| pubmed-article:15294142 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C0611285 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C0078939 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C1416912 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C1417509 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C1419111 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C0962722 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C1723136 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C1869507 | lld:lifeskim |
| pubmed-article:15294142 | lifeskim:mentions | umls-concept:C2354310 | lld:lifeskim |
| pubmed-article:15294142 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15294142 | pubmed:dateCreated | 2004-8-5 | lld:pubmed |
| pubmed-article:15294142 | pubmed:abstractText | LRP (low-density lipoprotein receptor-related protein) is linked to Alzheimer's disease (AD). Here, we report amyloid beta-peptide Abeta40 binds to immobilized LRP clusters II and IV with high affinity (Kd = 0.6-1.2 nM) compared to Abeta42 and mutant Abeta, and LRP-mediated Abeta brain capillary binding, endocytosis, and transcytosis across the mouse blood-brain barrier are substantially reduced by the high beta sheet content in Abeta and deletion of the receptor-associated protein gene. Despite low Abeta production in the brain, transgenic mice expressing low LRP-clearance mutant Abeta develop robust Abeta cerebral accumulations much earlier than Tg-2576 Abeta-overproducing mice. While Abeta does not affect LRP internalization and synthesis, it promotes proteasome-dependent LRP degradation in endothelium at concentrations > 1 microM, consistent with reduced brain capillary LRP levels in Abeta-accumulating transgenic mice, AD, and patients with cerebrovascular beta-amyloidosis. Thus, low-affinity LRP/Abeta interaction and/or Abeta-induced LRP loss at the BBB mediate brain accumulation of neurotoxic Abeta. | lld:pubmed |
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| pubmed-article:15294142 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15294142 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15294142 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15294142 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15294142 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15294142 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15294142 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15294142 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15294142 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15294142 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15294142 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15294142 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15294142 | pubmed:issn | 0896-6273 | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:MehneDD | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:LentingPeter... | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:GEARJJ | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:GuoHuangH | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:DavisJudianne... | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:ZlokovicBeris... | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:SpijkersPatri... | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:SongXiaomeiX | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:WuZhenhuaZ | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:DeaneRashidR | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:Du YanShiS | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:SagareAbhayA | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:ParisiMargare... | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:LaRueBarbraB | lld:pubmed |
| pubmed-article:15294142 | pubmed:author | pubmed-author:HuHong WeiHW | lld:pubmed |
| pubmed-article:15294142 | pubmed:copyrightInfo | Copyright 2004 Cell Press | lld:pubmed |
| pubmed-article:15294142 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15294142 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:15294142 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:15294142 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15294142 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15294142 | pubmed:pagination | 333-44 | lld:pubmed |
| pubmed-article:15294142 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:15294142 | pubmed:meshHeading | pubmed-meshheading:15294142... | lld:pubmed |
| pubmed-article:15294142 | pubmed:meshHeading | pubmed-meshheading:15294142... | lld:pubmed |
| pubmed-article:15294142 | pubmed:meshHeading | pubmed-meshheading:15294142... | lld:pubmed |
| pubmed-article:15294142 | pubmed:meshHeading | pubmed-meshheading:15294142... | lld:pubmed |
| pubmed-article:15294142 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15294142 | pubmed:articleTitle | LRP/amyloid beta-peptide interaction mediates differential brain efflux of Abeta isoforms. | lld:pubmed |
| pubmed-article:15294142 | pubmed:affiliation | Frank P. Smith Laboratories for Neuroscience and Neurosurgical Research, Department of Neurosurgery, Arthur Kornberg Medical Research Building, University of Rochester Medical Center, Rochester, NY 14642, USA. | lld:pubmed |
| pubmed-article:15294142 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15294142 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15294142 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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