Mammalian brain glycoproteins exhibit diminished glycan complexity compared to other tissues

Sarah E. Williams, Maxence Noel, Sylvain Lehoux, Murat Cetinbas, Ramnik J. Xavier, Ruslan I. Sadreyev, Edward M. Scolnick, Jordan W. Smoller, Richard D. Cummings and Robert G. Mealer ()
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Sarah E. Williams: Massachusetts General Hospital, Harvard Medical School
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
Ruslan I. Sadreyev: Massachusetts General Hospital, Harvard Medical School
Edward M. Scolnick: Massachusetts General Hospital, Harvard Medical School
Jordan W. Smoller: 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

Nature Communications, 2022, vol. 13, issue 1, 1-16

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-021-27781-9

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