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GPI-glycan structures of human Prion from a human brain

ABSTRACT: To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins isolated from a human brain.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

SUBMITTER: Tetsuya Hirata

LAB HEAD: Taroh Kinoshita

PROVIDER: PXD017656 | Pride | 2020-04-22

REPOSITORIES: Pride

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α2,3 linkage of sialic acid to a GPI anchor and an unpredicted GPI attachment site in human prion protein.

Kobayashi Atsushi A Hirata Tetsuya T Nishikaze Takashi T Ninomiya Akinori A Maki Yuta Y Takada Yoko Y Kitamoto Tetsuyuki T Kinoshita Taroh T

The Journal of biological chemistry 20200422 22

Prion diseases are transmissible, lethal neurodegenerative disorders caused by accumulation of the aggregated scrapie form of the prion protein (PrPSc) after conversion of the cellular prion protein (PrPC). The glycosylphosphatidylinositol (GPI) anchor of PrPC is involved in prion disease pathogenesis, and especially sialic acid in a GPI side chain reportedly affects PrPC conversion. Thus, it is important to define the location and structure of the GPI ...[more]

PMID: 32321762

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