ArticleScientific reports2025
Alpha-synuclein is increased in erythrocytes in parkinson's disease cases.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Antemortem α-Synuclein levels from neuron-derived extracellular vesicles identify Lewy Body pathology in Parkinson's Disease and Alzheimer Disease.medRxiv : the preprint server for health sciences · 2026Article
- von Willebrand Factor fibers formed at pathological high shear provide a scaffold for α-synuclein binding and aggregation.Scientific reports · 2026Article
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
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Authors and funding
6 authors.
Funding
Abstract
Idiopathic Parkinson's disease (iPD) is the second most common neurodegenerative disease after Alzheimer's disease (AD). Mutations in the SCNA gene, which encodes the protein alpha synuclein (α-syn), are associated with familial forms of Parkinson's disease (PD). Additionally, Lewy bodies (LBs) rich in α-synuclein are a hallmark of idiopathic Parkinson's disease (iPD) pathology. Unlike AD, there are no effective blood-based diagnostic assays for iPD. Recent studies show that measures of misfolded α-syn in cerebrospinal fluid (CSF) and skin biopsies reflect the diagnosis of iPD. The presence of misfolded α-syn suggests that the altered cellular processes in the brain that lead to aggregated α-syn may also occur in the periphery. However, CSF and skin biopsies are intrusive, highlighting the need for a blood-based diagnostic assay. Erythrocytes are the richest source of α-syn in the body, and we hypothesized that peripheral α-syn changes could be detected in erythrocytes in iPD. To test this hypothesis, we used a targeted liquid chromatography-mass spectrometry (LC-MS) assay, that included
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