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