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rdf:type |
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lifeskim:mentions |
umls-concept:C0005854,
umls-concept:C0014139,
umls-concept:C0030956,
umls-concept:C0033414,
umls-concept:C0243125,
umls-concept:C0597601,
umls-concept:C0699900,
umls-concept:C1416912,
umls-concept:C1417509,
umls-concept:C1419111,
umls-concept:C1515654
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pubmed:issue |
1
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pubmed:dateCreated |
2008-3-21
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pubmed:abstractText |
The pathogenesis of Alzheimer's disease is characterized by aggregation of the amyloid-beta protein (Abeta) into neurotoxic plaques. Recent in vivo studies have suggested the non-proteolytic clearance of Abeta via receptor-mediated transport across the blood-brain barrier (BBB). The aim of this study was to investigate the role of P-glycoprotein (Pgp) and the low-density lipoprotein receptor-related protein (LRP) in Abeta efflux across the BBB. We developed an in vitro BBB-like model using Madin-Darby Canine Kidney (MDCK) cells seeded on filters separating apical (blood) and basolateral (brain) compartments. MDCK cells were stably transfected with Pgp or mLRP4, an LRP mini-receptor. When compared to empty vector-transfected cells, MDCK-Pgp cells did not transcytose radiolabeled Abeta in the basolateral-to-apical direction. MDCK-mLRP4 cells were found to endocytose and degrade, but not to trasncytose intact radiolabeled Abeta. These results implicate LRP as a mediator of Abeta degradation, but indicate that overexpression of LRP or Pgp alone is insufficient for non-proteolytic transcytosis of intact Abeta.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-10202530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-11067868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-11120756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-11181173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-11745727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-12130773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-12415125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-12694565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-12878439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-15125776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-15140180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-15294142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-15339642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-15713540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-16141364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-16239972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-16639431,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-16930455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-2269660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-2574723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-6980688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-7979249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-8108445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-9222170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-9425600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-9822694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18289866-9874698
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1095-953X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
94-102
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:18289866-Amyloid beta-Peptides,
pubmed-meshheading:18289866-Analysis of Variance,
pubmed-meshheading:18289866-Animals,
pubmed-meshheading:18289866-Biological Transport,
pubmed-meshheading:18289866-Biotinylation,
pubmed-meshheading:18289866-Blood-Brain Barrier,
pubmed-meshheading:18289866-Calcium Channel Blockers,
pubmed-meshheading:18289866-Cell Line, Transformed,
pubmed-meshheading:18289866-Dogs,
pubmed-meshheading:18289866-Endocytosis,
pubmed-meshheading:18289866-Epithelial Cells,
pubmed-meshheading:18289866-Hormone Antagonists,
pubmed-meshheading:18289866-Iodine Isotopes,
pubmed-meshheading:18289866-Low Density Lipoprotein Receptor-Related Protein-1,
pubmed-meshheading:18289866-Mifepristone,
pubmed-meshheading:18289866-Models, Biological,
pubmed-meshheading:18289866-P-Glycoprotein,
pubmed-meshheading:18289866-Peptide Fragments,
pubmed-meshheading:18289866-Time Factors,
pubmed-meshheading:18289866-Transfection,
pubmed-meshheading:18289866-Verapamil
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pubmed:year |
2008
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pubmed:articleTitle |
LRP promotes endocytosis and degradation, but not transcytosis, of the amyloid-beta peptide in a blood-brain barrier in vitro model.
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pubmed:affiliation |
Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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