Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126.

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Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126. / Turnbull, Stuart; Tabner, Brian J.; Brown, David R. et al.
In: Neuroscience Letters, Vol. 336, No. 3, 23.01.2003, p. 159-162.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Turnbull, S, Tabner, BJ, Brown, DR & Allsop, D 2003, 'Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126.', Neuroscience Letters, vol. 336, no. 3, pp. 159-162. https://doi.org/10.1016/S0304-3940(02)01254-5

APA

Turnbull, S., Tabner, B. J., Brown, D. R., & Allsop, D. (2003). Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126. Neuroscience Letters, 336(3), 159-162. https://doi.org/10.1016/S0304-3940(02)01254-5

Vancouver

Turnbull S, Tabner BJ, Brown DR, Allsop D. Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126. Neuroscience Letters. 2003 Jan 23;336(3):159-162. doi: 10.1016/S0304-3940(02)01254-5

Author

Turnbull, Stuart ; Tabner, Brian J. ; Brown, David R. et al. / Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126. In: Neuroscience Letters. 2003 ; Vol. 336, No. 3. pp. 159-162.

Bibtex

@article{49363b4eb3de472f98855503c4eea4c8,

title = "Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126.",

abstract = "Oligomeric forms of many of the aggregating proteins associated with neurodegenerative diseases are toxic to cultured cells. We have shown recently that Aβ and -synuclein can both induce the formation of hydroxyl radicals following incubation in solution, upon the addition of Fe(II). Thus, they appear to generate hydrogen peroxide, which is converted to hydroxyl radicals via the Fenton reaction. Here we show that the widely studied toxic peptide fragment of the prion protein, PrP106–126, has exactly the same property, but only in the presence of copper ions. Since the aggregation and toxicity of PrP106–126 have been reported to be critically dependent on copper binding, our data suggest that the published cytotoxic effects of this peptide could also be due to its ability to generate hydrogen peroxide.",

keywords = "Copper, Free radicals, Hydrogen peroxide, Oxidative stress, Prion protein",

author = "Stuart Turnbull and Tabner, {Brian J.} and Brown, {David R.} and David Allsop",

year = "2003",

month = jan,

day = "23",

doi = "10.1016/S0304-3940(02)01254-5",

language = "English",

volume = "336",

pages = "159--162",

journal = "Neuroscience Letters",

issn = "0304-3940",

publisher = "ELSEVIER IRELAND LTD",

number = "3",

}

RIS

TY - JOUR

T1 - Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126.

AU - Turnbull, Stuart

AU - Tabner, Brian J.

AU - Brown, David R.

AU - Allsop, David

PY - 2003/1/23

Y1 - 2003/1/23

N2 - Oligomeric forms of many of the aggregating proteins associated with neurodegenerative diseases are toxic to cultured cells. We have shown recently that Aβ and -synuclein can both induce the formation of hydroxyl radicals following incubation in solution, upon the addition of Fe(II). Thus, they appear to generate hydrogen peroxide, which is converted to hydroxyl radicals via the Fenton reaction. Here we show that the widely studied toxic peptide fragment of the prion protein, PrP106–126, has exactly the same property, but only in the presence of copper ions. Since the aggregation and toxicity of PrP106–126 have been reported to be critically dependent on copper binding, our data suggest that the published cytotoxic effects of this peptide could also be due to its ability to generate hydrogen peroxide.

AB - Oligomeric forms of many of the aggregating proteins associated with neurodegenerative diseases are toxic to cultured cells. We have shown recently that Aβ and -synuclein can both induce the formation of hydroxyl radicals following incubation in solution, upon the addition of Fe(II). Thus, they appear to generate hydrogen peroxide, which is converted to hydroxyl radicals via the Fenton reaction. Here we show that the widely studied toxic peptide fragment of the prion protein, PrP106–126, has exactly the same property, but only in the presence of copper ions. Since the aggregation and toxicity of PrP106–126 have been reported to be critically dependent on copper binding, our data suggest that the published cytotoxic effects of this peptide could also be due to its ability to generate hydrogen peroxide.

KW - Copper

KW - Free radicals

KW - Hydrogen peroxide

KW - Oxidative stress

KW - Prion protein

U2 - 10.1016/S0304-3940(02)01254-5

DO - 10.1016/S0304-3940(02)01254-5

M3 - Journal article

VL - 336

SP - 159

EP - 162

JO - Neuroscience Letters

JF - Neuroscience Letters

SN - 0304-3940

IS - 3

ER -

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