{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang LC"],"funding":["the National Science and Technology Major Project","the National Science Foundation of China"],"pagination":["62"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6151050"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["<h4>Background</h4>TEM8 is a cell membrane protein predominantly expressed in tumor endothelium, which serves as a receptor for the protective antigen (PA) of anthrax toxin. However, the physiological ligands for TEM8 remain unknown.<h4>Results</h4>Here we identified uPA as an interacting partner of TEM8. Binding of uPA stimulated the phosphorylation of TEM8 and augmented phosphorylation of EGFR and ERK1/2. Finally, TEM8-Fc, a recombinant fusion protein comprising the extracellular domain of human TEM8 linked to the Fc portion of human IgG1, efficiently abrogated the interaction between uPA and TEM8, blocked uPA-induced migration of HepG2 cells in vitro and inhibited the growth and metastasis of human MCF-7 xenografts in vivo. uPA, TEM8 and EGFR overexpression and ERK1/2 phosphorylation we"],"journal":["Cell communication and signaling : CCS"],"pubmed_title":["TEM8 functions as a receptor for uPA and mediates uPA-stimulated EGFR phosphorylation."],"pmcid":["PMC6151050"],"funding_grant_id":["2012ZX09102-301","2009ZX09103-626","3090592","30973670"],"pubmed_authors":["Chen HP","Wang YL","Liu J","Shao Y","Gao LH","Xi YY","Wu C","Chen W","Duan HF","Zhang LC","Hu XW","Xu Y"],"additional_accession":[]},"is_claimable":false,"name":"TEM8 functions as a receptor for uPA and mediates uPA-stimulated EGFR phosphorylation.","description":"<h4>Background</h4>TEM8 is a cell membrane protein predominantly expressed in tumor endothelium, which serves as a receptor for the protective antigen (PA) of anthrax toxin. However, the physiological ligands for TEM8 remain unknown.<h4>Results</h4>Here we identified uPA as an interacting partner of TEM8. Binding of uPA stimulated the phosphorylation of TEM8 and augmented phosphorylation of EGFR and ERK1/2. Finally, TEM8-Fc, a recombinant fusion protein comprising the extracellular domain of human TEM8 linked to the Fc portion of human IgG1, efficiently abrogated the interaction between uPA and TEM8, blocked uPA-induced migration of HepG2 cells in vitro and inhibited the growth and metastasis of human MCF-7 xenografts in vivo. uPA, TEM8 and EGFR overexpression and ERK1/2 phosphorylation we","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Sep","modification":"2026-06-08T05:59:20.101Z","creation":"2026-06-08T03:14:14.792Z"},"accession":"S-EPMC6151050","cross_references":{"pubmed":["30241478"],"doi":["10.1186/s12964-018-0272-8"]}}