Endoglin

Endoglin
Identifiers
Symbols	ENG; CD105; END; FLJ41744; HHT1; ORW; ORW1
External IDs	OMIM: 131195 MGI: 95392 HomoloGene: 92 GeneCards: ENG Gene
Gene Ontology Molecular function • transmembrane receptor activity • transforming growth factor beta receptor activity • transforming growth factor beta receptor, cytoplasmic mediator activity • type II transforming growth factor beta receptor binding • type II transforming growth factor beta receptor binding • protein binding • protein binding • galactose binding • glycosaminoglycan binding • glycosaminoglycan binding • type I transforming growth factor beta receptor binding • type I transforming growth factor beta receptor binding • protein homodimerization activity • activin binding • transforming growth factor beta binding Cellular component • extracellular space • membrane fraction • external side of plasma membrane • cell surface • membrane • integral to membrane • transforming growth factor beta receptor complex Biological process • negative regulation of transcription from RNA polymerase II promoter • chronological cell aging • patterning of blood vessels • vasculogenesis • response to hypoxia • positive regulation of protein phosphorylation • negative regulation of endothelial cell proliferation • heart looping • positive regulation of systemic arterial blood pressure • regulation of transcription, DNA-dependent • cell adhesion • transforming growth factor beta receptor signaling pathway • transforming growth factor beta receptor signaling pathway • heart development • positive regulation of pathway-restricted SMAD protein phosphorylation • positive regulation of pathway-restricted SMAD protein phosphorylation • cell migration • regulation of transforming growth factor beta receptor signaling pathway • central nervous system vasculogenesis • extracellular matrix disassembly • regulation of cell adhesion • BMP signaling pathway • negative regulation of transforming growth factor beta receptor signaling pathway • positive regulation of BMP signaling pathway • negative regulation of protein autophosphorylation • wound healing • regulation of cell proliferation • regulation of phosphorylation • positive regulation of transcription from RNA polymerase II promoter • smooth muscle tissue development • artery morphogenesis • venous blood vessel morphogenesis • cell motility • negative regulation of nitric-oxide synthase activity • cell chemotaxis • negative regulation of pathway-restricted SMAD protein phosphorylation • detection of hypoxia Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2022	13805
Ensembl	ENSG00000106991	ENSMUSG00000026814
UniProt	P17813	Q3UAM9
RefSeq (mRNA)	NM_000118.2	NM_007932
RefSeq (protein)	NP_000109.1	NP_031958
Location (UCSC)	Chr 9: 130.58 – 130.62 Mb	Chr 2: 32.5 – 32.54 Mb
PubMed search	[1]	[2]

Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.

The protein consists of a homodimer of 180 kDA with disulfide links. ^[1] It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells.

Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. ^[2] Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.^[2]

In humans endoglin may be involved in the autosomal dominant disorder known as hereditary hemorrhagic telangiectasia type 1.^[1] This condition leads to frequent nose bleeds, telangiectases on skin and mucosa and may cause arteriovenous malformations in different organs including brain, lung, and liver.

Endoglin levels have been found to be elevated in pregnant women who subsequently develop preeclampsia.^[3]

Interactions

Endoglin has been shown to interact with TGF beta receptor 2^[4][5] and TGF beta receptor 1.^[4][5]

See also

• Cluster of differentiation

References

1. ^ ^{a b} Michelle Letarte. "Structure and function of endoglin, a component of the TGF- beta receptor, etc". University of Toronto. Archived from the original on 2006-09-29. http://web.archive.org/web/20060929141224/http://www.immunology.utoronto.ca/English/Structure-and-function-of-endoglin-a-component-of-the-TGF--beta-receptor-expressed-on-endothelial-cells-and-activated-monocytes-and-the-target-gene-for-the-vascular-dominant-genetic-disorderetc.html. Retrieved 2006-08-28. 
2. ^ ^{a b} Sanz-Rodriguez, Francisco; Mercedes Guerrero-Esteo, Luisa-Maria Botella, Denis Banville (2004). "Endoglin Regulates Cytoskeletal Organization through Binding to ZRP-1, a Member of the Lim Family of Proteins". J. Biol. Chem. 279 (31): 32858–68. doi:10.1074/jbc.M400843200. PMID 15148318. 
3. ^ Venkatesha, S; Toporsian M, Lam C, Hanai J, Mammoto T, Kim YM, Bdolah Y, Lim KH, Yuan HT, Libermann TA, Stillman IE, Roberts D, D'Amore PA, Epstein FH, Sellke FW, Romero R, Sukhatme VP, Letarte M, Karumanchi SA. (2006). "Soluble endoglin contributes to the pathogenesis of preeclampsia". Nat Med 12 (6): 642–9. doi:10.1038/nm1429. PMID 16751767. 
4. ^ ^{a b} Guerrero-Esteo, Mercedes; Sanchez-Elsner Tilman, Letamendia Ainhoa, Bernabeu Carmelo (Aug. 2002). "Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II". J. Biol. Chem. (United States) 277 (32): 29197–209. doi:10.1074/jbc.M111991200. ISSN 0021-9258. PMID 12015308. 
5. ^ ^{a b} Barbara, N P; Wrana J L, Letarte M (Jan. 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". J. Biol. Chem. (UNITED STATES) 274 (2): 584–94. doi:10.1074/jbc.274.2.584. ISSN 0021-9258. PMID 9872992. 

Further reading

• Attisano L, Wrana JL (1997). "Signal transduction by members of the transforming growth factor-beta superfamily.". Cytokine Growth Factor Rev. 7 (4): 327–39. doi:10.1016/S1359-6101(96)00042-1. PMID 9023056. 
• Miyazono K (1997). "TGF-beta receptors and signal transduction.". Int. J. Hematol. 65 (2): 97–104. doi:10.1016/S0925-5710(96)00542-7. PMID 9071813. 
• Fonsatti E, Altomonte M, Nicotra MR, et al. (2003). "Endoglin (CD105): a powerful therapeutic target on tumor-associated angiogenetic blood vessels.". Oncogene 22 (42): 6557–63. doi:10.1038/sj.onc.1206813. PMID 14528280. 
• Luft FC (2007). "Soluble endoglin (sEng) joins the soluble fms-like tyrosine kinase (sFlt) receptor as a pre-eclampsia molecule.". Nephrol. Dial. Transplant. 21 (11): 3052–4. doi:10.1093/ndt/gfl439. PMID 16870672. 
• López-Novoa JM (2007). "Soluble endoglin is an accurate predictor and a pathogenic molecule in pre-eclampsia.". Nephrol. Dial. Transplant. 22 (3): 712–4. doi:10.1093/ndt/gfl768. PMID 17210583. 
• Blázquez-Medela AM, García-Ortiz L, Gómez-Marcos MA, Recio-Rodríguez JI, Sánchez-Rodríguez A, López-Novoa JM, Martínez-Salgado C (2010). "Increased plasma soluble endoglin levels as an indicator of cardiovascular alterations in hypertensive and diabetic patients". BMC Med 8: 86. doi:10.1186/1741-7015-8-86. PMC 3012013. PMID 21171985. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3012013. 

External links

• MeSH CD105+Antigen