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

• Published in: The Journal of biological chemistry Vol. 298; no. 3; p. 101720
• Main Authors: Hirata, Tetsuya, Kobayashi, Atsushi, Furuse, Tamio, Yamada, Ikuko, Tamura, Masaru, Tomita, Hiroyuki, Tokoro, Yuko, Ninomiya, Akinori, Fujihara, Yoshitaka, Ikawa, Masahito, Maeda, Yusuke, Murakami, Yoshiko, Kizuka, Yasuhiko, Kinoshita, Taroh
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.2022; American Society for Biochemistry and Molecular Biology
• Subjects: Acetylgalactosamine - chemistry; Acetylgalactosamine - metabolism; Animals; bone formation; Brain - metabolism; brain function; Creutzfeldt–Jakob disease; glycosylation; Glycosylphosphatidylinositols - chemistry; Glycosylphosphatidylinositols - metabolism; glycosyltransferase; GPI; Mice; Osteogenesis; prion; Prion Diseases - metabolism; Prions - metabolism; Structure-Activity Relationship; GPI; PrPSc; ALP; IHC; HRP; brain function; 2ME; WB; RBC; DW; prion; Creutzfeldt–Jakob disease; ISH; TBS; GSS; MS; IGD; glycosylation; ER; GPI-AP; ES; PrPC; glycosyltransferase; bone formation; PK; DRM

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 PrPC, have a glycan side chain composed of N-acetylgalactosamine (GalNAc)...