The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease.

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The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease. / Galvagnion, C.

In: Journal of Parkinson's Disease, Vol. 7, No. 3, 2017, p. 433-450.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Galvagnion, C 2017, 'The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease.', Journal of Parkinson's Disease, vol. 7, no. 3, pp. 433-450. https://doi.org/10.3233/jpd-171103

APA

Galvagnion, C. (2017). The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease. Journal of Parkinson's Disease, 7(3), 433-450. https://doi.org/10.3233/jpd-171103

Vancouver

Galvagnion C. The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease. Journal of Parkinson's Disease. 2017;7(3):433-450. https://doi.org/10.3233/jpd-171103

Author

Galvagnion, C. / The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease. In: Journal of Parkinson's Disease. 2017 ; Vol. 7, No. 3. pp. 433-450.

Bibtex

@article{cc0740d91b57479f8d12b7be5fd24190,
title = "The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease.",
abstract = "α-synuclein is a small protein abundantly expressed in the brain and mainly located in synaptic terminals. The conversion of α-synuclein into oligomers and fibrils is the hallmark of a range of neurodegenerative disorders including Parkinson's disease and dementia with Lewy bodies. α-synuclein is disordered in solution but can adopt an α-helical conformation upon binding to lipid membranes. This lipid-protein interaction plays an important role in its proposed biological function, i.e., synaptic plasticity, but can also entail the aggregation of the protein. Both the chemical properties of the lipids and the lipid-to-protein-ratio have been reported to modulate the aggregation propensity of α-synuclein. In this review, the influence of changes in the nature and levels of lipids on the aggregation propensity of α-synuclein in vivo and in vitro will be discussed within a common general framework. In particular, while biophysical measurements and kinetic analyses of the time courses of α-synuclein aggregation in the presence of different types of lipid vesicles allow a mechanistic dissection of the influence of the lipids on α-synuclein aggregation, biological studies of cellular and animal models of Parkinson's disease allow the determination of changes in lipid levels and properties associated with the disease.",
author = "C Galvagnion",
year = "2017",
doi = "10.3233/jpd-171103",
language = "English",
volume = "7",
pages = "433--450",
journal = "Journal of Parkinson's Disease",
issn = "1877-7171",
publisher = "I O S Press",
number = "3",

}

RIS

TY - JOUR

T1 - The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson's Disease.

AU - Galvagnion, C

PY - 2017

Y1 - 2017

N2 - α-synuclein is a small protein abundantly expressed in the brain and mainly located in synaptic terminals. The conversion of α-synuclein into oligomers and fibrils is the hallmark of a range of neurodegenerative disorders including Parkinson's disease and dementia with Lewy bodies. α-synuclein is disordered in solution but can adopt an α-helical conformation upon binding to lipid membranes. This lipid-protein interaction plays an important role in its proposed biological function, i.e., synaptic plasticity, but can also entail the aggregation of the protein. Both the chemical properties of the lipids and the lipid-to-protein-ratio have been reported to modulate the aggregation propensity of α-synuclein. In this review, the influence of changes in the nature and levels of lipids on the aggregation propensity of α-synuclein in vivo and in vitro will be discussed within a common general framework. In particular, while biophysical measurements and kinetic analyses of the time courses of α-synuclein aggregation in the presence of different types of lipid vesicles allow a mechanistic dissection of the influence of the lipids on α-synuclein aggregation, biological studies of cellular and animal models of Parkinson's disease allow the determination of changes in lipid levels and properties associated with the disease.

AB - α-synuclein is a small protein abundantly expressed in the brain and mainly located in synaptic terminals. The conversion of α-synuclein into oligomers and fibrils is the hallmark of a range of neurodegenerative disorders including Parkinson's disease and dementia with Lewy bodies. α-synuclein is disordered in solution but can adopt an α-helical conformation upon binding to lipid membranes. This lipid-protein interaction plays an important role in its proposed biological function, i.e., synaptic plasticity, but can also entail the aggregation of the protein. Both the chemical properties of the lipids and the lipid-to-protein-ratio have been reported to modulate the aggregation propensity of α-synuclein. In this review, the influence of changes in the nature and levels of lipids on the aggregation propensity of α-synuclein in vivo and in vitro will be discussed within a common general framework. In particular, while biophysical measurements and kinetic analyses of the time courses of α-synuclein aggregation in the presence of different types of lipid vesicles allow a mechanistic dissection of the influence of the lipids on α-synuclein aggregation, biological studies of cellular and animal models of Parkinson's disease allow the determination of changes in lipid levels and properties associated with the disease.

UR - http://europepmc.org/abstract/med/28671142

U2 - 10.3233/jpd-171103

DO - 10.3233/jpd-171103

M3 - Journal article

C2 - 28671142

VL - 7

SP - 433

EP - 450

JO - Journal of Parkinson's Disease

JF - Journal of Parkinson's Disease

SN - 1877-7171

IS - 3

ER -

ID: 310383585