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Mammalian brain glycoproteins exhibit diminished glycan complexity compared to other tissues

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Listed:
  • Sarah E. Williams

    (Massachusetts General Hospital, Harvard Medical School
    Beth Israel Deaconess Medical Center, Harvard Medical School
    Icahn School of Medicine at Mount Sinai)

  • Maxence Noel

    (Beth Israel Deaconess Medical Center, Harvard Medical School)

  • Sylvain Lehoux

    (Beth Israel Deaconess Medical Center, Harvard Medical School)

  • Murat Cetinbas

    (Massachusetts General Hospital, Harvard Medical School)

  • Ramnik J. Xavier

    (Massachusetts General Hospital, Harvard Medical School
    Massachusetts General Hospital, Harvard Medical School)

  • Ruslan I. Sadreyev

    (Massachusetts General Hospital, Harvard Medical School)

  • Edward M. Scolnick

    (Massachusetts General Hospital, Harvard Medical School
    The Stanley Center for Psychiatric Research at Broad Institute of Harvard/MIT)

  • Jordan W. Smoller

    (Massachusetts General Hospital, Harvard Medical School
    The Stanley Center for Psychiatric Research at Broad Institute of Harvard/MIT
    Massachusetts General Hospital, Harvard Medical School)

  • Richard D. Cummings

    (Beth Israel Deaconess Medical Center, Harvard Medical School)

  • Robert G. Mealer

    (Massachusetts General Hospital, Harvard Medical School
    Beth Israel Deaconess Medical Center, Harvard Medical School
    The Stanley Center for Psychiatric Research at Broad Institute of Harvard/MIT
    Massachusetts General Hospital, Harvard Medical School)

Abstract

Glycosylation is essential to brain development and function, but prior studies have often been limited to a single analytical technique and excluded region- and sex-specific analyses. Here, using several methodologies, we analyze Asn-linked and Ser/Thr/Tyr-linked protein glycosylation between brain regions and sexes in mice. Brain N-glycans are less complex in sequence and variety compared to other tissues, consisting predominantly of high-mannose and fucosylated/bisected structures. Most brain O-glycans are unbranched, sialylated O-GalNAc and O-mannose structures. A consistent pattern is observed between regions, and sex differences are minimal compared to those in plasma. Brain glycans correlate with RNA expression of their synthetic enzymes, and analysis of glycosylation genes in humans show a global downregulation in the brain compared to other tissues. We hypothesize that this restricted repertoire of protein glycans arises from their tight regulation in the brain. These results provide a roadmap for future studies of glycosylation in neurodevelopment and disease.

Suggested Citation

  • Sarah E. Williams & Maxence Noel & Sylvain Lehoux & Murat Cetinbas & Ramnik J. Xavier & Ruslan I. Sadreyev & Edward M. Scolnick & Jordan W. Smoller & Richard D. Cummings & Robert G. Mealer, 2022. "Mammalian brain glycoproteins exhibit diminished glycan complexity compared to other tissues," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-021-27781-9
    DOI: 10.1038/s41467-021-27781-9
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    Cited by:

    1. Diego E. Sastre & Nazneen Sultana & Marcos V. A. S. Navarro & Maros Huliciak & Jonathan Du & Javier O. Cifuente & Maria Flowers & Xu Liu & Pete Lollar & Beatriz Trastoy & Marcelo E. Guerin & Eric J. S, 2024. "Human gut microbes express functionally distinct endoglycosidases to metabolize the same N-glycan substrate," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Shweta Godbole & Hannah Voß & Antonia Gocke & Simon Schlumbohm & Yannis Schumann & Bojia Peng & Martin Mynarek & Stefan Rutkowski & Matthias Dottermusch & Mario M. Dorostkar & Andrey Korshunov & Thoma, 2024. "Multiomic profiling of medulloblastoma reveals subtype-specific targetable alterations at the proteome and N-glycan level," Nature Communications, Nature, vol. 15(1), pages 1-24, December.

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