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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1995-1-25
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pubmed:abstractText |
Amyloid beta (A beta) is a fibrillar component in Alzheimers' disease amyloid deposits and a soluble peptide (sA beta) normally present in body fluids. We have recently reported that the blood-brain barrier (BBB) has a capability to control cerebrovascular sequestration and transport of circulating sA beta. In this study, we examined whether two circulating amyloid-associated proteins shown to bind sA beta, apolipoproteins J (apo J) and E (apo E), can cross the BBB alone and/or complexed to a synthetic peptide homologous to a major form of sA beta, sA beta 1-40. Brain perfusion experiments in guinea pigs showed significant uptake of both apo J and sA beta 1-40-apo J complexes. In contrast, blood-brain transport of sA beta 1-40-apo E was negligible, while apo E had a limited access across the BBB, indicating that the apo E found within the brain is produced locally. It is concluded that sA beta 1-40 binding to apo J and apo E results in significant (> 100-fold) difference in brain uptake of their respective complexes. We hypothesize that in normal brain apo J facilitates sA beta transport.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E,
http://linkedlifedata.com/resource/pubmed/chemical/CLU protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Clusterin,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
205
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1431-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7802679-Amyloid beta-Peptides,
pubmed-meshheading:7802679-Animals,
pubmed-meshheading:7802679-Apolipoproteins E,
pubmed-meshheading:7802679-Blood-Brain Barrier,
pubmed-meshheading:7802679-Brain,
pubmed-meshheading:7802679-Capillaries,
pubmed-meshheading:7802679-Cerebrovascular Circulation,
pubmed-meshheading:7802679-Clusterin,
pubmed-meshheading:7802679-Female,
pubmed-meshheading:7802679-Glycoproteins,
pubmed-meshheading:7802679-Guinea Pigs,
pubmed-meshheading:7802679-Humans,
pubmed-meshheading:7802679-Male,
pubmed-meshheading:7802679-Microcirculation,
pubmed-meshheading:7802679-Molecular Chaperones,
pubmed-meshheading:7802679-Peptide Fragments,
pubmed-meshheading:7802679-Protein Binding
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pubmed:year |
1994
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pubmed:articleTitle |
Brain uptake of circulating apolipoproteins J and E complexed to Alzheimer's amyloid beta.
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pubmed:affiliation |
Department of Neurological Surgery, Childrens Hospital Los Angeles, USC School of Medicine 90033.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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