ArticleOrphanet journal of rare diseases2013
GPI-anchor and GPI-anchored protein expression in PMM2-CDG patients.
Article in Orphanet journal of rare diseases, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02503267 ("Incidence and Consequences of Disorders of Glycosylation in Patients With Conotruncal and Septal Heart Defects"), which is not on this map. Cited by 11 papers.
What it found
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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.
"Incidence and Consequences of Disorders of Glycosylation in Patients With Conotruncal and Septal Heart Defects" (CARDIoG)
Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Immunopathology in PMM2-CDG: Defective glycosylation impact in the TNFα -TNFR1 signalling pathway.Frontiers in immunology · 2025Article
- Investigation of Glycosylphosphatidylinositol (GPI)-Plasma Membrane Interaction in Live Cells and the Influence of GPI Glycan Structure on the Interaction.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Evaluation of Cell Models to Study Monocyte Functions in PMM2 Congenital Disorders of Glycosylation.Frontiers in immunology · 2022Article
- New Insights into Immunological Involvement in Congenital Disorders of Glycosylation (CDG) from a People-Centric Approach.Journal of clinical medicine · 2020Article
- Significantly different clinical phenotypes associated with mutations in synthesis and transamidase+remodeling glycosylphosphatidylinositol (GPI)-anchor biosynthesis genes.Orphanet journal of rare diseases · 2020Article
- Genetic predisposition to fetal alcohol syndrome: association with congenital disorders of N-glycosylation.Pediatric research · 2018Article
- Immunological aspects of congenital disorders of glycosylation (CDG): a review.Journal of inherited metabolic disease · 2016Review
- Synaptic roles for phosphomannomutase type 2 in a new Drosophila congenital disorder of glycosylation disease model.Disease models & mechanisms · 2016Article
- Natural Killer Cell Receptors and Cytotoxic Activity in Phosphomannomutase 2 Deficiency (PMM2-CDG).PloS one · 2016Article
- Neurological aspects of human glycosylation disorders.Annual review of neuroscience · 2015Review
- Genome-Wide Screening of Genes Required for Glycosylphosphatidylinositol Biosynthesis.PloS one · 2015Article
Corrections and comments
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Authors and funding
14 authors at 8 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMutations in PMM2 impair phosphomannomutase-2 activity and cause the most frequent congenital disorder of glycosylation, PMM2-CDG. Mannose-1-phosphate, that is deficient in this disorder, is also implicated in the biosynthesis of glycosylphosphatidyl inositol (GPI) anchors.
objectiveTo evaluate whether GPI-anchor and GPI-anchored proteins are defective in PMM2-CDG patients.
methodsThe expression of GPI-anchor and seven GPI-anchored proteins was evaluated by flow cytometry in different cell types from twelve PMM2-CDG patients. Additionally, neutrophil CD16 and plasma hepatic proteins were studied by Western blot. Transferrin glycoforms were evaluated by HPLC.
resultsPatients and controls had similar surface expression of GPI-anchor and most GPI-anchored proteins. Nevertheless, patients displayed a significantly diminished binding of two anti-CD16 antibodies (3G8 and KD1) to neutrophils and also of anti-CD14 (61D3) to monocytes. Interestingly, CD16 immunostaining and asialotransferrin levels significantly correlated with patients' age. Analysis by flow cytometry of CD14 with MΦP9, and CD16 expression in neutrophils by Western blot using H-80 ruled out deficiencies of these antigens.
conclusionsPMM2 mutations do not impair GPI-anchor or GPI-anchored protein expression. However, the glycosylation anomalies caused by PMM2 mutations might affect the immunoreactivity of monoclonal antibodies and lead to incorrect conclusions about the expression of different proteins, including GPI-anchored proteins. Neutrophils and monocytes are sensitive to PMM2 mutations, leading to abnormal glycosylation in immune receptors, which might potentially affect their affinity to their ligands, and contribute to infection. This study also confirms less severe hypoglycosylation defects in older PMM2-CDG patients.
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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.