Dissecting total plasma and protein-specific glycosylation profiles in congenital disorders of glycosylation
| Autor: | Manfred Wuhrer, Agnes L. Hipgrave Ederveen, Melissa Baerenfaenger, Dirk Lefeber, Noortje de Haan |
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| Přispěvatelé: | BioAnalytical Chemistry, AIMMS |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Male
Proteomics sialic acid linkage isomers Glycosylation Nucleotide sugar glycomics lcsh:Chemistry chemistry.chemical_compound Child lcsh:QH301-705.5 Spectroscopy mass spectrometry chemistry.chemical_classification biology Chemistry Glycopeptides Blood Proteins General Medicine Disorders of movement Donders Center for Medical Neuroscience [Radboudumc 3] Blood proteins congenital disorders of glycosylation Computer Science Applications Protein Transport Biochemistry Child Preschool symbols Female Adult Glycan Adolescent Article Catalysis Inorganic Chemistry Glycomics symbols.namesake All institutes and research themes of the Radboud University Medical Center Humans Physical and Theoretical Chemistry Molecular Biology Organic Chemistry Infant Golgi apparatus Sialic acid carbohydrates (lipids) lcsh:Biology (General) lcsh:QD1-999 Transferrin Sialic Acids biology.protein Protein Processing Post-Translational |
| Zdroj: | International Journal of Molecular Sciences, 21, 20 International Journal of Molecular Sciences; Volume 21; Issue 20; Pages: 7635 International Journal of Molecular Sciences, 21 International Journal of Molecular Sciences, 21(20):7635, 1-16. Multidisciplinary Digital Publishing Institute (MDPI) International Journal of Molecular Sciences International Journal of Molecular Sciences, 21(20). MDPI Bärenfänger, J M, Hipgrave Ederveen, A, de Haan, N, Lefeber, D J & Wuhrer, M 2020, ' Dissecting Total Plasma and Protein-Specific Glycosylation Profiles in Congenital Disorders of Glycosylation ', International Journal of Molecular Sciences, vol. 21, no. 20, 7635, pp. 1-16 . https://doi.org/10.3390/ijms21207635 International Journal of Molecular Sciences, Vol 21, Iss 7635, p 7635 (2020) |
| ISSN: | 1422-0067 |
| DOI: | 10.3390/ijms21207635 |
| Popis: | Protein N-glycosylation is a multifactorial process involved in many biological processes. A broad range of congenital disorders of glycosylation (CDGs) have been described that feature defects in protein N-glycan biosynthesis. Here, we present insights into the disrupted N-glycosylation of various CDG patients exhibiting defects in the transport of nucleotide sugars, Golgi glycosylation or Golgi trafficking. We studied enzymatically released N-glycans of total plasma proteins and affinity purified immunoglobulin G (IgG) from patients and healthy controls using mass spectrometry (MS). The applied method allowed the differentiation of sialic acid linkage isomers via their derivatization. Furthermore, protein-specific glycan profiles were quantified for transferrin and IgG Fc using electrospray ionization MS of intact proteins and glycopeptides, respectively. Next to the previously described glycomic effects, we report unprecedented sialic linkage-specific effects. Defects in proteins involved in Golgi trafficking (COG5-CDG) and CMP-sialic acid transport (SLC35A1-CDG) resulted in lower levels of sialylated structures on plasma proteins as compared to healthy controls. Findings for these specific CDGs include a more pronounced effect for α2,3-sialylation than for α2,6-sialylation. The diverse abnormalities in glycomic features described in this study reflect the broad range of biological mechanisms that influence protein glycosylation. |
| Databáze: | OpenAIRE |
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