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An investigation into the lipid-binding properties of α-, β- and γ-synucleins in human brain and cerebrospinal fluid

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An investigation into the lipid-binding properties of α-, β- and γ-synucleins in human brain and cerebrospinal fluid. / Salem, Sultan A; Allsop, David; Mann, David M A et al.
In: Experimental Brain Research, Vol. 1170, 19.09.2007, p. 103-111.

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Salem SA, Allsop D, Mann DMA, Tokuda T, El-Agnaf OMA. An investigation into the lipid-binding properties of α-, β- and γ-synucleins in human brain and cerebrospinal fluid. Experimental Brain Research. 2007 Sept 19;1170:103-111. doi: 10.1016/j.brainres.2007.07.027

Author

Salem, Sultan A ; Allsop, David ; Mann, David M A et al. / An investigation into the lipid-binding properties of α-, β- and γ-synucleins in human brain and cerebrospinal fluid. In: Experimental Brain Research. 2007 ; Vol. 1170. pp. 103-111.

Bibtex

@article{bcb86efaa5134a9686992fd5a28da38e,
title = "An investigation into the lipid-binding properties of α-, β- and γ-synucleins in human brain and cerebrospinal fluid",
abstract = "Parkinson's disease (PD) and dementia with Lewy bodies (DLB) are both characterized by the formation and intraneuronal accumulation of fibrillar aggregates of alpha-synuclein (alpha-syn) protein in affected brain regions. alpha-Syn has biochemical properties and a structural motif characteristic of fatty acid binding proteins. Using the fatty acid binding resin Lipidex-1000, we investigated the capture of alpha-, beta-, and gamma-syn proteins as lipid-associated proteins from normal and DLB brain lysates, and from normal human cerebrospinal fluid (CSF). These were eluted from Lipidex-1000 and analyzed by SDS-NuPAGE followed by Western blotting. Using this methodology, we have been able to extract full-length and truncated forms of alpha-syn from brain lysates. We also extracted low levels of beta-syn from DLB brains, but failed to extract any gamma-syn. We were able to capture only full-length monomeric alpha-syn from normal human CSF. Our data confirm the fatty acid binding properties of alpha-syn, and to a lesser extent beta-syn, but suggest that gamma-syn does not share this same characteristic.",
keywords = "Binding, Competitive, Brain, Brain Chemistry, Cerebrospinal Fluid, Dextrans, Electrophoresis, Polyacrylamide Gel, Humans, Lewy Body Disease, Membrane Lipids, Synucleins, alpha-Synuclein, beta-Synuclein, gamma-Synuclein",
author = "Salem, {Sultan A} and David Allsop and Mann, {David M A} and Takahiko Tokuda and El-Agnaf, {Omar M A}",
year = "2007",
month = sep,
day = "19",
doi = "10.1016/j.brainres.2007.07.027",
language = "English",
volume = "1170",
pages = "103--111",
journal = "Experimental Brain Research",
issn = "1432-1106",
publisher = "Springer Verlag",

}

RIS

TY - JOUR

T1 - An investigation into the lipid-binding properties of α-, β- and γ-synucleins in human brain and cerebrospinal fluid

AU - Salem, Sultan A

AU - Allsop, David

AU - Mann, David M A

AU - Tokuda, Takahiko

AU - El-Agnaf, Omar M A

PY - 2007/9/19

Y1 - 2007/9/19

N2 - Parkinson's disease (PD) and dementia with Lewy bodies (DLB) are both characterized by the formation and intraneuronal accumulation of fibrillar aggregates of alpha-synuclein (alpha-syn) protein in affected brain regions. alpha-Syn has biochemical properties and a structural motif characteristic of fatty acid binding proteins. Using the fatty acid binding resin Lipidex-1000, we investigated the capture of alpha-, beta-, and gamma-syn proteins as lipid-associated proteins from normal and DLB brain lysates, and from normal human cerebrospinal fluid (CSF). These were eluted from Lipidex-1000 and analyzed by SDS-NuPAGE followed by Western blotting. Using this methodology, we have been able to extract full-length and truncated forms of alpha-syn from brain lysates. We also extracted low levels of beta-syn from DLB brains, but failed to extract any gamma-syn. We were able to capture only full-length monomeric alpha-syn from normal human CSF. Our data confirm the fatty acid binding properties of alpha-syn, and to a lesser extent beta-syn, but suggest that gamma-syn does not share this same characteristic.

AB - Parkinson's disease (PD) and dementia with Lewy bodies (DLB) are both characterized by the formation and intraneuronal accumulation of fibrillar aggregates of alpha-synuclein (alpha-syn) protein in affected brain regions. alpha-Syn has biochemical properties and a structural motif characteristic of fatty acid binding proteins. Using the fatty acid binding resin Lipidex-1000, we investigated the capture of alpha-, beta-, and gamma-syn proteins as lipid-associated proteins from normal and DLB brain lysates, and from normal human cerebrospinal fluid (CSF). These were eluted from Lipidex-1000 and analyzed by SDS-NuPAGE followed by Western blotting. Using this methodology, we have been able to extract full-length and truncated forms of alpha-syn from brain lysates. We also extracted low levels of beta-syn from DLB brains, but failed to extract any gamma-syn. We were able to capture only full-length monomeric alpha-syn from normal human CSF. Our data confirm the fatty acid binding properties of alpha-syn, and to a lesser extent beta-syn, but suggest that gamma-syn does not share this same characteristic.

KW - Binding, Competitive

KW - Brain

KW - Brain Chemistry

KW - Cerebrospinal Fluid

KW - Dextrans

KW - Electrophoresis, Polyacrylamide Gel

KW - Humans

KW - Lewy Body Disease

KW - Membrane Lipids

KW - Synucleins

KW - alpha-Synuclein

KW - beta-Synuclein

KW - gamma-Synuclein

U2 - 10.1016/j.brainres.2007.07.027

DO - 10.1016/j.brainres.2007.07.027

M3 - Journal article

C2 - 17692832

VL - 1170

SP - 103

EP - 111

JO - Experimental Brain Research

JF - Experimental Brain Research

SN - 1432-1106

ER -