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GPI-glycan structures of human Prion (M232R) from knock-in mice_LC-MSMS

ABSTRACT: To determine glycosylphosphatidylinositol (GPI) structures of human prion proteins with M232R mutation isolated from knock-in mice those express human prion protein instead of mouse one.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

SUBMITTER: Tetsuya Hirata

LAB HEAD: Taroh Kinoshita

PROVIDER: PXD037584 | Pride | 2023-03-08

REPOSITORIES: Pride

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A point mutation in GPI-attachment signal peptide accelerates the development of prion disease.

Kobayashi Atsushi A Hirata Tetsuya T Shimazaki Taishi T Munesue Yoshiko Y Aoshima Keisuke K Kimura Takashi T Nio-Kobayashi Junko J Hasebe Rie R Takeuchi Atsuko A Matsuura Yuichi Y Kusumi Satoshi S Koga Daisuke D Iwasaki Yasushi Y Kinoshita Taroh T Mohri Shirou S Kitamoto Tetsuyuki T

Acta neuropathologica 20230306 5

A missense variant from methionine to arginine at codon 232 (M232R) of the prion protein gene accounts for ~ 15% of Japanese patients with genetic prion diseases. However, pathogenic roles of the M232R substitution for the induction of prion disease have remained elusive because family history is usually absent in patients with M232R. In addition, the clinicopathologic phenotypes of patients with M232R are indistinguishable from those of sporadic Creutzfeldt-Jakob disease patients. Furthermore, ...[more]

PMID: 36879070

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