| pubmed-article:15226301 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15226301 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:15226301 | lifeskim:mentions | umls-concept:C0023823 | lld:lifeskim |
| pubmed-article:15226301 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:15226301 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:15226301 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:15226301 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:15226301 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:15226301 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:15226301 | pubmed:issue | 37 | lld:pubmed |
| pubmed-article:15226301 | pubmed:dateCreated | 2004-9-6 | lld:pubmed |
| pubmed-article:15226301 | pubmed:abstractText | The type V TGF-beta receptor (TbetaR-V) plays an important role in growth inhibition by IGFBP-3 and TGF-beta in responsive cells. Unexpectedly, TbetaR-V was recently found to be identical to the LRP-1/alpha(2)M receptor; this has disclosed previously unreported growth regulatory functions of LRP-1. Here we demonstrate that, in addition to expressing LRP-1, all cells examined exhibit low affinity but high density acidic pH binding sites for LRP-1 growth regulatory ligands (TGF-beta(1), IGFBP-3, and alpha(2)M(*)). These sites, like LRP-1, are sensitive to receptor-associated protein and calcium depletion but, unlike LRP-1, are also sensitive to chondroitin sulfate and heparin and capable of directly binding ligands, which do not bind to LRP-1. Annexin VI has been identified as a major membrane-associated protein capable of directly binding alpha(2)M(*) at acidic pH. This is evidenced by: 1) structural and Western blot analyses of the protein purified from bovine liver plasma membranes by alpha(2)M(*) affinity column chromatography at acidic pH, and 2) dot blot analysis of the interaction of annexin VI and (125)I-alpha(2)M(*). Cell surface annexin VI is involved in (125)I-TGF-beta(1) and (125)I-alpha(2)M(*) binding to the acidic pH binding sites and (125)I-alpha(2)M(*) binding to LRP-1 at neutral pH as demonstrated by the sensitivity of cells to pretreatment with anti-annexin VI IgG. Cell surface annexin VI is also capable of mediating internalization and degradation of cell surface-bound (125)I-TGF-beta(1) and (125)I-alpha(2)M(*) at pH 6 and of forming ternary complexes with (125)I-alpha(2)M(*) and LRP-1 at neutral pH as demonstrated by co-immunoprecipitation. Trifluoperazine and fluphenazine, which inhibit ligand binding to the acidic pH binding sites, block degradation after internalization of cell surface-bound (125)I-TGF-beta(1) or (125)I-alpha(2)M(*). These results suggest that cell surface annexin VI may function as an acidic pH binding site or receptor and may also function as a co-receptor with LRP-1 at neutral pH. | lld:pubmed |
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| pubmed-article:15226301 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15226301 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15226301 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15226301 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15226301 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15226301 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15226301 | pubmed:author | pubmed-author:ChenChun-LinC... | lld:pubmed |
| pubmed-article:15226301 | pubmed:author | pubmed-author:HuangJung... | lld:pubmed |
| pubmed-article:15226301 | pubmed:author | pubmed-author:LingThai-YenT... | lld:pubmed |
| pubmed-article:15226301 | pubmed:author | pubmed-author:HuangShuan... | lld:pubmed |
| pubmed-article:15226301 | pubmed:author | pubmed-author:HuangYen-HuaY... | lld:pubmed |
| pubmed-article:15226301 | pubmed:author | pubmed-author:LiuI-HuaIH | lld:pubmed |
| pubmed-article:15226301 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15226301 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:15226301 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:15226301 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15226301 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15226301 | pubmed:pagination | 38736-48 | lld:pubmed |
| pubmed-article:15226301 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:15226301 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15226301 | pubmed:articleTitle | Identification and characterization of the acidic pH binding sites for growth regulatory ligands of low density lipoprotein receptor-related protein-1. | lld:pubmed |
| pubmed-article:15226301 | pubmed:affiliation | Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan. | lld:pubmed |
| pubmed-article:15226301 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15226301 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15226301 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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