.
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The local concentration of integrin-bound fibronectin increases, allowing bound fibronectin molecules to more readily interact with one another. Short fibronectin fibrils then begin to form between adjacent cells. As matrix assembly proceeds, the soluble fibrils are converted into larger insoluble fibrils that comprise the extracellular matrix.
Cells are believed to stretch fibronectin by pulling on their fibronectin-bound integrin receptors. This force partially unfolds the fibronectin ligandunmasking cryptic fibronectin-binding sites and allowing nearby fibronectin molecules to associate.
This fibronectin-fibronectin interaction enables the soluble, cell-associated fibrils to branch and stabilize into an insoluble fibronectin matrix. A transmembrane protein, CD93, has been shown to be essential for fibronectin matrix assembly fibrillogenesis in human dermal blood endothelial cells.
Moreover, the CD93 knockout mice retinas displayed disrupted fibronectin matrix at the retinal sprouting front.
The adhesion of lung carcinoma cells to fibronectin enhances tumorigenicity and confers resistance to apoptosis -inducing chemotherapeutic agents.
Fibronectin has been shown to stimulate the gonadal steroids that interact with vertebrate androgen receptorswhich are capable of controlling the expression of cyclin D and related genes involved in cell cycle control.
Fibronectin 1 acts as a potential biomarker for radioresistance. During blood clotting, the fibronectin remains associated with the clot, covalently cross-linked to fibrin with the help of Factor XIII fibrin-stabilizing factor.
Fibroblast adhesion to fibrin requires fibronectin, and was strongest when the fibronectin was cross-linked to the fibrin.
Fibronectin promotes particle phagocytosis by both macrophages and fibroblasts. Collagen deposition at the wound site by fibroblasts takes place with the help of fibronectin.
Fibronectin was also observed to be closely associated with the newly deposited collagen fibrils. Based on the size and histological staining characteristics of the fibrils, it is likely that at least in part they are composed of type III collagen reticulin.日本健康会議では、経済産業省と共に年度の認定法人として大規模法人部門(ホワイト)法人、中小規模法人部門法人を認定しました。.
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