Proteomics

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GPI-glycan structures of Prion from PGAP4-KO mouse brains


ABSTRACT: To determine glycosylphosphatidylinositol (GPI) structures of prion proteins isolated from PGAP4-KO mouse brains.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Brain

SUBMITTER: Tetsuya Hirata  

LAB HEAD: Taroh Kinoshita

PROVIDER: PXD029189 | Pride | 2022-04-04

REPOSITORIES: Pride

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Publications

Loss of the N-acetylgalactosamine side chain of the GPI-anchor impairs bone formation and brain functions and accelerates the prion disease pathology.

Hirata Tetsuya T   Kobayashi Atsushi A   Furuse Tamio T   Yamada Ikuko I   Tamura Masaru M   Tomita Hiroyuki H   Tokoro Yuko Y   Ninomiya Akinori A   Fujihara Yoshitaka Y   Ikawa Masahito M   Maeda Yusuke Y   Murakami Yoshiko Y   Kizuka Yasuhiko Y   Kinoshita Taroh T  

The Journal of biological chemistry 20220211 3


Glycosylphosphatidylinositol (GPI) is a posttranslational glycolipid modification of proteins that anchors proteins in lipid rafts on the cell surface. Although some GPI-anchored proteins (GPI-APs), including the prion protein PrP<sup>C</sup>, have a glycan side chain composed of N-acetylgalactosamine (GalNAc)-galactose-sialic acid on the core structure of GPI glycolipid, in vivo functions of this GPI-GalNAc side chain are largely unresolved. Here, we investigated the physiological and pathologi  ...[more]

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