ArticleMolecular medicine (Cambridge, Mass.)2026
Alpha-1 antitrypsin-glucocorticoid receptor axis: a new pathway in immune modulation.
Article in Molecular medicine (Cambridge, Mass.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- Glucocorticoid Receptor Gene Polymorphisms and Femoral Head Osteonecrosis.Medicina (Kaunas, Lithuania) · 2026Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAlpha-1 antitrypsin (AAT) has been reported to interact with the glucocorticoid receptor (GR) and modulate its signaling. We extended these findings by testing whether native (nAAT) and oxidized AAT (oxAAT) bind GR.
methodsBinding of native and modified AAT (oxidized and cleaved) to GR and candidate receptors (LRP1, SR-B1, TfR, CD36) was assessed by ELISA. AAT-GR colocalization was examined in PBMCs and macrophage models by confocal microscopy and co-immunoprecipitation. NR3C1 (GR) mRNA in PBMCs was analyzed after 24 h of treatment with AAT or dexamethasone.
resultsnAAT and oxAAT bound GR (EC₅₀ 0.9 and 2.6 µM) and LRP1 (EC₅₀ 2.9 and 1.3 µM), whereas binding to SR-B1, TfR, and CD36 was weak (EC₅₀ > 5 µM). Cleaved AAT showed no binding. AAT-GR colocalization was present in non-activated PBMCs but absent in macrophages, where GR was predominantly nuclear. Both nAAT and oxAAT significantly reduced NR3C1 mRNA, similar to dexamethasone.
conclusionnAAT and oxAAT, but not cleaved forms of AAT, bind GR in vitro and associate with cytoplasmic GR in non-activated immune cells. Our results support the role of AAT in regulating GR signaling and highlight the AAT-GR axis as a putative mechanism of immune regulation.
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