| http://purl.uniprot.org/citations/15226301 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15226301 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m310537200"xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/author | "Huang J.S."xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/author | "Chen C.L."xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/author | "Huang Y.H."xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/author | "Huang S.S."xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/author | "Ling T.Y."xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/author | "Liu I.H."xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/pages | "38736-38748"xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/title | "Identification and characterization of the acidic pH binding sites for growth regulatory ligands of low density lipoprotein receptor-related protein-1."xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15226301 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15226301 |
| http://purl.uniprot.org/citations/15226301 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15226301 |
| http://purl.uniprot.org/uniprot/P79134#attribution-06A6903C201612E23950BCF349A21090 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |
| http://purl.uniprot.org/uniprot/P79134#attribution-83EB0714F7C044B34B6D9DBF88107700 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |
| http://purl.uniprot.org/uniprot/P08133#attribution-9D360980444CB5C3A97045E6A945056D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |
| http://purl.uniprot.org/uniprot/P12429#attribution-9D360980444CB5C3A97045E6A945056D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |
| http://purl.uniprot.org/uniprot/P04083#attribution-9D360980444CB5C3A97045E6A945056D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |
| http://purl.uniprot.org/uniprot/P09525#attribution-9D360980444CB5C3A97045E6A945056D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |
| http://purl.uniprot.org/uniprot/P07355#attribution-9D360980444CB5C3A97045E6A945056D | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |
| http://purl.uniprot.org/uniprot/P01023#attribution-5F54039CA52090E05A4373C5BDB27ED2 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |
| http://purl.uniprot.org/uniprot/P01023#attribution-83EB0714F7C044B34B6D9DBF88107700 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15226301 |