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Tenascin-C is an extracellular matrix glycoprotein that is composed of 210-400 kDa subunits consisting of four domains. One subunit has a TA domain at the N-terminal end, then an epidermal growth factor-like sequence domain (EGF-like domain), a fibronectin type III (FN III) repeat domain, and a fibrinogen-like domain at the C-terminal end. There is an alternatively spliced domain in the FN III domain, and it generates some types of variants of tenascin-C. The subunits form a trimer by twisting at the N-terminal coiled domain and form a hexamer by a disulfide bond, in tissue. While low molecular weight variants of tenascin-C are present in normal tissue, it is said that high molecular weight variants of tenascin-C are expressed in various diseased tissue including cancer.
The tenascin C assay is a solid phase sandwich ELISA.
- Hsia HC, Schwarzbauer JE. Meet the tenascins: multifunctional and mysterious. J Biol Chem. 2005; 280:26641-26644.