ArticleCommunications biology2025
TMPRSS11E-mediated TFR1 cleavage influences IFN-γR2 internalization and the macrophage innate response.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Metabolic regulation of macrophage polarization in myocardial infarction: from mechanisms to targeted therapies.Journal of translational medicine · 2026Review
- Modulation of Macrophage Inflammatory Responses by UDP-Glucuronosyltransferase-Mediated PGEJournal of personalized medicine · 2026Article
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Authors and funding
11 authors.
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Abstract
TMPRSS11E is a serine protease whose expression is upregulated in macrophages during inflammation. Here, we identify TFR1 as an interacting protein of TMPRSS11E via LC-MS/MS. In vitro experiments reveal that TMPRSS11E cleaves TFR1 and releases soluble TFR1 (sTFR1). In alveolar macrophages isolated from pneumonia patients and inflammatory animal models or cultured LPS-challenged cell lines, upregulated TMPRSS11E expression and significantly increased sTFR1 release are observed. Moreover, THP-1 cells stably expressing TMPRSS11E present decreased iron uptake, increased cell surface IFN-γR2 accumulation, and a stronger response to IFN-γ stimulation. During M0 macrophage differentiation to the pro-inflammatory M1 phenotype, the specific induction of TMPRSS11E, decreased cell surface TFR1, and increased IFN-γR2 cell membrane localization are also observed. Taken together, our results suggest that TMPRSS11E contributes to M1 macrophage differentiation by regulating iron uptake and affecting IFN-γR2 internalization through TFR1 cleavage, indicating that TMPRSS11E plays an important role in iron homeostasis and the innate immune response.
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Registered trials
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