Tenascin/tenascin/tenascins/Tenascins
The tenascins are a highly conserved family of large oligomeric glycoproteins found in the extracellular matrix of vertebrate organisms. Two decades ago, the molecule now known as tenascin-C was among the first proteins shown to have an adhesion modulatory role antagonizing cell attachment to fibronectin. Cells that normally demonstrate a stationary phenotype on the fibronectin-containing matrix by spreading out and forming cortical actin stress fibers will show morphological changes when tenascin-C is included in the matrix by extending membrane protrusions and exhibiting decreased stress fiber formation, characteristics more typical of a migratory phenotype. There are currently four tenascin paralogues that have been identified in mammals, each designated with a letter derived, for the most part, from earlier eponyms : C, R, X, and W. Although each type has a distinctive expression pattern, the tenascins share the characteristic of having tightly regulated expression during development and throughout an organism’s life. Tenascins also share the characteristic of modulating cell-matrix interactions and mediating a state of matrix attachment that promotes motility while also influencing other cell functions. As such, this protein family has important functions not only during development but also during pathological states in the adult such as tissue injury and tumorigenesis where remodeling processes are promoted.
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