2024
Reduced progranulin increases tau and α-synuclein inclusions and alters mouse tauopathy phenotypes via glucocerebrosidase
Takahashi H, Bhagwagar S, Nies S, Ye H, Han X, Chiasseu M, Wang G, Mackenzie I, Strittmatter S. Reduced progranulin increases tau and α-synuclein inclusions and alters mouse tauopathy phenotypes via glucocerebrosidase. Nature Communications 2024, 15: 1434. PMID: 38365772, PMCID: PMC10873339, DOI: 10.1038/s41467-024-45692-3.Peer-Reviewed Original ResearchConceptsTau inclusionsComorbid proteinopathiesTau aggregation in vitroPromotes tau aggregation in vitroAlzheimer's diseaseProgranulin reductionTDP-43 proteinopathyTauopathy phenotypeTau aggregationAD-tauHuman tauopathiesNeurofibrillary tanglesTauopathy miceReduction of progranulinPurified GlcCerTDP-43Concomitant accumulationAggregation in vitroAssociated with synucleinopathiesNeurodegenerative disordersProteinopathiesGCase inhibitionTauGCaseGlcCer
2023
Prion Protein Complex with mGluR5 Mediates Amyloid-ß Synaptic Loss in Alzheimer’s Disease
Roseman G, Fu L, Strittmatter S. Prion Protein Complex with mGluR5 Mediates Amyloid-ß Synaptic Loss in Alzheimer’s Disease. 2023, 467-481. DOI: 10.1007/978-3-031-20565-1_22.ChaptersAlzheimer's diseaseMouse modelAD transgenic mouse modelLong-term potentiation impairmentPrimary histopathological featureAD mouse modelAmyloid-beta plaquesTransgenic mouse modelPotential therapeutic targetSynaptic lossHistopathological featuresAD pathophysiologyNeuronal dysfunctionSynapse densityCognitive dysfunctionNeurofibrillary tanglesTherapeutic targetMemory deficitsCellular prion proteinMGluR5DiseaseCell death characteristicCommon formSynaptotoxicityDysfunction
2012
Role of Cellular Prion Protein in the Amyloid-β Oligomer Pathophysiology of Alzheimer’s Disease
Kaufman A, Strittmatter S. Role of Cellular Prion Protein in the Amyloid-β Oligomer Pathophysiology of Alzheimer’s Disease. 2012, 35-48. DOI: 10.1007/978-1-4614-5305-5_3.Peer-Reviewed Original ResearchAlzheimer's diseaseMouse modelCellular prion proteinPrimary histopathological featureAD mouse modelAmyloid-beta plaquesTransgenic mouse modelLong-term potentiationHistopathological featuresPrion proteinNeuronal dysfunctionNeurofibrillary tanglesMemory deficitsMemory lossDiseaseExact mechanismCommon formEssential mediatorPathophysiologyToxic effectsCell deathPrPCHigh-affinity binding partnerSynaptotoxicityDysfunction