ArticleMolecular neurobiology2026
Glycomic Profiling Reveals Enhanced Sialylation and Plasma-Derived Fibrinogen Accumulation in the Parkinson's Disease Cerebellum.
Article in Molecular neurobiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Authors and funding
11 authors.
Funding
Abstract
Parkinson's disease (PD) is characterized by the degeneration of dopaminergic neurons in the substantia nigra, a key component of the basal ganglia. The cerebellum, which supports motor learning and cognition and forms a functional network with the basal ganglia, has been associated with both motor and non-motor symptoms of PD. N-glycosylation has been linked to neurodegeneration and alterations in cerebellar neuroimmune and synaptic regulation; however, the structural characteristics of cerebellar N-glycans remain unclear. In this study, we employed a comprehensive liquid chromatography (LC)-quadrupole-Orbitrap-tandem mass spectrometry (MS/MS)-based glycoproteomic approach to characterize N-glycans and N-glycopeptides in postmortem cerebellar tissues from neurologically normal (NM) and PD brains. Forty-two N-glycans were structurally identical but quantitatively distinct, with PD exhibiting increased sialylation (A2G2S2, A2G2S1, A2G1S1) and decreased mannosylation (M5). Glycoproteomic analysis revealed 11 N-glycopeptides in PD, six of which were unique to PD. Three PD-specific N-glycopeptides (DLQSLEDILHQVEN
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