| http://purl.uniprot.org/citations/8636223 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8636223 | http://www.w3.org/2000/01/rdf-schema#comment | "Integrin alpha v beta 3 is distinct in its capacity to recognize the sequence Arg-Gly-Asp (RGD) in many extra-cellular matrix (ECM) components. Here, we demonstrate that in addition to the recognition of ECM components, alpha v beta 3 can interact with the neural cell adhesion molecule L1-CAM; a member of the immunoglobulin superfamily (IgSF). M21 melanoma cells displayed significant Ca(++)-dependent adhesion and spreading on immunopurified rat L1 (NILE). This adhesion was found to be dependent on the expression of the alpha v-integrin subunit and could be significantly inhibited by an antibody to the alpha v beta 3 heterodimer. M21 cells also displayed some alpha v beta 3-dependent adhesion and spreading on immunopurified human L1. Ligation between this ligand and alpha v beta 3 was also observed to promote significant haptotactic cell migration. To map the site of alpha v beta 3 ligation we used recombinant L1 fragments comprising the entire extracellular domain of human L1. Significant alpha v beta 3-dependent adhesion and spreading was evident on a L1 fragment containing Ig-like domains 4, 5, and 6. Importantly, mutation of an RGD sequence present in the sixth Ig-like domain of L1 abrogated M21 cell adhesion. We conclude that alpha v beta 3-dependent recognition of human L1 is dependent on ligation of this RGD site. Despite high levels of L1 expression the M21 melanoma cells did not display significant adhesion via a homophilic L1-L1 interaction. These data suggest that M21 melanoma cells recognize and adhere to L1 through a mechanism that is primarily heterophilic and integrin dependent. Finally, we present evidence that melanoma cells can shed and deposit L1 in occluding ECM. In this regard, alpha v beta 3 may recognize L1 in a cell-cell or cell-substrate interaction."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.org/dc/terms/identifier | "doi:10.1083/jcb.132.3.475"xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/author | "Zhao X."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/author | "Siu C.H."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/author | "Becker J.C."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/author | "Reisfeld R.A."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/author | "Lemmon V.P."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/author | "Cheresh D.A."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/author | "Montgomery A.M."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/author | "Pancook J.D."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/date | "1996"xsd:gYear |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/name | "J Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/pages | "475-485"xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/title | "Human neural cell adhesion molecule L1 and rat homologue NILE are ligands for integrin alpha v beta 3."xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://purl.uniprot.org/core/volume | "132"xsd:string |
| http://purl.uniprot.org/citations/8636223 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8636223 |
| http://purl.uniprot.org/citations/8636223 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8636223 |
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