The fibronectin type III domain from human tenascin, colored from blue (N-terminus) to red (C-terminus).[1]

Tenascins are extracellular matrix glycoproteins. They are abundant in the extracellular matrix of developing vertebrate embryos and they reappear around healing wounds and in the stroma of some tumors.


There are four members of the tenascin gene family: tenascin-C, tenascin-R, tenascin-X and tenascin-W.

The basic structure is 14 EGF-like repeats towards the N-terminal end, and 8 or more fibronectin-III domains which vary upon species and variant.

Tenascin-C is the most intensely studied member of the family. It has anti-adhesive properties, causing cells in tissue culture to become rounded after it is added to the medium. One mechanism to explain this may come from its ability to bind to the extracellular matrix glycoprotein fibronectin and block fibronectin's interactions with specific syndecans. The expression of tenascin-C in the stroma of certain tumors is associated with a poor prognosis.


  1. ^ PDB: 1TEN​; Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP (November 1992). "Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein". Science. 258 (5084): 987–91. doi:10.1126/science.1279805. PMID 1279805.
  2. ^ Bristow J, Carey W, Egging D, Schalkwijk J (2005). "Tenascin-X, collagen, elastin, and the Ehlers-Danlos syndrome". Am J Med Genet C Semin Med Genet. 139 (1): 24–30. doi:10.1002/ajmg.c.30071. PMID 16278880.

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