Abstract
Among the proteins of the animal organism, fibronectin (FN) occupies a special place due to the exceptional diversity and importance of biological properties. In 1948, Morrison et al. [69] for the first time it was discovered as part of the I fraction of blood plasma by Cohn, but interest in FN increased rapidly only in the 70s after its identification with one of the proteins of the outer cell membrane. At various times, FN has been described under numerous names that determined any property of this protein or its localization, for example, large external transformation-sensitive (LETS) protein, cold-insoluble globulin, cell adhesion factor, opsonic a2-SB-glycoprotein, anti-gelatin factor, etc. Currently, these names are almost not used, and the term "fibronectin" (fibra fiber, nectere bind) is adopted to refer to all forms of this protein cellular and extracellular, soluble and membrane-associated cells that form a population of immunologically related molecules with some differences in physicochemical and biological properties.
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