Evidence map›Paper›PMID 40576648›Full record

ArticleCellular and molecular life sciences : CMLS2025

Glycosphingolipid synthesis is impaired in SLC35A2-CDG and improves with galactose supplementation.

Andrea Jáñez Pedrayes, Sam De Craemer, Jakub Idkowiak, Dries Verdegem, Christian Thiel, Rita Barone, Mercedes Serrano, Tomáš Honzík, Eva Morava, Pieter Vermeersch and 7 more

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Disrupted O-GalNAc glycosylation as a mechanism and biomarker ofbioRxiv : the preprint server for biology · 2026
    Article
  4. International journal of molecular sciences · 2025
    Review
  5. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

17 authors.

Andrea Jáñez PedrayesLaboratory of Applied Mass Spectrometry, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, 3000, Belgium.
Sam De CraemerLaboratory of Applied Mass Spectrometry, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, 3000, Belgium.
Jakub IdkowiakLaboratory of Lipid Metabolism and Cancer, Department of Oncology, Leuven Cancer Institute (LKI) and Leuven Institute for Single Cell Omics (LISCO), KU Leuven, Leuven, 3000, Belgium.
Dries VerdegemLaboratory of Applied Mass Spectrometry, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, 3000, Belgium.
Christian ThielCenter for Pediatric and Adolescent Medicine, Department Pediatrics I, Heidelberg University, 69120, Heidelberg, Germany.
Rita BaroneChild Neurology and Psychiatry Unit, Department of Clinical and Experimental Medicine, University of Catania, Catania, 95131, Italy.
Mercedes SerranoPediatric Neurology Department, Hospital Sant Joan de Déu, Esplugues de Llobregat, Barcelona, 08950, Spain.
Tomáš HonzíkDepartment of Paediatrics and Inherited Metabolic Disorders, First Medical Faculty, Charles University and General University Hospital in Prague, Prague 2, CZ-121 08, Czech Republic.
Eva MoravaDepartment of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, NY, 10029, USA.
Pieter VermeerschClinical Department of Laboratory Medicine, University Hospitals Leuven, Leuven, 3000, Belgium.
François FoulquierUMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, CNRS, University of Lille, Lille, F-59000, France.
Willy MorelleUMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, CNRS, University of Lille, Lille, F-59000, France.
Johannes V SwinnenLaboratory of Lipid Metabolism and Cancer, Department of Oncology, Leuven Cancer Institute (LKI) and Leuven Institute for Single Cell Omics (LISCO), KU Leuven, Leuven, 3000, Belgium.
Daisy RymenCenter for Metabolic Diseases, Department of Paediatrics, University Hospitals Leuven, Leuven, 3000, Belgium.
David CassimanDepartment of Hepatology, University Hospitals Leuven, Leuven, 3000, Belgium.
Bart Ghesquière *Laboratory of Applied Mass Spectrometry, Department of Cellular and Molecular Medicine, KU Leuven, Leuven, 3000, Belgium.
Peter Witters *Department of Development and Regeneration, KU Leuven, Leuven, 3000, Belgium. peter.witters@uzleuven.be.ORCID http://orcid.org/0000-0002-9264-6153

Funding

Czech Health Research Council AZV MZ CR NU22-07-00474Fonds Wetenschappelijk Onderzoek 18B4322NFonds Wetenschappelijk Onderzoek G049220NFonds Wetenschappelijk Onderzoek K200523NMinisterstvo Zdravotnictví Ceské Republiky RVO-VFN 64165
6 · The paper itself

Abstract

SLC35A2-CDG is an X-linked congenital disorder of glycosylation (CDG), characterized by defective UDP-galactose transport into the Golgi and endoplasmic reticulum and consequent insufficient galactosylation of glycans. Clinically, this translates into a range of predominantly neurological symptoms. Although the pathomechanism of this disorder is not fully understood, oral galactose supplementation has led to clinical and biochemical improvement in some patients. Here, we show that protein glycosylation (N- and O-linked) was only minimally disturbed in SLC35A2-CDG patient-derived fibroblasts. However, lipid glycosylation was significantly impaired, with accumulation of glucosylceramide and deficiency of digalactosylated glycosphingolipids (GSLs) and complex gangliosides. Galactose supplementation increased UDP-galactose, its transport into the Golgi, and improved deficient GSL synthesis through direct incorporation of the provided galactose. This improved GSL homeostasis in all patient-derived fibroblasts and in another SLC35A2 deficient cell model (CHO-Lec8). Additionally, SLC35A2-CDG serum analysis identified hydroxylated GSLs, particularly GM3, as potential disease biomarkers. Given the essential role of gangliosides in central nervous system function, their deficiency is likely a key factor in the neurological involvement of this disorder. These findings pave the way for new nutritional therapies with GSL supplements and highlight the importance of studying lipid glycosylation to better understand the complex pathophysiology of CDG.

Indexed as

Congenital Disorders of GlycosylationGalactoseGlycosphingolipidsAnimalsCHO CellsCricetulusDietary SupplementsFibroblastsGlycosylationGolgi ApparatusHumansMonosaccharide Transport ProteinsUDP-Galactose TranslocatorsGalactoseGlycosphingolipidsMonosaccharide Transport ProteinsUDP-Galactose TranslocatorsCDGGangliosidesGlycosphingolipidsGSLSLC35A2-CDGTracer metabolomics

Identifiers

PMID40576648
PMCPMC12204976

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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Registered trials

None linked

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 Socratic graph.