| pubmed-article:21585370 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21585370 | lifeskim:mentions | umls-concept:C0007806 | lld:lifeskim |
| pubmed-article:21585370 | lifeskim:mentions | umls-concept:C0221102 | lld:lifeskim |
| pubmed-article:21585370 | lifeskim:mentions | umls-concept:C0234562 | lld:lifeskim |
| pubmed-article:21585370 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:21585370 | lifeskim:mentions | umls-concept:C1416912 | lld:lifeskim |
| pubmed-article:21585370 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:21585370 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:21585370 | pubmed:dateCreated | 2011-7-13 | lld:pubmed |
| pubmed-article:21585370 | pubmed:abstractText | Amyloid-? peptide (A?) concentration in CSF is potentially a diagnostic and therapeutic target for Alzheimer's disease (AD). The purpose of this study was to clarify the elimination mechanism of human A?(1-40) [hA? (1-40)] from CSF. After intracerebroventricular (ICV) administration, [(125) I]hA?(1-40) was eliminated from the rat CSF with a half-life of 17.3 min. The elimination of [(125) I]hA?(1-40) was significantly inhibited by human receptor-associated protein (RAP) and the elimination was attenuated in either anti-low-density lipoprotein receptor-related protein (LRP)1 antibody-treated or RAP-deficient mice, suggesting that a member(s) of the low-density lipoprotein receptor gene family is involved in the elimination of hA?(1-40) from CSF. The amounts of LRP1 and LRP2 proteins were determined by means of liquid chromatography-tandem mass spectrometry, and the LRP1 content in rat choroid plexus was determined to be 3.7 fmol/?g protein, whereas the LRP2 content was below the detection limit (<0.2 fmol/?g protein). Conditionally, immortalized rat choroid plexus epithelial cells exhibited predominant apical-to-basal and apical-to-cell transport of [(125) I]hA?(1-40). These results indicated that hA?(1-40) is actively eliminated from CSF and this process is at least partly mediated by LRP1 expressed at choroid plexus epithelial cells, which therefore play a role in determining CSF concentrations of hA?(1-40). | lld:pubmed |
| pubmed-article:21585370 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21585370 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21585370 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21585370 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21585370 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21585370 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21585370 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21585370 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21585370 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21585370 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:21585370 | pubmed:issn | 1471-4159 | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:IwatsuboTakes... | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:TerasakiTetsu... | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:OhtsukiSumioS | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:HashimotoTada... | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:KamiieJunichi... | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:HosoyaKen-Ich... | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:UchidaYasuoY | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:TachikawaMasa... | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:ItoShingoS | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:FujiyoshiMasa... | lld:pubmed |
| pubmed-article:21585370 | pubmed:author | pubmed-author:AkanumaShin-I... | lld:pubmed |
| pubmed-article:21585370 | pubmed:copyrightInfo | © 2011 The Authors. Journal of Neurochemistry © 2011 International Society for Neurochemistry. | lld:pubmed |
| pubmed-article:21585370 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21585370 | pubmed:volume | 118 | lld:pubmed |
| pubmed-article:21585370 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21585370 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21585370 | pubmed:pagination | 407-15 | lld:pubmed |
| pubmed-article:21585370 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:21585370 | pubmed:meshHeading | pubmed-meshheading:21585370... | lld:pubmed |
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| pubmed-article:21585370 | pubmed:meshHeading | pubmed-meshheading:21585370... | lld:pubmed |
| pubmed-article:21585370 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21585370 | pubmed:articleTitle | Amyloid-? peptide(1-40) elimination from cerebrospinal fluid involves low-density lipoprotein receptor-related protein 1 at the blood-cerebrospinal fluid barrier. | lld:pubmed |
| pubmed-article:21585370 | pubmed:affiliation | Division of Membrane Transport and Drug Targeting, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan. | lld:pubmed |
| pubmed-article:21585370 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21585370 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:299858 | entrezgene:pubmed | pubmed-article:21585370 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21585370 | lld:entrezgene |
