Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing

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Standard

Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing. / Pedersen, Jeppe Trudslev; Chen, Serene W.; Borg, Christian Bernsen; Ness, Samuel; Bahl, Justyna M.; Heegard, Niels H. H.; Dobson, Christopher M.; Hemmingsen, Lars Bo Stegeager; Cremades, Nunilo; Teilum, Kaare.

I: Journal of the American Chemical Society, Bind 138, Nr. 12, 2016, s. 3966-3969.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Pedersen, JT, Chen, SW, Borg, CB, Ness, S, Bahl, JM, Heegard, NHH, Dobson, CM, Hemmingsen, LBS, Cremades, N & Teilum, K 2016, 'Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing', Journal of the American Chemical Society, bind 138, nr. 12, s. 3966-3969. https://doi.org/10.1021/jacs.5b13577

APA

Pedersen, J. T., Chen, S. W., Borg, C. B., Ness, S., Bahl, J. M., Heegard, N. H. H., Dobson, C. M., Hemmingsen, L. B. S., Cremades, N., & Teilum, K. (2016). Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing. Journal of the American Chemical Society, 138(12), 3966-3969. https://doi.org/10.1021/jacs.5b13577

Vancouver

Pedersen JT, Chen SW, Borg CB, Ness S, Bahl JM, Heegard NHH o.a. Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing. Journal of the American Chemical Society. 2016;138(12):3966-3969. https://doi.org/10.1021/jacs.5b13577

Author

Pedersen, Jeppe Trudslev ; Chen, Serene W. ; Borg, Christian Bernsen ; Ness, Samuel ; Bahl, Justyna M. ; Heegard, Niels H. H. ; Dobson, Christopher M. ; Hemmingsen, Lars Bo Stegeager ; Cremades, Nunilo ; Teilum, Kaare. / Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing. I: Journal of the American Chemical Society. 2016 ; Bind 138, Nr. 12. s. 3966-3969.

Bibtex

@article{de5f8be3548749a18c6ef65484d274f6,
title = "Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing",
abstract = "The formation of reactive oxygen species (ROS) is linked to the pathogenesis of Alzheimer's and Parkinson's diseases. Here we have investigated the effect of soluble and aggregated Aβ and α-synuclein, associated with Alzheimer's and Parkinson's disease 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 the Cu2+ is bound to Aβ or α-synuclein, particularly when they are in the 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 Aβ or α-synuclein 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 patho-logical amyloid structures.",
author = "Pedersen, {Jeppe Trudslev} and Chen, {Serene W.} and Borg, {Christian Bernsen} and Samuel Ness and Bahl, {Justyna M.} and Heegard, {Niels H. H.} and Dobson, {Christopher M.} and Hemmingsen, {Lars Bo Stegeager} and Nunilo Cremades and Kaare Teilum",
year = "2016",
doi = "10.1021/jacs.5b13577",
language = "English",
volume = "138",
pages = "3966--3969",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "ACS Publications",
number = "12",

}

RIS

TY - JOUR

T1 - Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing

AU - Pedersen, Jeppe Trudslev

AU - Chen, Serene W.

AU - Borg, Christian Bernsen

AU - Ness, Samuel

AU - Bahl, Justyna M.

AU - Heegard, Niels H. H.

AU - Dobson, Christopher M.

AU - Hemmingsen, Lars Bo Stegeager

AU - Cremades, Nunilo

AU - Teilum, Kaare

PY - 2016

Y1 - 2016

N2 - The formation of reactive oxygen species (ROS) is linked to the pathogenesis of Alzheimer's and Parkinson's diseases. Here we have investigated the effect of soluble and aggregated Aβ and α-synuclein, associated with Alzheimer's and Parkinson's disease 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 the Cu2+ is bound to Aβ or α-synuclein, particularly when they are in the 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 Aβ or α-synuclein 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 patho-logical amyloid structures.

AB - The formation of reactive oxygen species (ROS) is linked to the pathogenesis of Alzheimer's and Parkinson's diseases. Here we have investigated the effect of soluble and aggregated Aβ and α-synuclein, associated with Alzheimer's and Parkinson's disease 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 the Cu2+ is bound to Aβ or α-synuclein, particularly when they are in the 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 Aβ or α-synuclein 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 patho-logical amyloid structures.

U2 - 10.1021/jacs.5b13577

DO - 10.1021/jacs.5b13577

M3 - Journal article

C2 - 26967463

VL - 138

SP - 3966

EP - 3969

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 12

ER -

ID: 158550918