Cysteine 144 is a key residue in the copper reduction by the β-amyloid precursor protein

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dc.contributor.authorRuiz, FH
dc.contributor.authorGonzález, Y
dc.contributor.authorBodini, M
dc.contributor.authorOpazo, C
dc.contributor.authorInestrosa, NC
dc.date.accessioned2025-01-21T01:31:54Z
dc.date.available2025-01-21T01:31:54Z
dc.date.issued1999
dc.description.abstractThe beta-amyloid precursor protein (beta-APP) contains a copper-binding site localized between amino acids 135 and 156 (beta-APP(135-156)). We have employed synthetic beta-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type beta-APP(135-156) peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by beta-APP(135-156). We report here that beta-APP's copper-binding domain reduced Cu(II) to Cu(I). The single-mutant beta-APP(His147-->Ala) and the double-mutant beta-APP(His147-->Ala/His149-->Ala) showed a small decrease in copper reduction in relation to the wild-type peptide and the beta-APP(Cys144-->Ser) mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble beta-APP is involved in the reduction of Cu(II) to Cu(I).
dc.fuente.origenWOS
dc.identifier.issn0022-3042
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/97167
dc.identifier.wosidWOS:000082037000046
dc.issue.numero3
dc.language.isoen
dc.pagina.final1292
dc.pagina.inicio1288
dc.revistaJournal of neurochemistry
dc.rightsacceso restringido
dc.subjectbeta-amyloid precursor protein
dc.subjectcopper reduction
dc.subjectAlzheimer's disease
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleCysteine 144 is a key residue in the copper reduction by the β-amyloid precursor protein
dc.typeartículo
dc.volumen73
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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