Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state

Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state

Alzheimer’s disease (AD) is characterized by the deposition of amyloid b-peptide (Aß) and neuronal degeneration in brain regions involved in learning and memory. One of the leading etiologic hypotheses regarding AD is the involvement of free radical-mediated oxidative stress in neuronal degeneration...

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Autores principales: OPAZO,CARLOS, RUIZ,FRANCISCA H, INESTROSA,NIBALDO C
Lenguaje:English
Publicado: Sociedad de Biología de Chile 2000
Materias:
Aß peptide
amyloid fibrils
copper reduction
oxidative damage
Alzheimer’s Disease
Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602000000200012
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spelling oai:scielo:S0716-976020000002000122010-02-11Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation stateOPAZO,CARLOSRUIZ,FRANCISCA HINESTROSA,NIBALDO C Aß peptide amyloid fibrils copper reduction oxidative damage Alzheimer’s Disease Alzheimer’s disease (AD) is characterized by the deposition of amyloid b-peptide (Aß) and neuronal degeneration in brain regions involved in learning and memory. One of the leading etiologic hypotheses regarding AD is the involvement of free radical-mediated oxidative stress in neuronal degeneration. Recent evidence suggests that metals concentrated in amyloid deposits may contribute to the oxidative insults observed in AD-affected brains. We hypothesized that Aß peptide in the presence of copper enhances its neurotoxicity generating free radicals via copper reduction. In the present study, we have examined the effect of the aggregation state of amyloid-ß-peptide on copper reduction. In independent experiments we measured the copper-reducing ability of soluble and fibrillar Aß1-40 forms by bathocuproine assays. As it was previously observed for the amyloid precursor protein (APP), the Aß peptide showed copper-reducing ability. The capacity of Aß to reduce copper was independent of the aggregation state. Finally, the Aß peptide derived from the human sequence has a greater effect than the Aß peptide derived from the rat sequence, suggesting that histidine 13 may play a role in copper reduction. In agreement with this possibility, the Aß peptide reduces less copper in the presence of exogenous histidineinfo:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.33 n.2 20002000-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602000000200012en10.4067/S0716-97602000000200012
institution Scielo Chile
collection Scielo Chile
language English
topic Aß peptide
amyloid fibrils
copper reduction
oxidative damage
Alzheimer’s Disease
spellingShingle Aß peptide
amyloid fibrils
copper reduction
oxidative damage
Alzheimer’s Disease
OPAZO,CARLOS
RUIZ,FRANCISCA H
INESTROSA,NIBALDO C
Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state
description Alzheimer’s disease (AD) is characterized by the deposition of amyloid b-peptide (Aß) and neuronal degeneration in brain regions involved in learning and memory. One of the leading etiologic hypotheses regarding AD is the involvement of free radical-mediated oxidative stress in neuronal degeneration. Recent evidence suggests that metals concentrated in amyloid deposits may contribute to the oxidative insults observed in AD-affected brains. We hypothesized that Aß peptide in the presence of copper enhances its neurotoxicity generating free radicals via copper reduction. In the present study, we have examined the effect of the aggregation state of amyloid-ß-peptide on copper reduction. In independent experiments we measured the copper-reducing ability of soluble and fibrillar Aß1-40 forms by bathocuproine assays. As it was previously observed for the amyloid precursor protein (APP), the Aß peptide showed copper-reducing ability. The capacity of Aß to reduce copper was independent of the aggregation state. Finally, the Aß peptide derived from the human sequence has a greater effect than the Aß peptide derived from the rat sequence, suggesting that histidine 13 may play a role in copper reduction. In agreement with this possibility, the Aß peptide reduces less copper in the presence of exogenous histidine
author OPAZO,CARLOS
RUIZ,FRANCISCA H
INESTROSA,NIBALDO C
author_facet OPAZO,CARLOS
RUIZ,FRANCISCA H
INESTROSA,NIBALDO C
author_sort OPAZO,CARLOS
title Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state
title_short Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state
title_full Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state
title_fullStr Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state
title_full_unstemmed Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state
title_sort amyloid-ß-peptide reduces copper(ii) to copper(i) independent of its aggregation state
publisher Sociedad de Biología de Chile
publishDate 2000
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602000000200012
work_keys_str_mv AT opazocarlos amyloidßpeptidereducescopperiitocopperiindependentofitsaggregationstate
AT ruizfranciscah amyloidßpeptidereducescopperiitocopperiindependentofitsaggregationstate
AT inestrosanibaldoc amyloidßpeptidereducescopperiitocopperiindependentofitsaggregationstate
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