Endoglin
From Wikipedia, the free encyclopedia
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Endoglin (Osler-Rendu-Weber syndrome 1)
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| Identifiers | ||||||||||||||
| Symbol(s) | ENG; CD105; END; FLJ41744; HHT1; ORW; ORW1 | |||||||||||||
| External IDs | OMIM: 131195 MGI: 95392 HomoloGene: 92 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 2022 | 13805 | ||||||||||||
| Ensembl | ENSG00000106991 | ENSMUSG00000026814 | ||||||||||||
| Uniprot | P17813 | Q3UAM9 | ||||||||||||
| Refseq | NM_000118 (mRNA) NP_000109 (protein) |
NM_007932 (mRNA) NP_031958 (protein) |
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| Location | Chr 9: 129.62 - 129.66 Mb | Chr 2: 32.47 - 32.5 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]
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[edit] See also
[edit] References
- ^ a b Michelle Letarte. Structure and function of endoglin, a component of the TGF- beta receptor, etc. University of Toronto.
- ^ 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:. PMID 15148318.
- ^ 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:. PMID 16751767.
[edit] 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. PMID 9023056.
- Miyazono K (1997). "TGF-beta receptors and signal transduction.". Int. J. Hematol. 65 (2): 97–104. 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:. 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:. 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:. PMID 17210583.
