Linked Life Data

8405269

Source:http://linkedlifedata.com/resource/pubmed/id/8405269

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-26
pubmed:abstractText
The senile plaque and congophilic angiopathy in brains of patients with Alzheimer's disease contain abnormal extracellular depositions. These depositions have very complex molecular structure, some elements of which have been identified. The most abundant protein in these structures is beta A amyloid peptide, which is produced by proteolytic processing of a larger protein, the amyloid precursor protein. It is not known how plaques and angiopathy are formed. Binding of proteins with the beta A peptide may be critical in this process. Using synthetic beta A peptides we show that the amyloid precursor protein found in cerebrospinal fluid binds beta A peptide with high avidity. Analysis of recombinant amyloid precursor proteins containing deletions of various domains demonstrate that the beta A peptide binds to the amino terminus of its own precursor. A model of plaque assembly is presented.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0014-4886
pubmed:author
pubmed:issnType
Print
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-34
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Avid binding of beta A amyloid peptide to its own precursor.
pubmed:affiliation
Department of Medicine (Neurology), Joseph and Kathleen Bryan Alzheimer's Disease Research Center, Duke University Medical Center, Durham, North Carolina 27710.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't