ArticleCell communication and signaling : CCS2018
TEM8 functions as a receptor for uPA and mediates uPA-stimulated EGFR phosphorylation.
Article in Cell communication and signaling : CCS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 7 citations in OpenAlex.
- Unravelling the Phosphorylation Landscape of Anthrax Toxin Receptor 1: Mechanisms and Functional Insights Through Phosphoproteomic Data Integration.The protein journal · 2025Article
- Elevated expression ofFrontiers in molecular biosciences · 2024Article
- TEM8 marks neovasculogenic tumor-initiating cells in triple-negative breast cancer.Nature communications · 2021Article
- Latest therapeutic target for gastric cancer: Anthrax toxin receptor 1.World journal of gastrointestinal oncology · 2021Review
- Article
- Upregulated Circular RNAs in Gastric Cancer: Target Identification and Tools for Therapeutic Intervention.Cancer genomics & proteomicsReview
- GLIPR1 Protects Against Cigarette Smoke-Induced Airway Inflammation via PLAU/EGFR Signaling.International journal of chronic obstructive pulmonary diseaseArticle
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
backgroundTEM8 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.
resultsHere 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 were found co-located on frozen cancer tissue sections.
conclusionsTaken together, our data provide evidence that TEM8 is a novel receptor for uPA, which may play a significant role in the regulation of tumor growth and metastasis.
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Registered trials
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