ArticleNature communications2025
Lysosome-mediated aggregation of galactose-deficient IgA1 with transferrin receptor 1 links to IgA nephropathy.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Efficacy and Safety of Telitacicept in Posttransplant Recurrent IgA Nephropathy.Kidney international reports · 2026Article
- Modified Huangqi Chifeng decoction alleviates IgA nephropathy inflammation and renal fibrosis via miR-146a/TLR4/NF-κB signaling modulation.Frontiers in immunology · 2026Article
- Gut-kidney axis in IgA nephropathy: mechanisms linking microbiota dysbiosis to immune dysregulation, Gd-IgA1 generation, and renal injury.Frontiers in immunology · 2026Review
- Layered immune biomarker monitoring in IgA nephropathy: from mucosal IgA dysregulation to precision therapeutic response assessment.Frontiers in medicine · 2026Review
- Precision targeting of gut-kidney axis: mucosal immunomodulation in IgA nephropathy-a perspective.Frontiers in medicine · 2026Article
- Unveiling the immune landscape and microenvironmental architecture of IgA nephropathy using single-cell imaging mass cytometry.Clinical & translational immunology · 2026Article
- A Literature Review of the Renal Manifestations in Pediatric Celiac Disease and Its Associated Clinical Implications.Cureus · 2025Review
Corrections and comments
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Authors and funding
16 authors.
Funding
Abstract
The retention of galactose-deficient IgA1 (Gd-IgA1) in the mesangium is central to IgA nephropathy (IgAN), but its intracellular fate remains unclear. Here, we show that transferrin receptor 1 (TfR1) mediates Gd-IgA1 uptake into mesangial cell lysosomes, where it forms non-digestible aggregates, disrupts lysosomal function, and triggers inflammatory responses. In renal biopsies from IgAN patients, IgA1 aggregates co-localize with TfR1 within lysosomes. In male mice, TfR1 overexpression enhanced lysosomal accumulation of Gd-IgA1, whereas TfR1 knockdown reduced it. Mechanistically, acidic pH strengthens TfR1-Gd-IgA1 binding via the galactose-deficient hinge region and residue R276. While we acknowledge that sialylation commonly found in patient-derived IgA1 might influence TfR1 binding and that other receptors, such as ASGPR, were not evaluated, our findings nonetheless reveal a lysosome-centered mechanism in IgAN and highlight receptor-mediated retention of Gd-IgA1 as a potential therapeutic target.
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Registered trials
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