Tenascin

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

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.

Contents

Types

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.

Related Research Articles

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<span class="mw-page-title-main">TENM3</span> Protein-coding gene in the species Homo sapiens

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Ruth Chiquet-Ehrismann was a Swiss biochemist and cell biologist working on interactions in the extracellular matrix.

RCCX is a complex, multiallelic, and tandem copy number variation (CNV) human DNA locus on chromosome 6p21.3, a cluster located in the major histocompatibility complex (MHC) class III region. CNVs are segments of DNA that vary in copy number compared to a reference genome and play a significant role in human phenotypic variation and disease development. The RCCX cluster consists of one or more modules each having a series of genes close to each other: serine/threonine kinase 19 (STK19), complement 4 (C4), steroid 21-hydroxylase (CYP21), and tenascin-X (TNX).

References

  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.