rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
6501
|
pubmed:dateCreated |
1994-11-29
|
pubmed:abstractText |
The protease inhibitor alpha 1-antichymotrypsin and the lipid transport protein apolipoprotein E (apoE) are intimately associated with the 42-amino-acid beta-peptide (A beta) in the filamentous amyloid deposits of Alzheimer's disease. We report here that these two amyloid-associated proteins serve a strong stimulatory role in the polymerization of A beta into amyloid filaments. Addition of either alpha 1-anti-chymotrypsin or apoE to the A beta peptide promoted a 10- to 20-fold increase in filament formation, with apoE-4, the isoform recently linked to the development of late-onset Alzheimer's disease, showing the highest catalytic activity. These and other experiments suggest that Alzheimer amyloid deposits arise when A beta is induced to form filaments by amyloid-promoting factors (pathological chaperones) expressed in certain brain regions.
|
pubmed:commentsCorrections |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0028-0836
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
3
|
pubmed:volume |
372
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
92-4
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:7969426-Alzheimer Disease,
pubmed-meshheading:7969426-Amyloid beta-Peptides,
pubmed-meshheading:7969426-Apolipoprotein E2,
pubmed-meshheading:7969426-Apolipoprotein E3,
pubmed-meshheading:7969426-Apolipoprotein E4,
pubmed-meshheading:7969426-Apolipoproteins E,
pubmed-meshheading:7969426-Biopolymers,
pubmed-meshheading:7969426-Humans,
pubmed-meshheading:7969426-Molecular Chaperones,
pubmed-meshheading:7969426-Peptide Fragments,
pubmed-meshheading:7969426-alpha 1-Antichymotrypsin
|
pubmed:year |
1994
|
pubmed:articleTitle |
Amyloid-associated proteins alpha 1-antichymotrypsin and apolipoprotein E promote assembly of Alzheimer beta-protein into filaments.
|
pubmed:affiliation |
Department of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|