{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jendresen C"],"funding":["Norges Forskningsråd","Helse Sør-Øst RHF","Anders Jahres Fond til Vitenskapens Fremme","Universitetet i Oslo"],"pagination":["59"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5360024"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(1)"],"pubmed_abstract":["<h4>Background</h4>Triggering receptor expressed on myeloid cells 2 (TREM2) and apolipoprotein E (APOE) are genetically linked to Alzheimer's disease. Here, we investigated whether human ApoE mediates signal transduction through human and murine TREM2 and sought to identify a TREM2-binding domain in human ApoE.<h4>Methods</h4>To investigate cell signaling through TREM2, a cell line was used which expressed an NFAT-inducible β-galactosidase reporter and human or murine TREM2, fused to CD8 transmembrane and CD3ζ intracellular signaling domains. ELISA-based binding assays were used to determine binding affinities of human ApoE isoforms to human TREM2 and to identify a TREM2-binding domain in ApoE.<h4>Results</h4>ApoE was found to be an agonist to human TREM2 with EC<sub>50</sub> in the low nM"],"journal":["Journal of neuroinflammation"],"pubmed_title":["The Alzheimer's disease risk factors apolipoprotein E and TREM2 are linked in a receptor signaling pathway."],"pmcid":["PMC5360024"],"funding_grant_id":["237250","2013016","240316"],"pubmed_authors":["Arskog V","Daws MR","Nilsson LN","Jendresen C"],"additional_accession":[]},"is_claimable":false,"name":"The Alzheimer's disease risk factors apolipoprotein E and TREM2 are linked in a receptor signaling pathway.","description":"<h4>Background</h4>Triggering receptor expressed on myeloid cells 2 (TREM2) and apolipoprotein E (APOE) are genetically linked to Alzheimer's disease. Here, we investigated whether human ApoE mediates signal transduction through human and murine TREM2 and sought to identify a TREM2-binding domain in human ApoE.<h4>Methods</h4>To investigate cell signaling through TREM2, a cell line was used which expressed an NFAT-inducible β-galactosidase reporter and human or murine TREM2, fused to CD8 transmembrane and CD3ζ intracellular signaling domains. ELISA-based binding assays were used to determine binding affinities of human ApoE isoforms to human TREM2 and to identify a TREM2-binding domain in ApoE.<h4>Results</h4>ApoE was found to be an agonist to human TREM2 with EC<sub>50</sub> in the low nM","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Mar","modification":"2025-04-04T12:39:27.447Z","creation":"2019-03-27T02:39:10Z"},"accession":"S-EPMC5360024","cross_references":{"pubmed":["28320424"],"doi":["10.1186/s12974-017-0835-4"]}}