Linked Life Data

10859663

Source:http://linkedlifedata.com/resource/pubmed/id/10859663

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-7-10
pubmed:abstractText
The hypothesis is advanced that human betaA4--as opposed to rodent betaA4--may exert a protective function against the iron-induced oxidative stress associated with neurological diseases (notably Alzheimer's disease). Subsequent to its release by the host in response to oxidative injury, human betaA4 would interact with Cu(2+)ions whose level is correlatively elevated, adopting the 'aggregated' structure recently characterized by Atwood et al.(15). Then, depending on the oxidative state--hence the pH--of the medium, it might either return to its original structure if physiological pH is restored, or undergo site-specific copper-mediated oxidation and, finally, degradation. In this context, betaA4 pathogenicity could be due to an interfering mechanism preventing the degradation of the oxidized peptide, making its aggregation irreversible and inducing its final deposition. Coordination of side group oxygen donors of the oxidized peptide with 'hard' metal ions occurring in the physiological medium (notably Al(3+)) might be at the origin of this interference.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0306-9877
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Harcourt Publishers Ltd.
pubmed:issnType
Print
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
672-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Does human betaA4 exert a protective function against oxidative stress in Alzheimer's disease?
pubmed:affiliation
Equipe de Chimie Bioinorganique Médicale, Université Paul Sabatier, Toulouse, France. berthon@cict.fr
pubmed:publicationType
Journal Article