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Mammalian brain glycoproteins exhibit diminished glycan complexity compared to other tissues.
Williams, Sarah E; Noel, Maxence; Lehoux, Sylvain; Cetinbas, Murat; Xavier, Ramnik J; Sadreyev, Ruslan I; Scolnick, Edward M; Smoller, Jordan W; Cummings, Richard D; Mealer, Robert G.
Afiliação
  • Williams SE; Psychiatric and Neurodevelopmental Genetics Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
  • Noel M; Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
  • Lehoux S; Nash Family Department of Neuroscience, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
  • Cetinbas M; Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
  • Xavier RJ; Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
  • Sadreyev RI; Department of Molecular Biology, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
  • Scolnick EM; Department of Molecular Biology, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
  • Smoller JW; Center for Computational and Integrative Biology, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
  • Cummings RD; Department of Molecular Biology, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
  • Mealer RG; Psychiatric and Neurodevelopmental Genetics Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
Nat Commun ; 13(1): 275, 2022 01 12.
Article em En | MEDLINE | ID: mdl-35022400
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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Encéfalo / Glicoproteínas Limite: Animals Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Polissacarídeos / Encéfalo / Glicoproteínas Limite: Animals Idioma: En Ano de publicação: 2022 Tipo de documento: Article