Linked Life Data

21585370

Source:http://linkedlifedata.com/resource/pubmed/id/21585370

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-7-13
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).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1471-4159
pubmed:author
pubmed:copyrightInfo
© 2011 The Authors. Journal of Neurochemistry © 2011 International Society for Neurochemistry.
pubmed:issnType
Electronic
pubmed:volume
118
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
407-15
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:21585370-Algorithms, pubmed-meshheading:21585370-Amyloid beta-Peptides, pubmed-meshheading:21585370-Animals, pubmed-meshheading:21585370-Biological Transport, Active, pubmed-meshheading:21585370-Blood-Brain Barrier, pubmed-meshheading:21585370-Cell Line, pubmed-meshheading:21585370-Choroid Plexus, pubmed-meshheading:21585370-Injections, Intraventricular, pubmed-meshheading:21585370-Kinetics, pubmed-meshheading:21585370-Low Density Lipoprotein Receptor-Related Protein-1, pubmed-meshheading:21585370-Low Density Lipoprotein Receptor-Related Protein-2, pubmed-meshheading:21585370-Male, pubmed-meshheading:21585370-Mass Spectrometry, pubmed-meshheading:21585370-Mice, pubmed-meshheading:21585370-Mice, Inbred C57BL, pubmed-meshheading:21585370-Peptide Fragments, pubmed-meshheading:21585370-Rats, pubmed-meshheading:21585370-Rats, Sprague-Dawley
pubmed:year
2011
pubmed:articleTitle
Amyloid-? peptide(1-40) elimination from cerebrospinal fluid involves low-density lipoprotein receptor-related protein 1 at the blood-cerebrospinal fluid barrier.
pubmed:affiliation
Division of Membrane Transport and Drug Targeting, Graduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't