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Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder
Changes in protein glycosylation are associated with most biological processes, and the importance of glycomic analysis in the research of disorders is constantly increasing, including in the neurodevelopmental field. We glycoprofiled sera in 10 children with attention-deficit hyperactivity disorder...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10218324/ https://www.ncbi.nlm.nih.gov/pubmed/37240090 http://dx.doi.org/10.3390/ijms24108745 |
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author | Kianičková, Kristína Pažitná, Lucia Kundalia, Paras H. Pakanová, Zuzana Nemčovič, Marek Baráth, Peter Katrlíková, Eva Šuba, Ján Trebatická, Jana Katrlík, Jaroslav |
author_facet | Kianičková, Kristína Pažitná, Lucia Kundalia, Paras H. Pakanová, Zuzana Nemčovič, Marek Baráth, Peter Katrlíková, Eva Šuba, Ján Trebatická, Jana Katrlík, Jaroslav |
author_sort | Kianičková, Kristína |
collection | PubMed |
description | Changes in protein glycosylation are associated with most biological processes, and the importance of glycomic analysis in the research of disorders is constantly increasing, including in the neurodevelopmental field. We glycoprofiled sera in 10 children with attention-deficit hyperactivity disorder (ADHD) and 10 matching healthy controls for 3 types of samples: whole serum, sera after depletion of abundant proteins (albumin and IgG), and isolated IgG. The analytical methods used were a lectin-based glycoprotein microarray enabling high-throughput glycan analysis and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) as a standard method for the identification of glycan structures. For microarray analysis, the samples printed on microarray slides were incubated with biotinylated lectins and detected using the fluorescent conjugate of streptavidin by a microarray scanner. In the ADHD patient samples, we found increased antennary fucosylation, decreased di-/triantennary N-glycans with bisecting N-acetylglucosamine (GlcNAc), and decreased α2-3 sialylation. The results obtained by both independent methods were consistent. The study’s sample size and design do not allow far-reaching conclusions to be drawn. In any case, there is a strong demand for a better and more comprehensive diagnosis of ADHD, and the obtained results emphasize that the presented approach brings new horizons to studying functional associations of glycan alterations in ADHD. |
format | Online Article Text |
id | pubmed-10218324 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-102183242023-05-27 Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder Kianičková, Kristína Pažitná, Lucia Kundalia, Paras H. Pakanová, Zuzana Nemčovič, Marek Baráth, Peter Katrlíková, Eva Šuba, Ján Trebatická, Jana Katrlík, Jaroslav Int J Mol Sci Article Changes in protein glycosylation are associated with most biological processes, and the importance of glycomic analysis in the research of disorders is constantly increasing, including in the neurodevelopmental field. We glycoprofiled sera in 10 children with attention-deficit hyperactivity disorder (ADHD) and 10 matching healthy controls for 3 types of samples: whole serum, sera after depletion of abundant proteins (albumin and IgG), and isolated IgG. The analytical methods used were a lectin-based glycoprotein microarray enabling high-throughput glycan analysis and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) as a standard method for the identification of glycan structures. For microarray analysis, the samples printed on microarray slides were incubated with biotinylated lectins and detected using the fluorescent conjugate of streptavidin by a microarray scanner. In the ADHD patient samples, we found increased antennary fucosylation, decreased di-/triantennary N-glycans with bisecting N-acetylglucosamine (GlcNAc), and decreased α2-3 sialylation. The results obtained by both independent methods were consistent. The study’s sample size and design do not allow far-reaching conclusions to be drawn. In any case, there is a strong demand for a better and more comprehensive diagnosis of ADHD, and the obtained results emphasize that the presented approach brings new horizons to studying functional associations of glycan alterations in ADHD. MDPI 2023-05-14 /pmc/articles/PMC10218324/ /pubmed/37240090 http://dx.doi.org/10.3390/ijms24108745 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kianičková, Kristína Pažitná, Lucia Kundalia, Paras H. Pakanová, Zuzana Nemčovič, Marek Baráth, Peter Katrlíková, Eva Šuba, Ján Trebatická, Jana Katrlík, Jaroslav Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder |
title | Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder |
title_full | Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder |
title_fullStr | Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder |
title_full_unstemmed | Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder |
title_short | Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder |
title_sort | alterations in the glycan composition of serum glycoproteins in attention-deficit hyperactivity disorder |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10218324/ https://www.ncbi.nlm.nih.gov/pubmed/37240090 http://dx.doi.org/10.3390/ijms24108745 |
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