ArticleScientific reports2019
Abundant neuroprotective chaperone Lipocalin-type prostaglandin D synthase (L-PGDS) disassembles the Amyloid-β fibrils.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Cell-based polygenic risk scores predict clinical progression and prioritize network-based therapeutic targets in Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026Article
- Apolipoprotein D acts as a chaperone of Aβ peptide delaying its assembly into amyloid aggregates.Cellular and molecular life sciences : CMLS · 2026Article
- Mirtazapine Induces Lipocalin-Type Prostaglandin D Synthase Expression in Brain Pericytes.Biomolecules · 2026Article
- Broken but not beaten: Challenge of reducing the amyloids pathogenicity by degradation.Journal of advanced research · 2025Review
- On the reversibility of amyloid fibril formation.Biophysics reviews · 2025Review
- APOE from astrocytes restores Alzheimer's Aβ-pathology and DAM-like responses in APOE deficient microglia.EMBO molecular medicine · 2024Article
- Article
- Article
- Normal-Tension Glaucoma and Potential Clinical Links to Alzheimer's Disease.Journal of clinical medicine · 2024Review
- Lipocalin-type prostaglandin D synthase: a glymphopathy marker in idiopathic hydrocephalus.Frontiers in aging neuroscience · 2024Article
- Prostaglandins in the Inflamed Central Nervous System: Potential Therapeutic Targets.Current drug targets · 2024Review
- Proteomics of the astrocyte secretome reveals changes in their response to soluble oligomeric Aβ.Journal of neurochemistry · 2023Article
- Chaperone Activity and Protective Effect against Aβ-Induced Cytotoxicity ofPharmaceuticals (Basel, Switzerland) · 2023Article
- Release of frustration drives corneal amyloid disaggregation by brain chaperone.Communications biology · 2023Article
- Analyzing alternative splicing in Alzheimer's disease postmortem brain: a cell-level perspective.Frontiers in molecular neuroscience · 2023Article
- Amyloid Disassembly: What Can We Learn from Chaperones?Biomedicines · 2022Review
- Timapiprant, a prostaglandin D2 receptor antagonist, ameliorates pathology in a rat Alzheimer's model.Life science alliance · 2022Article
- Clusterin, other extracellular chaperones, and eye disease.Progress in retinal and eye research · 2022Review
- In vivo liquid-liquid phase separation protects amyloidogenic and aggregation-prone peptides during overexpression in Escherichia coli.Protein science : a publication of the Protein Society · 2022Article
- High Correlation among Brain-Derived Major Protein Levels in Cerebrospinal Fluid: Implication for Amyloid-Beta and Tau Protein Changes in Alzheimer's Disease.Metabolites · 2022Article
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13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Misfolding of Amyloid β (Aβ) peptides leads to the formation of extracellular amyloid plaques. Molecular chaperones can facilitate the refolding or degradation of such misfolded proteins. Here, for the first time, we report the unique ability of Lipocalin-type Prostaglandin D synthase (L-PGDS) protein to act as a disaggregase on the pre-formed fibrils of Aβ(1-40), abbreviated as Aβ40, and Aβ(25-35) peptides, in addition to inhibiting the aggregation of Aβ monomers. Furthermore, our proteomics results indicate that L-PGDS can facilitate extraction of several other proteins from the insoluble aggregates extracted from the brain of an Alzheimer's disease patient. In this study, we have established the mode of binding of L-PGDS with monomeric and fibrillar Aβ using Nuclear Magnetic Resonance (NMR) Spectroscopy, Small Angle X-ray Scattering (SAXS), and Transmission Electron Microscopy (TEM). Our results confirm a direct interaction between L-PGDS and monomeric Aβ40 and Aβ(25-35), thereby inhibiting their spontaneous aggregation. The monomeric unstructured Aβ40 binds to L-PGDS via its C-terminus, while the N-terminus remains free which is observed as a new domain in the L-PGDS-Aβ40 complex model.
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