Linked Life Data

8012386

Source:http://linkedlifedata.com/resource/pubmed/id/8012386

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-7-25
pubmed:abstractText
Mutations within the beta-amyloid precursor protein gene cosegregate with the early-onset form of familial Alzheimer's Disease (FAD). It is not known how these mutations result in disease; however, one early-onset AD mutation in a Swedish kindred increases potentially amyloidogenic fragments and beta-protein production in cells expressing the mutant beta-APP. Using a novel recombinant reporter system we found a qualitative change in the secreted product, from cleavage within the beta-protein sequence to cleavage near the N-terminal region of the beta-protein, even though the total amount of secreted mutant product is similar to wild-type. The results suggest that the increased formation of potentially amyloidogenic fragments in cells expressing the Swedish FAD occurs by enzymatic cleavage in the secretory pathway. Alterations in the secretory process may predispose an individual to AD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1061-4036
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
251-5
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Altered cleavage and secretion of a recombinant beta-APP bearing the Swedish familial Alzheimer's disease mutation.
pubmed:affiliation
CNS-Department of Biophysics and Molecular Biology, Bristol-Myers Squibb, Pharmaceutical Research Institute, Wallingford, Connecticut 06492.
pubmed:publicationType
Journal Article