α-Synuclein expression is modulated at the translational level by iron

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α-Synuclein expression is modulated at the translational level by iron. / Febbraro, Fabia; Giorgi, Marcello; Caldarola, Sara; Loreni, Fabrizio; Romero-Ramos, Marina.

In: NeuroReport, Vol. 23, No. 9, 2012, p. 576-80.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Febbraro, F, Giorgi, M, Caldarola, S, Loreni, F & Romero-Ramos, M 2012, 'α-Synuclein expression is modulated at the translational level by iron', NeuroReport, vol. 23, no. 9, pp. 576-80. https://doi.org/10.1097/WNR.0b013e328354a1f0

APA

Febbraro, F., Giorgi, M., Caldarola, S., Loreni, F., & Romero-Ramos, M. (2012). α-Synuclein expression is modulated at the translational level by iron. NeuroReport, 23(9), 576-80. https://doi.org/10.1097/WNR.0b013e328354a1f0

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Febbraro, Fabia ; Giorgi, Marcello ; Caldarola, Sara ; Loreni, Fabrizio ; Romero-Ramos, Marina. / α-Synuclein expression is modulated at the translational level by iron. In: NeuroReport. 2012 ; Vol. 23, No. 9. pp. 576-80.

Bibtex

@article{791b1c46d344498a977e73ca92f3db35,
title = "α-Synuclein expression is modulated at the translational level by iron",
abstract = "Several studies have suggested an interaction between α-synuclein protein and iron in Parkinson's disease. The presence of iron together with α-synuclein in Lewy bodies, the increase of iron in the substantia nigra and the correlation between polymorphism of the several genes implicated in iron metabolism and Parkinson's disease, support a role for iron in the neurodegeneration. Analysis of post mortem brains revealed increased amount of insoluble α-synuclein protein despite unchanged/reduced levels of α-synuclein mRNA in Parkinson's disease. Interestingly, on the basis of the presence of a putative iron responsive element in the 5'-UTR, it has been suggested that there is a possible iron-dependent translational control of human α-synuclein mRNA. Considering the similarity between the sequences present in human α-synuclein mRNA and the ferritin iron responsive element, we postulated that iron deficiency would decrease the translation of α-synuclein mRNA. Here we used HEK293 cells treated with iron chelator deferoxamine or ferric ammonium citrate to verify the possible iron-dependent translational control of human α-synuclein biosynthesis. We show that the amount of polysome-associated endogenous human α-synuclein mRNA decreases in presence of deferoxamine. Our data demonstrate that human α-synuclein expression is regulated by iron mainly at the translational level. This result not only supports a role for iron in the translational control of α-synuclein expression, but also suggests that iron chelation may be a valid approach to control α-synuclein levels in the brain.",
author = "Fabia Febbraro and Marcello Giorgi and Sara Caldarola and Fabrizio Loreni and Marina Romero-Ramos",
year = "2012",
doi = "10.1097/WNR.0b013e328354a1f0",
language = "English",
volume = "23",
pages = "576--80",
journal = "NeuroReport",
issn = "0959-4965",
publisher = "LIPPINCOTT WILLIAMS & WILKINS",
number = "9",

}

RIS

TY - JOUR

T1 - α-Synuclein expression is modulated at the translational level by iron

AU - Febbraro, Fabia

AU - Giorgi, Marcello

AU - Caldarola, Sara

AU - Loreni, Fabrizio

AU - Romero-Ramos, Marina

PY - 2012

Y1 - 2012

N2 - Several studies have suggested an interaction between α-synuclein protein and iron in Parkinson's disease. The presence of iron together with α-synuclein in Lewy bodies, the increase of iron in the substantia nigra and the correlation between polymorphism of the several genes implicated in iron metabolism and Parkinson's disease, support a role for iron in the neurodegeneration. Analysis of post mortem brains revealed increased amount of insoluble α-synuclein protein despite unchanged/reduced levels of α-synuclein mRNA in Parkinson's disease. Interestingly, on the basis of the presence of a putative iron responsive element in the 5'-UTR, it has been suggested that there is a possible iron-dependent translational control of human α-synuclein mRNA. Considering the similarity between the sequences present in human α-synuclein mRNA and the ferritin iron responsive element, we postulated that iron deficiency would decrease the translation of α-synuclein mRNA. Here we used HEK293 cells treated with iron chelator deferoxamine or ferric ammonium citrate to verify the possible iron-dependent translational control of human α-synuclein biosynthesis. We show that the amount of polysome-associated endogenous human α-synuclein mRNA decreases in presence of deferoxamine. Our data demonstrate that human α-synuclein expression is regulated by iron mainly at the translational level. This result not only supports a role for iron in the translational control of α-synuclein expression, but also suggests that iron chelation may be a valid approach to control α-synuclein levels in the brain.

AB - Several studies have suggested an interaction between α-synuclein protein and iron in Parkinson's disease. The presence of iron together with α-synuclein in Lewy bodies, the increase of iron in the substantia nigra and the correlation between polymorphism of the several genes implicated in iron metabolism and Parkinson's disease, support a role for iron in the neurodegeneration. Analysis of post mortem brains revealed increased amount of insoluble α-synuclein protein despite unchanged/reduced levels of α-synuclein mRNA in Parkinson's disease. Interestingly, on the basis of the presence of a putative iron responsive element in the 5'-UTR, it has been suggested that there is a possible iron-dependent translational control of human α-synuclein mRNA. Considering the similarity between the sequences present in human α-synuclein mRNA and the ferritin iron responsive element, we postulated that iron deficiency would decrease the translation of α-synuclein mRNA. Here we used HEK293 cells treated with iron chelator deferoxamine or ferric ammonium citrate to verify the possible iron-dependent translational control of human α-synuclein biosynthesis. We show that the amount of polysome-associated endogenous human α-synuclein mRNA decreases in presence of deferoxamine. Our data demonstrate that human α-synuclein expression is regulated by iron mainly at the translational level. This result not only supports a role for iron in the translational control of α-synuclein expression, but also suggests that iron chelation may be a valid approach to control α-synuclein levels in the brain.

U2 - 10.1097/WNR.0b013e328354a1f0

DO - 10.1097/WNR.0b013e328354a1f0

M3 - Journal article

C2 - 22581044

VL - 23

SP - 576

EP - 580

JO - NeuroReport

JF - NeuroReport

SN - 0959-4965

IS - 9

ER -