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...
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MDPI AG
2023-05-01
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| Series: | International Journal of Molecular Sciences |
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| author | Kristína Kianičková Lucia Pažitná Paras H. Kundalia Zuzana Pakanová Marek Nemčovič Peter Baráth Eva Katrlíková Ján Šuba Jana Trebatická Jaroslav Katrlík |
| author_facet | Kristína Kianičková Lucia Pažitná Paras H. Kundalia Zuzana Pakanová Marek Nemčovič Peter Baráth Eva Katrlíková Ján Šuba Jana Trebatická Jaroslav Katrlík |
| author_sort | Kristína Kianičková |
| collection | DOAJ |
| 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. |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T03:39:23Z |
| publishDate | 2023-05-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-3550fd86a7444f05b7f009df8ded2b202023-11-18T01:41:08ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-05-012410874510.3390/ijms24108745Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity DisorderKristína Kianičková0Lucia Pažitná1Paras H. Kundalia2Zuzana Pakanová3Marek Nemčovič4Peter Baráth5Eva Katrlíková6Ján Šuba7Jana Trebatická8Jaroslav Katrlík9Institute of Chemistry, Slovak Academy of Sciences, SK-84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, SK-84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, SK-84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, SK-84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, SK-84538 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, SK-84538 Bratislava, SlovakiaDepartment of Paediatric Psychiatry, Faculty of Medicine, Comenius University, The National Institute of Children’s Diseases, SK-83340 Bratislava, SlovakiaDepartment of Paediatric Psychiatry, Faculty of Medicine, Comenius University, The National Institute of Children’s Diseases, SK-83340 Bratislava, SlovakiaDepartment of Paediatric Psychiatry, Faculty of Medicine, Comenius University, The National Institute of Children’s Diseases, SK-83340 Bratislava, SlovakiaInstitute of Chemistry, Slovak Academy of Sciences, SK-84538 Bratislava, SlovakiaChanges 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.https://www.mdpi.com/1422-0067/24/10/8745glycosylationADHDlectin-based glycoprotein microarrayMALDI-TOF mass spectrometrybiomarker |
| spellingShingle | Kristína Kianičková Lucia Pažitná Paras H. Kundalia Zuzana Pakanová Marek Nemčovič Peter Baráth Eva Katrlíková Ján Šuba Jana Trebatická Jaroslav Katrlík Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder International Journal of Molecular Sciences glycosylation ADHD lectin-based glycoprotein microarray MALDI-TOF mass spectrometry biomarker |
| 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 | glycosylation ADHD lectin-based glycoprotein microarray MALDI-TOF mass spectrometry biomarker |
| url | https://www.mdpi.com/1422-0067/24/10/8745 |
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