Cellular prion protein participates in amyloid-β transcytosis across the blood-brain barrier

被引：31

作者：

Pflanzner, Thorsten ^{[1
]}

Petsch, Benjamin ^{[2
]}

Andre-Dohmen, Bettina ^{[1
]}

Mueller-Schiffmann, Andreas ^{[3
]}

Tschickardt, Sabrina ^{[1
]}

Weggen, Sascha ^{[3
]}

Stitz, Lothar ^{[2
]}

Korth, Carsten ^{[3
]}

Pietrzik, Claus U. ^{[1
]}

机构：

[1] Johannes Gutenberg Univ Mainz, Inst Pathobiochem, Univ Med Ctr, D-55099 Mainz, Germany

[2] Friedrich Loeffler Inst, Inst Immunol, Tubingen, Germany

[3] Univ Dusseldorf, Dept Neuropathol, D-40225 Dusseldorf, Germany

来源：

JOURNAL OF CEREBRAL BLOOD FLOW AND METABOLISM | 2012年 / 32卷 / 04期

关键词：

Alzheimer's disease; amyloid-beta; blood-brain barrier; cellular prion protein; transcytosis; RECEPTOR-RELATED PROTEIN-1; CELLS; IMPAIRMENT; CLEARANCE; PEPTIDE;

D O I：

10.1038/jcbfm.2012.7

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

The blood-brain barrier (BBB) facilitates amyloid-beta (A beta) exchange between the blood and the brain. Here, we found that the cellular prion protein (PrPc), a putative receptor implicated in mediating A beta neurotoxicity in Alzheimer's disease (AD), participates in A beta transcytosis across the BBB. Using an in vitro BBB model, [I-125]-A beta(1-40) 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 A beta(1-40) binds to PrPc. These observations provide new mechanistic insights into the role of PrPc in AD. Journal of Cerebral Blood Flow & Metabolism (2012) 32, 628-632; doi:10.1038/jcbfm.2012.7; published online 1 February 2012

引用

页码：628 / 632

页数：5

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