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Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta.
Open accessAbstract
Human endoglin is a dimeric protein that binds transforming growth factor-beta (TGF-beta). A porcine cDNA clone for endoglin was obtained from a porcine uterus cDNA library. The deduced sequence of the primary translated product of endoglin consists of 643 amino acids with a high sequence identity (96%) to human endoglin in the transmembrane and intracellular domains, but with a lower sequence similarity (66%) in the extracellular domain. In contrast to human endoglin, porcine endoglin has no Arg-Gly-Asp tripeptide in its sequence. Antibodies, raised against a peptide corresponding to the intracellular domain of porcine endoglin, immunoprecipitated an 84-kDa protein under reducing condition and a 130-kDa protein under nonreducing condition in porcine aortic endothelial cells. Porcine endoglin bound TGF-beta 1 and -beta 3 efficiently, but TGF-beta 2 less efficiently. Endoglin was found to be coimmunoprecipitated with TGF-beta receptors type I and/or II by the endoglin antibodies or by TGF-beta receptor II antibodies in the presence of ligand. Thus, endoglin and TGF-beta receptors I and/or II most likely formed a heteromeric receptor complex. Endoglin was phosphorylated on serine residue(s), which did not change after stimulation by TGF-beta 1. These results revealed that endoglin is a phosphorylated protein which forms a heteromeric complex with signaling receptors for TGF-beta.
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Metadata
- Authors
- Yamashita, H., Ichijo, H., Grimsby, S., Morén, A., ten Dijke, P., & Miyazono, K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-01
- Volume
- 269
- Issue
- 3
- Pages
- 1995-2001
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1568363145
- Cited by
- 194
- References
- 1
- FWCI
- 4.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 9797 d)
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- Yamashita, H., Ichijo, H., Grimsby, S., Morén, A., ten Dijke, P., & Miyazono, K. (1994). Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)42126-0
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