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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1994-2-25
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/ENG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transforming Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transforming Growth Factor beta,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Cell Adhesion Molecule-1
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1995-2001
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8294451-Amino Acid Sequence,
pubmed-meshheading:8294451-Animals,
pubmed-meshheading:8294451-Antigens, CD,
pubmed-meshheading:8294451-Aorta,
pubmed-meshheading:8294451-Base Sequence,
pubmed-meshheading:8294451-Cloning, Molecular,
pubmed-meshheading:8294451-DNA, Complementary,
pubmed-meshheading:8294451-Endothelium, Vascular,
pubmed-meshheading:8294451-Female,
pubmed-meshheading:8294451-Gene Library,
pubmed-meshheading:8294451-Humans,
pubmed-meshheading:8294451-Macromolecular Substances,
pubmed-meshheading:8294451-Membrane Glycoproteins,
pubmed-meshheading:8294451-Molecular Sequence Data,
pubmed-meshheading:8294451-Phosphorylation,
pubmed-meshheading:8294451-Protein Biosynthesis,
pubmed-meshheading:8294451-Receptors, Cell Surface,
pubmed-meshheading:8294451-Receptors, Transforming Growth Factor beta,
pubmed-meshheading:8294451-Recombinant Proteins,
pubmed-meshheading:8294451-Sequence Homology, Amino Acid,
pubmed-meshheading:8294451-Signal Transduction,
pubmed-meshheading:8294451-Swine,
pubmed-meshheading:8294451-Transforming Growth Factor beta,
pubmed-meshheading:8294451-Uterus,
pubmed-meshheading:8294451-Vascular Cell Adhesion Molecule-1
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pubmed:year |
1994
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pubmed:articleTitle |
Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta.
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pubmed:affiliation |
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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