α-O-Glycosylation at Tyrosine 10 Promotes the Astrocyte Clearance of Amyloid-β Peptide 1-42.
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| Natura: | Artículo científico |
| Lingua: | en |
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Chembiochem : a European journal of chemical biology
2026
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| _version_ | 1868266119878410241 |
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| author | Huang, Lu Liu, Dangliang Wei, Qijia He, Changdong Zhang, Jun Dong, Suwei |
| author_facet | Huang, Lu Liu, Dangliang Wei, Qijia He, Changdong Zhang, Jun Dong, Suwei Huang, Lu Liu, Dangliang Wei, Qijia He, Changdong Zhang, Jun Dong, Suwei |
| collection | PubMed - marine biology |
| contents | α-O-Glycosylation at Tyrosine 10 Promotes the Astrocyte Clearance of Amyloid-β Peptide 1-42. Huang, Lu Liu, Dangliang Wei, Qijia He, Changdong Zhang, Jun Dong, Suwei Amyloid beta-Peptides Glycosylation Animals Peptide Fragments Astrocytes Mice Tyrosine Humans Alzheimer Disease Therapies targeting amyloid β (Aβ), especially promoting Aβ clearance, have attracted increasing attention in treating Alzheimer's disease (AD). However, the regulatory factors in Aβ metabolism remain poorly understood. Herein, three homogeneously glycosylated Aβ peptides are utilized to explore the impacts of Tyr10 O-glycosylation on Aβ clearance in astrocytes. Based on various biochemical and cellular assays, it is shown that the introduced α-O-glycan stabilizes the Aβ oligomers and enhances Aβ endocytosis and autophagy in astrocytes, which ultimately promotes the intracellular degradation of Aβ and the secretion of Aβ-degrading enzymes. Particularly, a disaccharide, Galβ1-3GalNAc, exhibits the most substantial clearance-enhancing effect. Moreover, experiments with AD-like model mice show protective effects from the disaccharide modification in alleviating Aβ-induced impairment of spatial cognitive performance. Thus, beyond showing the influences induced by particular O-glycosylation on Aβ degradation, the study provides implications of a possible role of Tyr10 O-glycan in regulating Aβ clearance in the brain. |
| format | Artículo científico |
| id | pubmed_41321280 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Chembiochem : a European journal of chemical biology |
| record_format | pubmed |
| spellingShingle | α-O-Glycosylation at Tyrosine 10 Promotes the Astrocyte Clearance of Amyloid-β Peptide 1-42. Huang, Lu Liu, Dangliang Wei, Qijia He, Changdong Zhang, Jun Dong, Suwei Amyloid beta-Peptides Glycosylation Animals Peptide Fragments Astrocytes Mice Tyrosine Humans Alzheimer Disease α-O-Glycosylation at Tyrosine 10 Promotes the Astrocyte Clearance of Amyloid-β Peptide 1-42. Huang, Lu Liu, Dangliang Wei, Qijia He, Changdong Zhang, Jun Dong, Suwei Amyloid beta-Peptides Glycosylation Animals Peptide Fragments Astrocytes Mice Tyrosine Humans Alzheimer Disease Therapies targeting amyloid β (Aβ), especially promoting Aβ clearance, have attracted increasing attention in treating Alzheimer's disease (AD). However, the regulatory factors in Aβ metabolism remain poorly understood. Herein, three homogeneously glycosylated Aβ peptides are utilized to explore the impacts of Tyr10 O-glycosylation on Aβ clearance in astrocytes. Based on various biochemical and cellular assays, it is shown that the introduced α-O-glycan stabilizes the Aβ oligomers and enhances Aβ endocytosis and autophagy in astrocytes, which ultimately promotes the intracellular degradation of Aβ and the secretion of Aβ-degrading enzymes. Particularly, a disaccharide, Galβ1-3GalNAc, exhibits the most substantial clearance-enhancing effect. Moreover, experiments with AD-like model mice show protective effects from the disaccharide modification in alleviating Aβ-induced impairment of spatial cognitive performance. Thus, beyond showing the influences induced by particular O-glycosylation on Aβ degradation, the study provides implications of a possible role of Tyr10 O-glycan in regulating Aβ clearance in the brain. |
| title | α-O-Glycosylation at Tyrosine 10 Promotes the Astrocyte Clearance of Amyloid-β Peptide 1-42. |
| topic | Amyloid beta-Peptides Glycosylation Animals Peptide Fragments Astrocytes Mice Tyrosine Humans Alzheimer Disease |
| url | https://pubmed.ncbi.nlm.nih.gov/41321280/ |