ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
Extracellular LCN2 Binding to 24p3R in Astrocytes Impedes α-Synuclein Endocytosis in Parkinson's Disease.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Colchicine alleviates severe acute pancreatitis in rats by inhibiting acinar cell ferroptosisEuropean journal of histochemistry : EJH · 2026Article
- Axonopathy: mechanisms and potential therapeutic targets for neurodegenerative diseases.Translational neurodegeneration · 2026Review
- RRx-001 ameliorates astrocyte pyroptosis by regulating LCN2-NLRP3 inflammasome activation in an MPTP-induced parkinson's disease mouse model.Cellular and molecular life sciences : CMLS · 2026Article
- Extracellular LCN2 Binding to 24p3R in Astrocytes Impedes α-Synuclein Endocytosis in Parkinson's Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Astrocytic and microglial cell functions in neuroinflammatory diseases and their animal models.Frontiers in cellular neuroscience · 2025Review
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Authors and funding
15 authors.
Funding
Abstract
The spread or transmission of pathologic α-synuclein (α-Syn) is emerging as potentially important driver of Parkinson's disease (PD) pathogenesis. Emerging evidence suggests that astrocytes play an important role in uptake/clearance of extracellular α-Syn. However, underlying mechanisms and molecular entities responsible for uptake/clearance of extracellular α-Syn by astrocytes are not known. Here, it is shown that lipocalin-2 (LCN2) is upregulated in astrocytes of MPTP-treated mice by RNA-Seq analysis and positively correlates with pathologic α-Syn level in α-Syn PFF model. Strikingly, deletion of astrocytic LCN2 significantly prevents the pathologic α-Syn accumulation and neurodegeneration. Moreover, 24p3R as a crucial receptor of α-Syn uptake by astrocytes is identified, as well as an important mediator of α-Syn spread in the brain. 24p3R specifically binds to α-Syn and then mediates α-Syn uptake. LCN2 prevents astrocytic uptake of α-Syn by impeding the binding of 24p3R and α-Syn. The identification of LCN2/24p3R as a key regulator of α-Syn by astrocytes provides a new target for the treatment of PD and related α-synucleinopathies.
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