ArticleProceedings of the National Academy of Sciences of the United States of America2025
Endothelial cells sialylate IgG within the FcRn-mediated recycling pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- Therapeutic effect of galactosyltransferase- and sialyltransferase-encoding mRNA in rheumatoid arthritis.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Reducing IgG accumulation via neonatal Fc receptor (FcRn) blockade relieves neuropathic pain.Brain, behavior, and immunity · 2025Article
- Ghost vessels in the eye: Cell free choriocapillaris domains in atrophic age-related macular degeneration.Experimental eye research · 2024Article
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10 authors.
Funding
Abstract
IgG is a key to adaptive immunity and a critical platform for drug design. Sialic acid on the conserved glycan within the Fc domain is believed to promote anti-inflammatory IgG function; however, regulation of sialylation remains poorly defined. We previously showed that IgG sialylation is primarily mediated by B cell-extrinsic processes in mice. Here, we found that IgG sialylation occurs in the subcellular compartments of the FcRn-mediated IgG recycling pathway of endothelial cells. This process is down-regulated by inflammatory signals and up-regulated during gestation, providing mechanistic insight into the epidemiology associating IgG glycosylation, pregnancy and inflammatory disease. These findings demonstrate that plasma-localized IgG glycosylation is dynamically altered by the endothelium, revealing a potential mechanism through which the function of all endogenous and administered IgG and Fc-containing pharmaceuticals could be altered.
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