Cellular Prion Protein Participates in Amyloid-β Transcytosis across the Blood—Brain Barrier
T Pflanzner, B Petsch… - Journal of Cerebral …, 2012 - journals.sagepub.com
T Pflanzner, B Petsch, B André-Dohmen, A Müller-Schiffmann, S Tschickardt, S Weggen…
Journal of Cerebral Blood Flow & Metabolism, 2012•journals.sagepub.comThe 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 …
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 …
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.
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