| pubmed-article:8106553 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C0328767 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C0017973 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C0106158 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C0040690 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C0004266 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C1517880 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C1551336 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C1709060 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C1554184 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C1283195 | lld:lifeskim |
| pubmed-article:8106553 | lifeskim:mentions | umls-concept:C0444454 | lld:lifeskim |
| pubmed-article:8106553 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8106553 | pubmed:dateCreated | 1994-3-24 | lld:pubmed |
| pubmed-article:8106553 | pubmed:abstractText | Betaglycan, also known as the TGF-beta type III receptor, is a membrane-anchored proteoglycan that presents TGF-beta to the type II signaling receptor, a transmembrane serine/threonine kinase. The betaglycan extracellular region, which can be shed by cells into the medium, contains a NH2-terminal domain related to endoglin and a COOH-terminal domain related to uromodulin, sperm receptors Zp2 and 3, and pancreatic secretory granule GP-2 protein. We identified residues Ser535 and Ser546 in the uromodulin-related region as the glycosaminoglycan (GAG) attachment sites. Their mutation to alanine prevents GAG attachment but does not interfere with betaglycan stability or ability to bind and present TGF-beta to receptor II. Using a panel of deletion mutants, we found that TGF-beta binds to the NH2-terminal endoglin-related region of betaglycan. The remainder of the extracellular domain and the cytoplasmic domain are not required for presentation of TGF-beta to receptor II; however, membrane anchorage is required. Soluble betaglycan can bind TGF-beta but does not enhance binding to membrane receptors. In fact, recombinant soluble betaglycan acts as potent inhibitor of TGF-beta binding to membrane receptors and blocks TGF-beta action, this effect being particularly pronounced with the TGF-beta 2 isoform. The results suggest that release of betaglycan into the medium converts this enhancer of TGF-beta action into a TGF-beta antagonist. | lld:pubmed |
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| pubmed-article:8106553 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8106553 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8106553 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8106553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8106553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8106553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8106553 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8106553 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8106553 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8106553 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:8106553 | pubmed:author | pubmed-author:MassaguéJJ | lld:pubmed |
| pubmed-article:8106553 | pubmed:author | pubmed-author:AndrewJ HJH | lld:pubmed |
| pubmed-article:8106553 | pubmed:author | pubmed-author:López-Casilla... | lld:pubmed |
| pubmed-article:8106553 | pubmed:author | pubmed-author:PayneH MHM | lld:pubmed |
| pubmed-article:8106553 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8106553 | pubmed:volume | 124 | lld:pubmed |
| pubmed-article:8106553 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8106553 | pubmed:authorsComplete | Y | lld:pubmed |
