| http://purl.uniprot.org/citations/8557754 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8557754 | http://www.w3.org/2000/01/rdf-schema#comment | "The L1 adhesion molecule is a member of the immunoglobulin superfamily shared by neural and immune cells. In the nervous system L1 can mediate cell binding by a homophilic mechanism. To analyze its function on leukocytes we studied whether L1 could interact with integrins. Here we demonstrate that VLA-5, an RGD-specific fibronectin receptor on a wide variety of cell types, can bind to murine L1. Mouse ESb-MP cells expressing VLA-5 and L1 could be induced to aggregate in the presence of specific mAbs to CD24 (heat-stable antigen), a highly and heterogeneously glycosylated glycophosphatidylinositol-linked differentiation antigen of hematopoietic and neural cells. The aggregation was blocked by both mAbs to L1 and VLA-5, respectively. Aggregation was blocked also by a synthetic RGD-containing peptide derived from the Ig-domain VI of the L1 protein. ESb-MP subclones with low L1 expression could not aggregate. In heterotypic binding assays mouse bone marrow cells could adhere in an L1-dependent fashion to platelets that expressed VLA-5. Also purified L1 coated to polystyrene beads could bind to platelets. The binding of L1-beads was again inhibited by mAbs to L1 and VLA-5, by soluble L1 and the L1-RGD peptide in a dose-dependent manner. Thymocytes or human Nalm-6 tumor cells expressing VLA-5 could adhere to affinity-purified L1 and to the L1-derived RGD-containing peptide coated to glass slides. The adhesion was strongly enhanced in the presence of Mn(2+)-ions and blocked by mAbs to VLA-5. We also demonstrate a direct L1-VLA-5 protein interaction. Our results suggest a novel binding pathway, in which the VLA-5 integrin binds to L1 on adjacent cells. Given its rapid downregulation on lymphocytes after induction of cell proliferation, L1 may be important in integrin-mediated and activation-regulated cell-cell interactions."xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.131.6.1881"xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/author | "Ruppert M."xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/author | "Aigner S."xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/author | "Altevogt P."xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/author | "Yagita H."xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/author | "Hubbe M."xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/name | "J Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/pages | "1881-1891"xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/title | "The L1 adhesion molecule is a cellular ligand for VLA-5."xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://purl.uniprot.org/core/volume | "131"xsd:string |
| http://purl.uniprot.org/citations/8557754 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8557754 |
| http://purl.uniprot.org/citations/8557754 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8557754 |
| http://purl.uniprot.org/uniprot/P24807#attribution-DAA163E30676C33EA08DAA9025DE8B09 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/P11688#attribution-65848AD71EA49CBCCBF176483FADC900 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/P11688#attribution-DAA163E30676C33EA08DAA9025DE8B09 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/Q00651#attribution-DAA163E30676C33EA08DAA9025DE8B09 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/Q61739#attribution-DAA163E30676C33EA08DAA9025DE8B09 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/P24063#attribution-DAA163E30676C33EA08DAA9025DE8B09 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/P05555#attribution-DAA163E30676C33EA08DAA9025DE8B09 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/P11627#attribution-65848AD71EA49CBCCBF176483FADC900 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/P11627#attribution-DAA163E30676C33EA08DAA9025DE8B09 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |
| http://purl.uniprot.org/uniprot/P43406#attribution-DAA163E30676C33EA08DAA9025DE8B09 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/8557754 |