Evidence map›Paper›PMID 42593233›Full record

ArticleJournal of inherited metabolic disease2026

Proteo-Metabolomic Profiling of PMM2-CDG Reveals Dysregulation of Retinoic Acid Synthesis, Myo-Inositol, and the Hexosamine Pathway.

Diana Gallego, Giuseppina Andreotti, Maria Monticelli, Debora Paris, Arturo Martín-Martínez, Alejandra Gámez, Mercedes Serrano, José Córdoba-Caballero, Pedro Seoane, Juan A G Ranea and 1 more

Abstract read
In one paragraph

Article in Journal of inherited metabolic disease, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

11 authors.

Diana GallegoCentro de Diagnóstico de Enfermedades Moleculares. Centro de Biología Molecular, Universidad Autónoma de Madrid. CIBERER. IdiPAZ, Madrid, Spain.ORCID https://orcid.org/0000-0002-3866-7316
Giuseppina AndreottiInstitute of Biomolecular Chemistry (ICB), National Research Council of Italy, Naples, Italy.ORCID https://orcid.org/0000-0002-1594-0156
Maria MonticelliInstitute of Biomolecular Chemistry (ICB), National Research Council of Italy, Naples, Italy.ORCID https://orcid.org/0000-0003-3136-2138
Debora ParisInstitute of Biomolecular Chemistry (ICB), National Research Council of Italy, Naples, Italy.ORCID https://orcid.org/0000-0003-4526-8353
Arturo Martín-MartínezCentro de Diagnóstico de Enfermedades Moleculares. Centro de Biología Molecular, Universidad Autónoma de Madrid. CIBERER. IdiPAZ, Madrid, Spain.
Alejandra GámezCentro de Diagnóstico de Enfermedades Moleculares. Centro de Biología Molecular, Universidad Autónoma de Madrid. CIBERER. IdiPAZ, Madrid, Spain.ORCID https://orcid.org/0000-0002-2414-2586
Mercedes SerranoPediatric Neurology Department, Hospital Sant Joan de Déu, Barcelona, Spain and Institut de Recerca Sant Joan de Déu, CIBERER, Barcelona, Spain.ORCID https://orcid.org/0000-0002-2056-2428
José Córdoba-CaballeroDepartment of Molecular Biology and Biochemistry, University of Malaga, 29010, Malaga, Spain. CIBERER. Institute of Biomedical Research in Malaga and Platform of Nanomedicine, IBIMA Plataforma BIONAND, 29071, Malaga, Spain. Spanish National Bioinformatics Institute (INB/ELIXIR-ES), Instituto de Salud Carlos III (ISCIII), Madrid, Spain.
Pedro SeoaneDepartment of Molecular Biology and Biochemistry, University of Malaga, 29010, Malaga, Spain. CIBERER. Institute of Biomedical Research in Malaga and Platform of Nanomedicine, IBIMA Plataforma BIONAND, 29071, Malaga, Spain. Spanish National Bioinformatics Institute (INB/ELIXIR-ES), Instituto de Salud Carlos III (ISCIII), Madrid, Spain.ORCID https://orcid.org/0000-0002-3020-1415
Juan A G RaneaDepartment of Molecular Biology and Biochemistry, University of Malaga, 29010, Malaga, Spain. CIBERER. Institute of Biomedical Research in Malaga and Platform of Nanomedicine, IBIMA Plataforma BIONAND, 29071, Malaga, Spain. Spanish National Bioinformatics Institute (INB/ELIXIR-ES), Instituto de Salud Carlos III (ISCIII), Madrid, Spain.
Belén PérezCentro de Diagnóstico de Enfermedades Moleculares. Centro de Biología Molecular, Universidad Autónoma de Madrid. CIBERER. IdiPAZ, Madrid, Spain.ORCID https://orcid.org/0000-0002-3190-1958

Funding

Fundación Ramón Areces XXII Concurso Nacionalde AyudaInstituto de Salud Carlos III PI22/00699, PI25/01398Regione Campania B83C25000740002
6 · The paper itself

Abstract

Phosphomannomutase deficiency (PMM2-CDG), the most common congenital disorder of glycosylation (CDG), is characterized by multisystem involvement and a lack of disease-modifying therapies. While previous transcriptomic studies have uncovered disrupted cellular pathways, the functional consequences of these alterations remain poorly understood. To further investigate PMM2-CDG pathophysiology, we integrated proteomic and metabolomic profiling of patient-derived fibroblasts with previously published transcriptomic data. Proteomic analysis was performed using Tandem Mass Tag-based mass spectrometry, while metabolomics was conducted via Nuclear Magnetic Resonance spectroscopy. Multi-omics integration was performed using principal component analysis-based dimensionality reduction, incorporating clinical metadata as supplementary variables. Proteomic analysis identified 43 significantly altered proteins, with enrichment in the retinoic acid synthesis pathway, wound healing, and cytoskeletal organization. Metabolomic profiling revealed altered amino acid levels and elevated concentrations of UDP-GlcNAc, consistent with perturbation of the hexosamine biosynthesis pathway, and increased levels of myo-inositol. Notably, myo-inositol levels showed a strong association with disease severity in the integrated analysis. RT-qPCR confirmed the upregulation of GFPT2. This integrative multi-omics study identifies consistent alterations in the retinoic acid synthesis pathway and hexosamine biosynthesis in PMM2-CDG patient-derived fibroblasts and reveals an association between intracellular myo-inositol levels and disease severity. These findings provide new insights into PMM2-CDG-associated molecular alterations and illustrate the value of multi-omics integration for hypothesis generation in rare diseases.

Indexed as

Congenital Disorders of GlycosylationHexosaminesInositolPhosphotransferases (Phosphomutases)TretinoinFibroblastsHumansMetabolomicsMultiomicsProteomicsHexosaminesInositolphosphomannomutase 2, humanPhosphotransferases (Phosphomutases)Tretinoinhexosamine pathwaymetabolomicsmyo‐inositolPMM2‐CDGproteomicsretinoic acidretinol

Identifiers

PMID42593233
PMCPMC13471400

What OpenQuestion holds

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Registered trials

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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.