Glycobiology of Neurodegeneration: Implications of Aberrant Glycosylation in Alzheimer’s Disease

Alzheimer's disease (AD) is the most common neurodegenerative illness in the world. It is caused by the buildup of amyloid-β (Aβ) plaques and hyperphosphorylated tau neurofibrillary tangles. These protein clumps have been the main focus of treatment research, but new evidence reveals that abnormal protein glycosylation is a key part of the development of Alzheimer's disease. Glycosylation is the process by which enzymes attach carbohydrate groups to proteins. This process controls how proteins fold, how stable they are, where they are located, and what they do. This review looks at the growing evidence for dysregulated glycosylation in Alzheimer's disease (AD), with a focus on important pathogenic proteins like amyloid precursor protein (APP), tau, and other related components. We look at how changes in glycosylation patterns lead to neurodegeneration and talk about how addressing glycobiological processes could help treat Alzheimer's disease.