000056067 001__ 56067
000056067 005__ 20200221144250.0
000056067 0247_ $$2doi$$a10.1021/jacs.5b13577
000056067 0248_ $$2sideral$$a95015
000056067 037__ $$aART-2016-95015
000056067 041__ $$aeng
000056067 100__ $$aPedersen, J.T.
000056067 245__ $$aAmyloid-ß and a-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing
000056067 260__ $$c2016
000056067 5060_ $$aAccess copy available to the general public$$fUnrestricted
000056067 5203_ $$aThe formation of reactive oxygen species (ROS) is linked to the pathogenesis of neurodegenerative diseases. Here we have investigated the effect of soluble and aggregated amyloid-ß (Aß) and a-synuclein (aS), associated with Alzheimer''s and Parkinson''s diseases, respectively, on the Cu2+-catalyzed formation of ROS in vitro in the presence of a biological reductant. We find that the levels of ROS, and the rate by which ROS is generated, are significantly reduced when Cu2+ is bound to Aß or aS, particularly when they are in their oligomeric or fibrillar forms. This effect is attributed to a combination of radical scavenging and redox silencing mechanisms. Our findings suggest that the increase in ROS associated with the accumulation of aggregated Aß or aS does not result from a particularly ROS-active form of these peptides, but rather from either a local increase of Cu2+ and other ROS-active metal ions in the aggregates or as a downstream consequence of the formation of the pathological amyloid structures.
000056067 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000056067 590__ $$a13.858$$b2016
000056067 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b10 / 166 = 0.06$$c2016$$dQ1$$eT1
000056067 592__ $$a7.492$$b2016
000056067 593__ $$aBiochemistry$$c2016$$dQ1
000056067 593__ $$aColloid and Surface Chemistry$$c2016$$dQ1
000056067 593__ $$aChemistry (miscellaneous)$$c2016$$dQ1
000056067 593__ $$aCatalysis$$c2016$$dQ1
000056067 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000056067 700__ $$aChen, S.W.
000056067 700__ $$aBorg, C.B.
000056067 700__ $$aNess, S.
000056067 700__ $$aBahl, J.M.
000056067 700__ $$aHeegaard, N.H.H.
000056067 700__ $$aDobson, C.M.
000056067 700__ $$aHemmingsen, L.
000056067 700__ $$0(orcid)0000-0002-9138-6687$$aCremades, N.$$uUniversidad de Zaragoza
000056067 700__ $$aTeilum, K.
000056067 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000056067 773__ $$g138, 12 (2016), 3966-3969$$pJ. Am. Chem. Soc.$$tJOURNAL OF THE AMERICAN CHEMICAL SOCIETY$$x0002-7863
000056067 8564_ $$s1085384$$uhttps://zaguan.unizar.es/record/56067/files/texto_completo.pdf$$yVersión publicada
000056067 8564_ $$s131738$$uhttps://zaguan.unizar.es/record/56067/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000056067 909CO $$ooai:zaguan.unizar.es:56067$$particulos$$pdriver
000056067 951__ $$a2020-02-21-13:27:07
000056067 980__ $$aARTICLE