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Changes in Tissue Protein N-Glycosylation and Associated Molecular Signature Occur in the Human Parkinsonian Brain in a Region-Specific Manner

Ana Lúcia Rebelo, Richard R. Drake, Martina Marchetti-Deschmann, Radka Saldova, View ORCID ProfileAbhay Pandit
doi: https://doi.org/10.1101/2022.05.19.492623
Ana Lúcia Rebelo
1SFI CÚRAM Research Centre for Medical Devices, National University of Ireland Galway, Ireland
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Richard R. Drake
2Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, USA
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Martina Marchetti-Deschmann
3Institute of Chemical Technologies and Analytics, Vienna University of Technology, Vienna, Austria
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Radka Saldova
1SFI CÚRAM Research Centre for Medical Devices, National University of Ireland Galway, Ireland
4National Institute for Bioprocessing Research and Training (NIBRT), University College Dublin, Ireland
5School of Medicine, College of Health and Agricultural Science, University College Dublin, Ireland
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Abhay Pandit
1SFI CÚRAM Research Centre for Medical Devices, National University of Ireland Galway, Ireland
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  • ORCID record for Abhay Pandit
  • For correspondence: abhay.pandit@nuigalway.ie
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ABSTRACT

Parkinson’s Disease (PD) associated state of neuroinflammation due to the aggregation of aberrant proteins is widely reported. One type of post-translational modification involved in protein stability is glycosylation. Here, we aimed to spatially characterise the human Parkinsonian nigro-striatal N-glycome, and related transcriptome/proteome, and its correlation with endoplasmic reticulum stress and unfolded protein response (UPR), providing a comprehensive characterisation of the PD molecular signature.

Significant changes were seen upon PD: 3% increase in sialylation and 5% increase in fucosylation in both regions, and 2% increase in oligomannosylated N-glycans in the substantia nigra. In the latter, a decrease in the mRNA expression of sialidases and an upregulation in the UPR pathway were also seen.

This complete characterisation of the human nigro-striatal N-glycome provides an insight into the glycomic profile of PD through a transversal approach while combining the other PD “omics” pieces, which can potentially assist in the development of glyco-focused therapeutics.

Competing Interest Statement

The authors have declared no competing interest.

  • ABREVIATIONS

    ATF6
    activating transcription factor 6
    CNS
    Central nervous system
    DMB
    1,2-diamino-4,5-methylenedioxybenzene Dihydrochloride
    ER
    Endoplasmic reticulum
    ERAD
    Endoplasmic reticulum associated protein degradation
    GFAP
    Glial fibrillary acidic protein
    GRP78
    heat shock protein 70, binding immunoglobulin protein (BiP)
    GRP94
    heat shock protein 90
    HBP
    Hexosamine biosynthetic pathway
    HILIC-UPLC
    Hydrophilic Interaction Liquid Chromatography - Ultra Performance Liquid Chromatography
    Iba1
    Ionized calcium binding adaptor molecule 1
    ILBD
    Incidental Lewy body disease
    IRE1
    Inositol requiring enzyme 1
    LC-MS
    Liquid chromatography-mass spectrometry
    LLO
    Lipid-linked oligosaccharide
    PERK
    Protein kinase-like endoplasmic reticulum kinase
    PAS
    periodic acid Schiff
    PD
    Parkinson’s disease
    PDI
    Protein disulphide isomerase
    UHPLC
    Ultra-High Performance Liquid Chromatography
    UGGT
    UDP-glucose:glycoprotein glucosyltransferase
    UPR
    Unfolded protein response
    VGIC
    voltage-gated ion channels
    WAX-UPLC
    Weak Anion Exchange - Ultra Performance Liquid Chromatography
  • Copyright 
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    Posted May 20, 2022.
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    Changes in Tissue Protein N-Glycosylation and Associated Molecular Signature Occur in the Human Parkinsonian Brain in a Region-Specific Manner
    Ana Lúcia Rebelo, Richard R. Drake, Martina Marchetti-Deschmann, Radka Saldova, Abhay Pandit
    bioRxiv 2022.05.19.492623; doi: https://doi.org/10.1101/2022.05.19.492623
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    Changes in Tissue Protein N-Glycosylation and Associated Molecular Signature Occur in the Human Parkinsonian Brain in a Region-Specific Manner
    Ana Lúcia Rebelo, Richard R. Drake, Martina Marchetti-Deschmann, Radka Saldova, Abhay Pandit
    bioRxiv 2022.05.19.492623; doi: https://doi.org/10.1101/2022.05.19.492623

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