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RESEARCH PRODUCT
Cellular Prion Protein Participates in Amyloid-β Transcytosis across the Blood—Brain Barrier
Benjamin PetschCarsten KorthSascha WeggenAndreas Müller-schiffmannThorsten PflanznerSabrina TschickardtBettina André-dohmenLothar StitzClaus U. Pietrziksubject
Amyloid βanimal diseasesBiologyBrief CommunicationBlood–brain barrierModels BiologicalMiceAlzheimer Diseasemental disordersmedicineAnimalsPrPC ProteinsPrion proteinReceptorCells CulturedAmyloid beta-PeptidesNeurotoxicitymedicine.diseaseMolecular biologyPeptide FragmentsIn vitronervous system diseasesCell biologymedicine.anatomical_structureNeurologyTranscytosisBlood-Brain BarrierGene Knockdown Techniquesbiology.proteinNeurology (clinical)AntibodyTranscytosisCardiology and Cardiovascular MedicineProtein Bindingdescription
The blood—brain barrier (BBB) facilitates amyloid-β (Aβ) exchange between the blood and the brain. Here, we found that the cellular prion protein (PrPc), a putative receptor implicated in mediating Aβ neurotoxicity in Alzheimer's disease (AD), participates in Aβ transcytosis across the BBB. Using an in vitro BBB model, [125I]-Aβ1–40 transcytosis was reduced by genetic knockout of PrPc or after addition of a competing PrPc-specific antibody. Furthermore, we provide evidence that PrPc is expressed in endothelial cells and, that monomeric Aβ1–40 binds to PrPc. These observations provide new mechanistic insights into the role of PrPc in AD.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2012-02-02 | Journal of Cerebral Blood Flow & Metabolism |