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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6293
|
| pubmed:dateCreated |
1990-11-21
|
| pubmed:abstractText |
A pathological hallmark of Alzheimer's disease is the deposition of amyloid fibrils in the brain. The principal component of the amyloid fibril is beta/A4 protein, which is derived from a large membrane-bound glycoprotein, Alzheimer amyloid protein precursor (APP). Although the deposition of amyloid is thought to result from the aberrant processing of APP, the detailed molecular mechanisms of amyloidogenesis remain unclear. A C-terminal fragment of APP which spans the beta/A4 and cytoplasmic domains has a tendency to self-aggregate. In an attempt to establish a cultured-cell model for amyloid fibril formation, we have transfected COS-1 cells with complementary DNA encoding the C-terminal 100 residues of APP. In the perinuclear regions of a small population of DNA-transfected cells, we observed inclusion-like deposits which showed a strong immunohistochemical reaction towards an anti-C-terminal APP antibody or an anti-beta/A4 amyloid core-specific antibody. Electron microscope observations of the inclusion-carrying cells revealed an accumulation of amyloid-like fibrils of 8-22 nm diameter near and on the nuclear membrane. The fibrils showed a beaded or helical structure, and reacted positively with the anti-C-terminus antibody by immunoelectron microscopy. These results suggest that the formation of amyloid fibrils is an inherent characteristic of the C-terminal peptide of APP. The present system provides a suitable model for the molecular dissection of the process of brain amyloidogenesis.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0028-0836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
11
|
| pubmed:volume |
347
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
566-9
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:1977086-Alzheimer Disease,
pubmed-meshheading:1977086-Amyloid beta-Peptides,
pubmed-meshheading:1977086-Amyloid beta-Protein Precursor,
pubmed-meshheading:1977086-Animals,
pubmed-meshheading:1977086-Base Sequence,
pubmed-meshheading:1977086-Cell Line,
pubmed-meshheading:1977086-Cercopithecus aethiops,
pubmed-meshheading:1977086-Cloning, Molecular,
pubmed-meshheading:1977086-DNA,
pubmed-meshheading:1977086-Gene Expression,
pubmed-meshheading:1977086-Immunoenzyme Techniques,
pubmed-meshheading:1977086-Immunohistochemistry,
pubmed-meshheading:1977086-Inclusion Bodies,
pubmed-meshheading:1977086-Macromolecular Substances,
pubmed-meshheading:1977086-Microscopy, Electron,
pubmed-meshheading:1977086-Microscopy, Immunoelectron,
pubmed-meshheading:1977086-Molecular Sequence Data,
pubmed-meshheading:1977086-Peptide Fragments,
pubmed-meshheading:1977086-Protein Precursors,
pubmed-meshheading:1977086-Transfection
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Formation of amyloid-like fibrils in COS cells overexpressing part of the Alzheimer amyloid protein precursor.
|
| pubmed:affiliation |
Department of Molecular Biology, Psychiatric Research Institute of Tokyo, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|