Article ; Online: O-GlcNAcylation and Its Roles in Neurodegenerative Diseases.
Journal of Alzheimer's disease : JAD
2024 Volume 97, Issue 3, Page(s) 1051–1068
Abstract: As a non-classical post-translational modification, O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) is widely found in human organ systems, particularly in our brains, and is indispensable for healthy cell biology. With the ... ...
| Abstract | As a non-classical post-translational modification, O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) is widely found in human organ systems, particularly in our brains, and is indispensable for healthy cell biology. With the increasing age of the global population, the incidence of neurodegenerative diseases is increasing, too. The common characteristic of these disorders is the aggregation of abnormal proteins in the brain. Current research has found that O-GlcNAcylation dysregulation is involved in misfolding or aggregation of these abnormal proteins to mediate disease progression, but the specific mechanism has not been defined. This paper reviews recent studies on O-GlcNAcylation's roles in several neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, Huntington's disease, Machado-Joseph's disease, and giant axonal neuropathy, and shows that O-GlcNAcylation, as glucose metabolism sensor, mediating synaptic function, participating in oxidative stress response and signaling pathway conduction, directly or indirectly regulates characteristic pathological protein toxicity and affects disease progression. The existing results suggest that targeting O-GlcNAcylation will provide new ideas for clinical diagnosis, prevention, and treatment of neurodegenerative diseases. |
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| MeSH term(s) | Humans ; Neurodegenerative Diseases/metabolism ; Protein Processing, Post-Translational ; Proteins/metabolism ; Alzheimer Disease/pathology ; Acetylglucosamine/metabolism ; Disease Progression ; N-Acetylglucosaminyltransferases/metabolism | |||||
| Chemical Substances | Proteins ; Acetylglucosamine (V956696549) ; N-Acetylglucosaminyltransferases (EC 2.4.1.-) | |||||
| Language | English | |||||
| Publishing date | 2024-01-03 | |||||
| Publishing country | Netherlands | |||||
| Document type | Journal Article ; Review | |||||
| ZDB-ID | 1440127-7 | |||||
| ISSN | 1875-8908 ; 1387-2877 | |||||
| ISSN (online) | 1875-8908 | |||||
| ISSN | 1387-2877 | |||||
| DOI | 10.3233/JAD-230955 | |||||
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| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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