Lancaster EPrints

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

Salem, Sultan A and Allsop, David and Mann, David M A and Tokuda, Takahiko and El-Agnaf, Omar M A (2007) An investigation into the lipid-binding properties of α-, β- and γ-synucleins in human brain and cerebrospinal fluid. Experimental Brain Research, 1170. pp. 103-111.

Full text not available from this repository.

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.

Item Type: Article
Journal or Publication Title: Experimental Brain Research
Uncontrolled 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
Subjects: UNSPECIFIED
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
ID Code: 50813
Deposited By: ep_importer_pure
Deposited On: 07 Nov 2011 10:17
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 19:43
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/50813

Actions (login required)

View Item