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endoglin

approved gene symbol: ENG. Abbr. also: Edg.

The primary structure of endoglin as deduced from the cloned cDNA suggests a type 1 integral membrane protein with an extracellular domain of 561 amino acids, a membrane-spanning region of 25 amino acids, and a cytoplasmic tail of 47 amino acids (Gougos and Letarte, 1990). Two alternative splice variants of endoglin have been described. L-endoglin (long form) is the predominant isoform and possesses a cytoplasmic tail of 47 residues. The minor isoform, S-endoglin, contains a cytoplasmic tail of only 14 amino acids (Bellon et al, 1993; Perez-Gomez et al, 2005).

Endoglin has been shown to be a component of the TGF-beta receptor system in human endothelial cells (Cheifetz et al, 1992). Yamashita et al (1994) have shown that endoglin forms heteromeric complexes with TGF-beta receptors. Parker et al have shown that endoglin is expressed on human chondrocytes at levels comparable with endothelial cells and that it forms higher order complexes with both TGF-beta receptors and also with betaglycan. The formation of complexes between endoglin and betaglycan can occur independently of the type 2 TGF-beta receptor.

Lebrin et al (2004) have shown that endoglin plays a pivotal role in the balance of ALK1 and ALK5 signalling to regulate endothelial cell proliferation in response to TGF-beta. Scherner et al (2007) have shown that endoglin inhibits TGF-beta-1 signalling pathways but enhances signalling pathways involving BMP7 and SMAD1, SMAD5.

Both isoforms of endoglin have the capacity to bind ligand (Bellon et al, 1993). They differ in their level of phosphorylation (Lastres et al, 1994), and in their capacity to regulate some cellular responses dependent on TGF-beta (Lastres et al, 1996; Velasco et al, 2008). Velasco et al (2008) have shown, for example, that in myoblasts L-endoglin decreases collagen type 1 and CTGF expression in response to TGF-beta-1 and increases cell proliferation, whereas S-endoglin strongly increases collagen type 1 and CTGF expression in response to TGF-beta-1 and reduces cell proliferation in response to TGF-beta-1.

Mutations in the endoglin gene have been shown to be responsible for hereditary haemorrhagic telangiectasia type 1 (see: HHT1), or Rendu-Osler-Weber syndrome (reviewed by Shovlin, 2010).

In the nomenclature of CD antigens this protein has been given the designation CD105.

For additional information on CD antigens see also: CD antigens MiniCOPE Dictionary.


Copyright 2012 by H IBELGAUFTS. All rights reserved.
ENTRY LAST MODIFIED: January 2010



 

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