fbpx
Wikipedia

Tenascin

January 01, 1970

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.

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

Types edit

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.

References edit

  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.
  • Chiquet-Ehrismann R, Chiquet M (2003). "Tenascins: regulation and putative functions during pathological stress". J Pathol. 200 (4): 488–99. doi:10.1002/path.1415. PMID 12845616.
  • Chiquet-Ehrismann R, Tucker R (2004). "Connective tissues: signalling by tenascins". Int J Biochem Cell Biol. 36 (6): 1085–9. doi:10.1016/j.biocel.2004.01.007. PMID 15094123.
  • Hsia H, Schwarzbauer J (2005). "Meet the tenascins: multifunctional and mysterious". J Biol Chem. 280 (29): 26641–4. doi:10.1074/jbc.R500005200. PMID 15932878.
  • Jones F, Jones P (2000). "The tenascin family of ECM glycoproteins: structure, function, and regulation during embryonic development and tissue remodeling". Dev Dyn. 218 (2): 235–59. doi:10.1002/(SICI)1097-0177(200006)218:2<235::AID-DVDY2>3.0.CO;2-G. PMID 10842355.

External links edit

January 01, 1970
tenascin, extracellular, matrix, glycoproteins, they, abundant, extracellular, matrix, developing, vertebrate, embryos, they, reappear, around, healing, wounds, stroma, some, tumors, fibronectin, type, domain, from, human, tenascin, colored, from, blue, termin. 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 The fibronectin type III domain from human tenascin colored from blue N terminus to red C terminus 1 Types editThere are four members of the tenascin gene family tenascin C tenascin R tenascin X and tenascin W Tenascin C is the founding member of the gene family In the embryo it is made by migrating cells like the neural crest it is also abundant in developing tendons bone and cartilage Tenascin R is found in the developing and adult nervous system Tenascin X is found primarily in loose connective tissue mutations in the human tenascin X gene can lead to a form of Ehlers Danlos syndrome 2 Tenascin W is found in the kidney and in developing bone 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 References edit 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 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 Chiquet Ehrismann R Chiquet M 2003 Tenascins regulation and putative functions during pathological stress J Pathol 200 4 488 99 doi 10 1002 path 1415 PMID 12845616 Chiquet Ehrismann R Tucker R 2004 Connective tissues signalling by tenascins Int J Biochem Cell Biol 36 6 1085 9 doi 10 1016 j biocel 2004 01 007 PMID 15094123 Hsia H Schwarzbauer J 2005 Meet the tenascins multifunctional and mysterious J Biol Chem 280 29 26641 4 doi 10 1074 jbc R500005200 PMID 15932878 Jones F Jones P 2000 The tenascin family of ECM glycoproteins structure function and regulation during embryonic development and tissue remodeling Dev Dyn 218 2 235 59 doi 10 1002 SICI 1097 0177 200006 218 2 lt 235 AID DVDY2 gt 3 0 CO 2 G PMID 10842355 External links editTenascin at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Tenascin amp oldid 1221971763, wikipedia, wiki, book, books, library,

article

, read, download, free, free download, mp3, video, mp4, 3gp, jpg, jpeg, gif, png, picture, music, song, movie, book, game, games.