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rdf:type |
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lifeskim:mentions |
umls-concept:C0002716,
umls-concept:C0006104,
umls-concept:C0007806,
umls-concept:C0017262,
umls-concept:C0023175,
umls-concept:C0025936,
umls-concept:C0185117,
umls-concept:C0332157,
umls-concept:C0441889,
umls-concept:C0442805,
umls-concept:C1364818,
umls-concept:C1416912,
umls-concept:C1533134,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
2011-1-25
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pubmed:abstractText |
Lead (Pb) is an environmental factor suspected of contributing to neurodegenerative diseases such as Alzheimer's disease (AD). In AD, it has been postulated that increased production and/or decreased metabolism/clearance of ?-amyloid (A?) may lead to amyloid plaque deposition as well as a cascade of other neuropathological changes. It has been suggested that Pb exposure may be associated with AD-like pathology and severe memory deficits in humans. Therefore, we investigated whether Pb exposure could induce A? accumulation in the brain. In this study, we demonstrated that acute Pb treatments lead to increased levels of A? in the cerebrospinal fluid (CSF) and brain tissues. Interestingly, Pb treatments did not affect A? production in brain neurons. Furthermore, Pb treatments significantly decreased LRP1 protein expression in the choroid plexus (CP). Our results suggest disrupted LRP1-mediated transport of A? in this region may be responsible for the A? accumulation in brain.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/APP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Protein Precursor,
http://linkedlifedata.com/resource/pubmed/chemical/Lead,
http://linkedlifedata.com/resource/pubmed/chemical/Lrp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Valine
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1872-7972
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pubmed:author |
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pubmed:copyrightInfo |
© 2010 Elsevier Ireland Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
490
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16-20
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pubmed:dateRevised |
2011-10-6
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pubmed:meshHeading |
pubmed-meshheading:21167913-Amyloid beta-Peptides,
pubmed-meshheading:21167913-Amyloid beta-Protein Precursor,
pubmed-meshheading:21167913-Animals,
pubmed-meshheading:21167913-Brain,
pubmed-meshheading:21167913-Cells, Cultured,
pubmed-meshheading:21167913-Choroid Plexus,
pubmed-meshheading:21167913-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:21167913-Gene Expression Regulation,
pubmed-meshheading:21167913-Humans,
pubmed-meshheading:21167913-Lead,
pubmed-meshheading:21167913-Mass Spectrometry,
pubmed-meshheading:21167913-Mice,
pubmed-meshheading:21167913-Mice, Inbred C57BL,
pubmed-meshheading:21167913-Mice, Transgenic,
pubmed-meshheading:21167913-Mutation,
pubmed-meshheading:21167913-Neurons,
pubmed-meshheading:21167913-Phenylalanine,
pubmed-meshheading:21167913-Plaque, Amyloid,
pubmed-meshheading:21167913-Receptors, LDL,
pubmed-meshheading:21167913-Tumor Suppressor Proteins,
pubmed-meshheading:21167913-Valine
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pubmed:year |
2011
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pubmed:articleTitle |
Lead exposure increases levels of ?-amyloid in the brain and CSF and inhibits LRP1 expression in APP transgenic mice.
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pubmed:affiliation |
Department of Neurology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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