ArticleGlycobiology2026
Cellular homeostasis of N-acetylneuraminic acid and non-canonical sialic acids is mediated by human N-acetylneuraminate lyase.
Article in Glycobiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Sialic acids are important for cellular communication, with N-acetylneuraminic acid (Neu5Ac) being the canonical form of sialic acid in humans. Presence of non-canonical sialic acids, derived from dietary intake or as metabolic side product, has been linked to immune disorders and cancer. As homeostasis of different sialic acids remains poorly understood in humans, we studied the role of N-acetylneuraminate lyase (NPL) in their catabolism. In vitro expression of NPL in different biological systems revealed broad substrate specificity towards sialic acids and related 2-keto-3-deoxy metabolites. In agreement with the broad substrate specificity, NPL-deficient red blood cells accumulated Neu5Ac and 3-deoxy-d-glycero-d-galacto-nonulosonic acid (KDN). Interestingly, endogenous levels of non-canonical sialic acids, including N-glycolylneuraminic acid (Neu5Gc) and KDN, were depleted in HEK293T cells upon NPL overexpression, while Neu5Ac and CMP-Neu5Ac levels remained stable. This was further confirmed by supplementation with different sialic acids. Detailed analysis of sugar phosphate intermediates of the hexosamine and sialic acid biosynthesis pathways showed strongly elevated ManNAc-6P (N-acetyl-d-mannosamine 6-phosphate) and Neu5Ac-9P, indicating efficient recycling of ManNAc to increase de novo Neu5Ac biosynthesis. However, this recycling was not efficient for Neu5Gc and KDN. While GlcNAc-6P (N-acetyl-d-glucosamine 6-phosphate) levels were slightly elevated, no evidence was found for further metabolism towards GlcN-6P (glucosamine 6-phosphate) and energy production via glycolysis as shown for bacterial neuraminate lyases. In conclusion, human NPL catabolizes a broad range of sialic acids. However, depending on the cellular context, NPL contributes to a net cellular reduction in non-canonical sialic acids, such as KDN, due to a lack of efficient recycling.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.