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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1996-8-8
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pubmed:abstractText |
Alzheimer's disease is characterized by the progressive accumulation of amyloid-beta protein (Abeta) in senile plaques and cerebral amyloid angiopathy. It is not known whether the plaque growth is a continuous and homogeneous process or whether some plaques have a more rapid evolution. As plaques grow by the deposition of Abeta, we used an in situ binding technique to analyze the deposition of fluorescein-conjugated and biotinylated Abeta1 40 and Abeta1-42 in cryosections of brains from Alzheimer's disease patients. Only a subset of senile plaques but all cerebrovascular Abeta deposits were labeled by both Abeta1-40 and Abeta1-42. Striking differences in binding were observed among adjacent plaques. Quantitative analysis showed that on average 60% of all plaques were labeled with Abeta1-42 and 31% of all plaques were labeled with Abeta1-40 (n=7; P<0.001). Confocal laser scanning microscopy of double-labeled sections revealed that the newly deposited Abeta was only partially co-localized to pre-existing Abeta and apolipoprotein E and was not co-localized to heparan sulfate proteoglycan. Abeta binding was preserved after glycolytic pretreatment with periodic acid. Our results suggest that at a given time point only a subset of active senile plaques accumulate A(beta) and that plaque growth may be conditioned by the presence of other distinct plaque components different from Abeta, apolipoprotein E or heparan sulfate proteoglycan.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-1406936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-1488123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-1608956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-1730616,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-2881207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-2974240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-3292706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-7534068,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-7619525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-7629198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-7695229,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-7695621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-7706234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-7837789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-7888181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8043280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8053502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8089103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8191290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8229004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8248178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8292358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8350998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8367470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8415756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8431762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8446617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8490014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8669461-8541473
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0002-9440
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
148
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1749-56
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:8669461-Aged,
pubmed-meshheading:8669461-Aged, 80 and over,
pubmed-meshheading:8669461-Alzheimer Disease,
pubmed-meshheading:8669461-Amino Acid Sequence,
pubmed-meshheading:8669461-Amyloid beta-Peptides,
pubmed-meshheading:8669461-Brain,
pubmed-meshheading:8669461-Female,
pubmed-meshheading:8669461-Humans,
pubmed-meshheading:8669461-Immunohistochemistry,
pubmed-meshheading:8669461-Male,
pubmed-meshheading:8669461-Microscopy, Confocal,
pubmed-meshheading:8669461-Microscopy, Fluorescence,
pubmed-meshheading:8669461-Molecular Sequence Data,
pubmed-meshheading:8669461-Peptide Fragments
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pubmed:year |
1996
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pubmed:articleTitle |
Selective binding of soluble Abeta1-40 and Abeta1-42 to a subset of senile plaques.
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pubmed:affiliation |
Department of Neurology, University of Düsseldorf, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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