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http://purl.uniprot.org/citations/23714211 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23714211 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundCell adhesion molecules (CAMs) are expressed ubiquitously. Each of the four families of CAMs is comprised of glycosylated, membrane-bound proteins that participate in multiple cellular processes including cell-cell communication, cell motility, inside-out and outside-in signaling, tumorigenesis, angiogenesis and metastasis. Intercellular adhesion molecule-2 (ICAM-2), a member of the immunoglobulin superfamily of CAMs, has six N-linked glycosylation sites at amino acids (asparagines) 47, 82, 105, 153, 178 and 187. Recently, we demonstrated a previously unknown function for ICAM-2 in tumor cells. We showed that ICAM-2 suppressed neuroblastoma cell motility and growth in soft agar, and induced a juxtamembrane distribution of F-actin in vitro. We also showed that ICAM-2 completely suppressed development of disseminated tumors in vivo in a murine model of metastatic NB. These effects of ICAM-2 on NB cell phenotype in vitro and in vivo depended on the interaction of ICAM-2 with the cytoskeletal linker protein α-actinin. Interestingly, ICAM-2 did not suppress subcutaneous growth of tumors in mice, suggesting that ICAM-2 affects the metastatic but not the tumorigenic potential of NB cells. The goal of the study presented here was to determine if the glycosylation status of ICAM-2 influenced its function in neuroblastoma cells.MethodsBecause it is well documented that glycosylation facilitates essential steps in tumor progression and metastasis, we investigated whether the glycosylation status of ICAM-2 affected the phenotype of NB cells. We used site-directed mutagenesis to express hypo- or non-glycosylated variants of ICAM-2, by substituting alanine for asparagine at glycosylation sites, and compared the impact of each variant on NB cell motility, anchorage-independent growth, interaction with intracellular proteins, effect on F-actin distribution and metastatic potential in vivo.ResultsThe in vitro and in vivo phenotypes of cells expressing glycosylation site variants differed from cells expressing fully-glycosylated ICAM-2 or no ICAM-2. Most striking was the finding that mice injected intravenously with NB cells expressing glycosylation site variants survived longer (P ≤ 0.002) than mice receiving SK-N-AS cells with undetectable ICAM-2. However, unlike fully-glycosylated ICAM-2, glycosylation site variants did not completely suppress disseminated tumor development.ConclusionsReduced glycosylation of ICAM-2 significantly attenuated, but did not abolish, its ability to suppress metastatic properties of NB cells."xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.org/dc/terms/identifier | "doi:10.1186/1471-2407-13-261"xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/author | "Yoon K.J."xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/author | "Bu S."xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/author | "Garcia P.L."xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/author | "Feduska J.M."xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/author | "Brennan S.B."xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/author | "Council L.N."xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/name | "BMC Cancer"xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/pages | "261"xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/title | "N-glycosylation of ICAM-2 is required for ICAM-2-mediated complete suppression of metastatic potential of SK-N-AS neuroblastoma cells."xsd:string |
http://purl.uniprot.org/citations/23714211 | http://purl.uniprot.org/core/volume | "13"xsd:string |
http://purl.uniprot.org/citations/23714211 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23714211 |
http://purl.uniprot.org/citations/23714211 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/23714211 |
http://purl.uniprot.org/uniprot/#_A8KAP5-mappedCitation-23714211 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23714211 |
http://purl.uniprot.org/uniprot/#_B7Z316-mappedCitation-23714211 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23714211 |
http://purl.uniprot.org/uniprot/#_P13598-mappedCitation-23714211 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23714211 |
http://purl.uniprot.org/uniprot/#_Q59ED3-mappedCitation-23714211 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23714211 |
http://purl.uniprot.org/uniprot/#_Q6FHE2-mappedCitation-23714211 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23714211 |
http://purl.uniprot.org/uniprot/#_Q9NZC6-mappedCitation-23714211 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/23714211 |
http://purl.uniprot.org/uniprot/Q9NZC6 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23714211 |
http://purl.uniprot.org/uniprot/Q59ED3 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23714211 |
http://purl.uniprot.org/uniprot/A8KAP5 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/23714211 |